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  • 92
    Millipore mia pa ca 2
    PF384 and PD901 in combination induces apoptosis in PDAC cell lines. a) BxPC-3, <t>MIA-Pa-Ca-2,</t> b) Panc-1 and Panc05.04 cells were treated as indicated for 24 hours after which fold-apoptosis was determined as caspase-3/7 activity normalised to MTT cell viability data. All data shown are the mean ± SEM for 3 independent experiments. *p ≤ 0.05, **p ≤ 0.01, ****p ≤ 0.0001, one-way ANOVA. CI
    Mia Pa Ca 2, supplied by Millipore, used in various techniques. Bioz Stars score: 92/100, based on 2 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Cell Signaling Technology Inc ca 2 induced ca2 release cicr mechanism
    PF384 and PD901 in combination induces apoptosis in PDAC cell lines. a) BxPC-3, <t>MIA-Pa-Ca-2,</t> b) Panc-1 and Panc05.04 cells were treated as indicated for 24 hours after which fold-apoptosis was determined as caspase-3/7 activity normalised to MTT cell viability data. All data shown are the mean ± SEM for 3 independent experiments. *p ≤ 0.05, **p ≤ 0.01, ****p ≤ 0.0001, one-way ANOVA. CI
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    85
    Millipore ca 2 ionophore
    PF384 and PD901 in combination induces apoptosis in PDAC cell lines. a) BxPC-3, <t>MIA-Pa-Ca-2,</t> b) Panc-1 and Panc05.04 cells were treated as indicated for 24 hours after which fold-apoptosis was determined as caspase-3/7 activity normalised to MTT cell viability data. All data shown are the mean ± SEM for 3 independent experiments. *p ≤ 0.05, **p ≤ 0.01, ****p ≤ 0.0001, one-way ANOVA. CI
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    93
    Cell Signaling Technology Inc ca2
    Dynamics of <t>Ca2+</t> concentrations on the network
    Ca2, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 93/100, based on 104 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    90
    Phenomenex rezex rcm monosaccharide ca 2
    Dynamics of <t>Ca2+</t> concentrations on the network
    Rezex Rcm Monosaccharide Ca 2, supplied by Phenomenex, used in various techniques. Bioz Stars score: 90/100, based on 16 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    85
    Thermo Fisher ca 2 sensor fluo 4
    Dynamics of <t>Ca2+</t> concentrations on the network
    Ca 2 Sensor Fluo 4, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 85/100, based on 18 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Nature Biotechnology endogenous ca 2
    Dynamics of <t>Ca2+</t> concentrations on the network
    Endogenous Ca 2, supplied by Nature Biotechnology, used in various techniques. Bioz Stars score: 92/100, based on 3 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Tosoh Corporation tskgel ca 2
    Dynamics of <t>Ca2+</t> concentrations on the network
    Tskgel Ca 2, supplied by Tosoh Corporation, used in various techniques. Bioz Stars score: 92/100, based on 4 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Fisher Scientific ca 2 mg2
    Dynamics of <t>Ca2+</t> concentrations on the network
    Ca 2 Mg2, supplied by Fisher Scientific, used in various techniques. Bioz Stars score: 85/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    92
    Thermo Fisher ca2
    Lack of homology among Slo3 sequences in the ligand-sensing cytosolic domain. ( A ) Alignments of human Slo1 and Slo3 from various species are shown for the membrane-associated, pore-forming part of the channels, indicating the relatively high extent of conservation through this part of the Slo3 protein. The Slo1 N-terminus is omitted to minimize effects of S0–S1 linker gaps on the alignment. Slo1 numbering starts from amino acids MDAL. Tick marks below each segment of residues counts every 10 residues in human Slo3. ( B ) Alignments of human Slo1 and Slo3 from various species are shown for the cytosolic gating ring domain beginning with the conserved sequence at the beginning of the first RCK domain. Blue highlights residue differences between human Slo1 and human Slo3. Yellow highlights differences of Slo3 of various species to human Slo3. Alignments were generated by Clustal 1.2.0 and minor adjustments were made based on structural considerations ( Leonetti et al., 2012 ). Above the residues, the correspondence of particular amino acid segments to structurally defined α-helical and β-strand segments is shown based on Leonetti et al. (2012) . In red, residues or segments identified in Slo1 or Slo3 isoforms which are implicated in ligand-sensing or species-specific functional differences are highlighted. Although extensive information is available regarding loci important in ligand-sensing in Slo1, such information for Slo3 remains lacking. Numbers identify the following: 1, the sequence of residues termed the Ca 2+ bowl ( Schreiber and Salkoff, 1997 ), for which there is good correspondence of mutations affecting <t>Ca2+-dependent</t> function ( Bao et al., 2004 ) and coordination of density in a crystal structure ( Yuan et al., 2012 ); 2, the D367 residue implicated in the role of the RCK1 domain in Ca 2+ -dependent activation ( Xia et al., 2002 ) which is clearly distinct from Ca 2+ -bowl dependent activation ( Zeng et al., 2005 ); 3, the M513 residue, which also affects Ca 2+− dependent activation involving the RCK1 domain ( Bao et al., 2002 ), but probably is not involved in ligand coordination; 4, residues E374 and E399 which have been implicated in low affinity effects of divalent cations, specifically Mg 2+ ( Shi et al., 2002 ; Xia et al., 2002 ; Yang et al., 2006 ); 5, residue E535 which may also be involved in Ca 2+ coordination in RCK1 ( Zhang et al., 2010 ); 6, residues H365 and H394, which have been implicated in proton-dependent activation of Slo1 and also influence Ca 2+ -dependent activation when protonated ( Hou et al., 2008 ); 7, H417 and segment 368–475, which influence pH-sensing in mouse Slo3 (Zhang et al., 2006); 8, segment 495–515 in bovine Slo3 which accounts for part of the different in functional properties between mouse Slo3 and bovine Slo3 ( Santi et al., 2009 ). Illustrated sequences and accession numbers include: HsSlo1 ( Homo sapiens ), NP_001154824, Gene ID 3778; HsSlo3 ( Homo sapiens ), NP_001027006, Gene ID 157855; MmSlo3 ( Mus musculus ), NP_032458, Gene ID 16532; RnSlo3 ( Rattus norvegicus ), XP_006253398, Gene ID 680912; TcSlo3 (Tupaia chinensis, Chinese tree shrew), XP_006171561, Gene ID 102493286; CcSlo3 ( Condylura cristata , star-nosed mole), XP_004682520, Gene ID 101620543; CfSlo3 (Canis lupus familiaris), XP_539971, Gene ID 482856; BtSlo3 (Bos taurus), NP_001156721, Gene ID 524144; OaSlo3 ( Ovis aries , sheep), XP_004021821, Gene ID 10110209. DOI: http://dx.doi.org/10.7554/eLife.01438.019
    Ca2, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 92/100, based on 5278 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    88
    Sanquin eggink ca 2
    Lack of homology among Slo3 sequences in the ligand-sensing cytosolic domain. ( A ) Alignments of human Slo1 and Slo3 from various species are shown for the membrane-associated, pore-forming part of the channels, indicating the relatively high extent of conservation through this part of the Slo3 protein. The Slo1 N-terminus is omitted to minimize effects of S0–S1 linker gaps on the alignment. Slo1 numbering starts from amino acids MDAL. Tick marks below each segment of residues counts every 10 residues in human Slo3. ( B ) Alignments of human Slo1 and Slo3 from various species are shown for the cytosolic gating ring domain beginning with the conserved sequence at the beginning of the first RCK domain. Blue highlights residue differences between human Slo1 and human Slo3. Yellow highlights differences of Slo3 of various species to human Slo3. Alignments were generated by Clustal 1.2.0 and minor adjustments were made based on structural considerations ( Leonetti et al., 2012 ). Above the residues, the correspondence of particular amino acid segments to structurally defined α-helical and β-strand segments is shown based on Leonetti et al. (2012) . In red, residues or segments identified in Slo1 or Slo3 isoforms which are implicated in ligand-sensing or species-specific functional differences are highlighted. Although extensive information is available regarding loci important in ligand-sensing in Slo1, such information for Slo3 remains lacking. Numbers identify the following: 1, the sequence of residues termed the Ca 2+ bowl ( Schreiber and Salkoff, 1997 ), for which there is good correspondence of mutations affecting <t>Ca2+-dependent</t> function ( Bao et al., 2004 ) and coordination of density in a crystal structure ( Yuan et al., 2012 ); 2, the D367 residue implicated in the role of the RCK1 domain in Ca 2+ -dependent activation ( Xia et al., 2002 ) which is clearly distinct from Ca 2+ -bowl dependent activation ( Zeng et al., 2005 ); 3, the M513 residue, which also affects Ca 2+− dependent activation involving the RCK1 domain ( Bao et al., 2002 ), but probably is not involved in ligand coordination; 4, residues E374 and E399 which have been implicated in low affinity effects of divalent cations, specifically Mg 2+ ( Shi et al., 2002 ; Xia et al., 2002 ; Yang et al., 2006 ); 5, residue E535 which may also be involved in Ca 2+ coordination in RCK1 ( Zhang et al., 2010 ); 6, residues H365 and H394, which have been implicated in proton-dependent activation of Slo1 and also influence Ca 2+ -dependent activation when protonated ( Hou et al., 2008 ); 7, H417 and segment 368–475, which influence pH-sensing in mouse Slo3 (Zhang et al., 2006); 8, segment 495–515 in bovine Slo3 which accounts for part of the different in functional properties between mouse Slo3 and bovine Slo3 ( Santi et al., 2009 ). Illustrated sequences and accession numbers include: HsSlo1 ( Homo sapiens ), NP_001154824, Gene ID 3778; HsSlo3 ( Homo sapiens ), NP_001027006, Gene ID 157855; MmSlo3 ( Mus musculus ), NP_032458, Gene ID 16532; RnSlo3 ( Rattus norvegicus ), XP_006253398, Gene ID 680912; TcSlo3 (Tupaia chinensis, Chinese tree shrew), XP_006171561, Gene ID 102493286; CcSlo3 ( Condylura cristata , star-nosed mole), XP_004682520, Gene ID 101620543; CfSlo3 (Canis lupus familiaris), XP_539971, Gene ID 482856; BtSlo3 (Bos taurus), NP_001156721, Gene ID 524144; OaSlo3 ( Ovis aries , sheep), XP_004021821, Gene ID 10110209. DOI: http://dx.doi.org/10.7554/eLife.01438.019
    Eggink Ca 2, supplied by Sanquin, used in various techniques. Bioz Stars score: 88/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    91
    Thermo Fisher hbss ca 2
    Lack of homology among Slo3 sequences in the ligand-sensing cytosolic domain. ( A ) Alignments of human Slo1 and Slo3 from various species are shown for the membrane-associated, pore-forming part of the channels, indicating the relatively high extent of conservation through this part of the Slo3 protein. The Slo1 N-terminus is omitted to minimize effects of S0–S1 linker gaps on the alignment. Slo1 numbering starts from amino acids MDAL. Tick marks below each segment of residues counts every 10 residues in human Slo3. ( B ) Alignments of human Slo1 and Slo3 from various species are shown for the cytosolic gating ring domain beginning with the conserved sequence at the beginning of the first RCK domain. Blue highlights residue differences between human Slo1 and human Slo3. Yellow highlights differences of Slo3 of various species to human Slo3. Alignments were generated by Clustal 1.2.0 and minor adjustments were made based on structural considerations ( Leonetti et al., 2012 ). Above the residues, the correspondence of particular amino acid segments to structurally defined α-helical and β-strand segments is shown based on Leonetti et al. (2012) . In red, residues or segments identified in Slo1 or Slo3 isoforms which are implicated in ligand-sensing or species-specific functional differences are highlighted. Although extensive information is available regarding loci important in ligand-sensing in Slo1, such information for Slo3 remains lacking. Numbers identify the following: 1, the sequence of residues termed the Ca 2+ bowl ( Schreiber and Salkoff, 1997 ), for which there is good correspondence of mutations affecting <t>Ca2+-dependent</t> function ( Bao et al., 2004 ) and coordination of density in a crystal structure ( Yuan et al., 2012 ); 2, the D367 residue implicated in the role of the RCK1 domain in Ca 2+ -dependent activation ( Xia et al., 2002 ) which is clearly distinct from Ca 2+ -bowl dependent activation ( Zeng et al., 2005 ); 3, the M513 residue, which also affects Ca 2+− dependent activation involving the RCK1 domain ( Bao et al., 2002 ), but probably is not involved in ligand coordination; 4, residues E374 and E399 which have been implicated in low affinity effects of divalent cations, specifically Mg 2+ ( Shi et al., 2002 ; Xia et al., 2002 ; Yang et al., 2006 ); 5, residue E535 which may also be involved in Ca 2+ coordination in RCK1 ( Zhang et al., 2010 ); 6, residues H365 and H394, which have been implicated in proton-dependent activation of Slo1 and also influence Ca 2+ -dependent activation when protonated ( Hou et al., 2008 ); 7, H417 and segment 368–475, which influence pH-sensing in mouse Slo3 (Zhang et al., 2006); 8, segment 495–515 in bovine Slo3 which accounts for part of the different in functional properties between mouse Slo3 and bovine Slo3 ( Santi et al., 2009 ). Illustrated sequences and accession numbers include: HsSlo1 ( Homo sapiens ), NP_001154824, Gene ID 3778; HsSlo3 ( Homo sapiens ), NP_001027006, Gene ID 157855; MmSlo3 ( Mus musculus ), NP_032458, Gene ID 16532; RnSlo3 ( Rattus norvegicus ), XP_006253398, Gene ID 680912; TcSlo3 (Tupaia chinensis, Chinese tree shrew), XP_006171561, Gene ID 102493286; CcSlo3 ( Condylura cristata , star-nosed mole), XP_004682520, Gene ID 101620543; CfSlo3 (Canis lupus familiaris), XP_539971, Gene ID 482856; BtSlo3 (Bos taurus), NP_001156721, Gene ID 524144; OaSlo3 ( Ovis aries , sheep), XP_004021821, Gene ID 10110209. DOI: http://dx.doi.org/10.7554/eLife.01438.019
    Hbss Ca 2, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 91/100, based on 14 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    93
    Cell Signaling Technology Inc anti ca2
    Lack of homology among Slo3 sequences in the ligand-sensing cytosolic domain. ( A ) Alignments of human Slo1 and Slo3 from various species are shown for the membrane-associated, pore-forming part of the channels, indicating the relatively high extent of conservation through this part of the Slo3 protein. The Slo1 N-terminus is omitted to minimize effects of S0–S1 linker gaps on the alignment. Slo1 numbering starts from amino acids MDAL. Tick marks below each segment of residues counts every 10 residues in human Slo3. ( B ) Alignments of human Slo1 and Slo3 from various species are shown for the cytosolic gating ring domain beginning with the conserved sequence at the beginning of the first RCK domain. Blue highlights residue differences between human Slo1 and human Slo3. Yellow highlights differences of Slo3 of various species to human Slo3. Alignments were generated by Clustal 1.2.0 and minor adjustments were made based on structural considerations ( Leonetti et al., 2012 ). Above the residues, the correspondence of particular amino acid segments to structurally defined α-helical and β-strand segments is shown based on Leonetti et al. (2012) . In red, residues or segments identified in Slo1 or Slo3 isoforms which are implicated in ligand-sensing or species-specific functional differences are highlighted. Although extensive information is available regarding loci important in ligand-sensing in Slo1, such information for Slo3 remains lacking. Numbers identify the following: 1, the sequence of residues termed the Ca 2+ bowl ( Schreiber and Salkoff, 1997 ), for which there is good correspondence of mutations affecting <t>Ca2+-dependent</t> function ( Bao et al., 2004 ) and coordination of density in a crystal structure ( Yuan et al., 2012 ); 2, the D367 residue implicated in the role of the RCK1 domain in Ca 2+ -dependent activation ( Xia et al., 2002 ) which is clearly distinct from Ca 2+ -bowl dependent activation ( Zeng et al., 2005 ); 3, the M513 residue, which also affects Ca 2+− dependent activation involving the RCK1 domain ( Bao et al., 2002 ), but probably is not involved in ligand coordination; 4, residues E374 and E399 which have been implicated in low affinity effects of divalent cations, specifically Mg 2+ ( Shi et al., 2002 ; Xia et al., 2002 ; Yang et al., 2006 ); 5, residue E535 which may also be involved in Ca 2+ coordination in RCK1 ( Zhang et al., 2010 ); 6, residues H365 and H394, which have been implicated in proton-dependent activation of Slo1 and also influence Ca 2+ -dependent activation when protonated ( Hou et al., 2008 ); 7, H417 and segment 368–475, which influence pH-sensing in mouse Slo3 (Zhang et al., 2006); 8, segment 495–515 in bovine Slo3 which accounts for part of the different in functional properties between mouse Slo3 and bovine Slo3 ( Santi et al., 2009 ). Illustrated sequences and accession numbers include: HsSlo1 ( Homo sapiens ), NP_001154824, Gene ID 3778; HsSlo3 ( Homo sapiens ), NP_001027006, Gene ID 157855; MmSlo3 ( Mus musculus ), NP_032458, Gene ID 16532; RnSlo3 ( Rattus norvegicus ), XP_006253398, Gene ID 680912; TcSlo3 (Tupaia chinensis, Chinese tree shrew), XP_006171561, Gene ID 102493286; CcSlo3 ( Condylura cristata , star-nosed mole), XP_004682520, Gene ID 101620543; CfSlo3 (Canis lupus familiaris), XP_539971, Gene ID 482856; BtSlo3 (Bos taurus), NP_001156721, Gene ID 524144; OaSlo3 ( Ovis aries , sheep), XP_004021821, Gene ID 10110209. DOI: http://dx.doi.org/10.7554/eLife.01438.019
    Anti Ca2, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 93/100, based on 26 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    92
    Cole-Parmer ca2 ion solution
    Lack of homology among Slo3 sequences in the ligand-sensing cytosolic domain. ( A ) Alignments of human Slo1 and Slo3 from various species are shown for the membrane-associated, pore-forming part of the channels, indicating the relatively high extent of conservation through this part of the Slo3 protein. The Slo1 N-terminus is omitted to minimize effects of S0–S1 linker gaps on the alignment. Slo1 numbering starts from amino acids MDAL. Tick marks below each segment of residues counts every 10 residues in human Slo3. ( B ) Alignments of human Slo1 and Slo3 from various species are shown for the cytosolic gating ring domain beginning with the conserved sequence at the beginning of the first RCK domain. Blue highlights residue differences between human Slo1 and human Slo3. Yellow highlights differences of Slo3 of various species to human Slo3. Alignments were generated by Clustal 1.2.0 and minor adjustments were made based on structural considerations ( Leonetti et al., 2012 ). Above the residues, the correspondence of particular amino acid segments to structurally defined α-helical and β-strand segments is shown based on Leonetti et al. (2012) . In red, residues or segments identified in Slo1 or Slo3 isoforms which are implicated in ligand-sensing or species-specific functional differences are highlighted. Although extensive information is available regarding loci important in ligand-sensing in Slo1, such information for Slo3 remains lacking. Numbers identify the following: 1, the sequence of residues termed the Ca 2+ bowl ( Schreiber and Salkoff, 1997 ), for which there is good correspondence of mutations affecting <t>Ca2+-dependent</t> function ( Bao et al., 2004 ) and coordination of density in a crystal structure ( Yuan et al., 2012 ); 2, the D367 residue implicated in the role of the RCK1 domain in Ca 2+ -dependent activation ( Xia et al., 2002 ) which is clearly distinct from Ca 2+ -bowl dependent activation ( Zeng et al., 2005 ); 3, the M513 residue, which also affects Ca 2+− dependent activation involving the RCK1 domain ( Bao et al., 2002 ), but probably is not involved in ligand coordination; 4, residues E374 and E399 which have been implicated in low affinity effects of divalent cations, specifically Mg 2+ ( Shi et al., 2002 ; Xia et al., 2002 ; Yang et al., 2006 ); 5, residue E535 which may also be involved in Ca 2+ coordination in RCK1 ( Zhang et al., 2010 ); 6, residues H365 and H394, which have been implicated in proton-dependent activation of Slo1 and also influence Ca 2+ -dependent activation when protonated ( Hou et al., 2008 ); 7, H417 and segment 368–475, which influence pH-sensing in mouse Slo3 (Zhang et al., 2006); 8, segment 495–515 in bovine Slo3 which accounts for part of the different in functional properties between mouse Slo3 and bovine Slo3 ( Santi et al., 2009 ). Illustrated sequences and accession numbers include: HsSlo1 ( Homo sapiens ), NP_001154824, Gene ID 3778; HsSlo3 ( Homo sapiens ), NP_001027006, Gene ID 157855; MmSlo3 ( Mus musculus ), NP_032458, Gene ID 16532; RnSlo3 ( Rattus norvegicus ), XP_006253398, Gene ID 680912; TcSlo3 (Tupaia chinensis, Chinese tree shrew), XP_006171561, Gene ID 102493286; CcSlo3 ( Condylura cristata , star-nosed mole), XP_004682520, Gene ID 101620543; CfSlo3 (Canis lupus familiaris), XP_539971, Gene ID 482856; BtSlo3 (Bos taurus), NP_001156721, Gene ID 524144; OaSlo3 ( Ovis aries , sheep), XP_004021821, Gene ID 10110209. DOI: http://dx.doi.org/10.7554/eLife.01438.019
    Ca2 Ion Solution, supplied by Cole-Parmer, used in various techniques. Bioz Stars score: 92/100, based on 4 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    85
    Draeger Safety a intracellular ca 2
    Lack of homology among Slo3 sequences in the ligand-sensing cytosolic domain. ( A ) Alignments of human Slo1 and Slo3 from various species are shown for the membrane-associated, pore-forming part of the channels, indicating the relatively high extent of conservation through this part of the Slo3 protein. The Slo1 N-terminus is omitted to minimize effects of S0–S1 linker gaps on the alignment. Slo1 numbering starts from amino acids MDAL. Tick marks below each segment of residues counts every 10 residues in human Slo3. ( B ) Alignments of human Slo1 and Slo3 from various species are shown for the cytosolic gating ring domain beginning with the conserved sequence at the beginning of the first RCK domain. Blue highlights residue differences between human Slo1 and human Slo3. Yellow highlights differences of Slo3 of various species to human Slo3. Alignments were generated by Clustal 1.2.0 and minor adjustments were made based on structural considerations ( Leonetti et al., 2012 ). Above the residues, the correspondence of particular amino acid segments to structurally defined α-helical and β-strand segments is shown based on Leonetti et al. (2012) . In red, residues or segments identified in Slo1 or Slo3 isoforms which are implicated in ligand-sensing or species-specific functional differences are highlighted. Although extensive information is available regarding loci important in ligand-sensing in Slo1, such information for Slo3 remains lacking. Numbers identify the following: 1, the sequence of residues termed the Ca 2+ bowl ( Schreiber and Salkoff, 1997 ), for which there is good correspondence of mutations affecting <t>Ca2+-dependent</t> function ( Bao et al., 2004 ) and coordination of density in a crystal structure ( Yuan et al., 2012 ); 2, the D367 residue implicated in the role of the RCK1 domain in Ca 2+ -dependent activation ( Xia et al., 2002 ) which is clearly distinct from Ca 2+ -bowl dependent activation ( Zeng et al., 2005 ); 3, the M513 residue, which also affects Ca 2+− dependent activation involving the RCK1 domain ( Bao et al., 2002 ), but probably is not involved in ligand coordination; 4, residues E374 and E399 which have been implicated in low affinity effects of divalent cations, specifically Mg 2+ ( Shi et al., 2002 ; Xia et al., 2002 ; Yang et al., 2006 ); 5, residue E535 which may also be involved in Ca 2+ coordination in RCK1 ( Zhang et al., 2010 ); 6, residues H365 and H394, which have been implicated in proton-dependent activation of Slo1 and also influence Ca 2+ -dependent activation when protonated ( Hou et al., 2008 ); 7, H417 and segment 368–475, which influence pH-sensing in mouse Slo3 (Zhang et al., 2006); 8, segment 495–515 in bovine Slo3 which accounts for part of the different in functional properties between mouse Slo3 and bovine Slo3 ( Santi et al., 2009 ). Illustrated sequences and accession numbers include: HsSlo1 ( Homo sapiens ), NP_001154824, Gene ID 3778; HsSlo3 ( Homo sapiens ), NP_001027006, Gene ID 157855; MmSlo3 ( Mus musculus ), NP_032458, Gene ID 16532; RnSlo3 ( Rattus norvegicus ), XP_006253398, Gene ID 680912; TcSlo3 (Tupaia chinensis, Chinese tree shrew), XP_006171561, Gene ID 102493286; CcSlo3 ( Condylura cristata , star-nosed mole), XP_004682520, Gene ID 101620543; CfSlo3 (Canis lupus familiaris), XP_539971, Gene ID 482856; BtSlo3 (Bos taurus), NP_001156721, Gene ID 524144; OaSlo3 ( Ovis aries , sheep), XP_004021821, Gene ID 10110209. DOI: http://dx.doi.org/10.7554/eLife.01438.019
    A Intracellular Ca 2, supplied by Draeger Safety, used in various techniques. Bioz Stars score: 85/100, based on 10 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Millipore ca 2÷ ionophore a23187
    Lack of homology among Slo3 sequences in the ligand-sensing cytosolic domain. ( A ) Alignments of human Slo1 and Slo3 from various species are shown for the membrane-associated, pore-forming part of the channels, indicating the relatively high extent of conservation through this part of the Slo3 protein. The Slo1 N-terminus is omitted to minimize effects of S0–S1 linker gaps on the alignment. Slo1 numbering starts from amino acids MDAL. Tick marks below each segment of residues counts every 10 residues in human Slo3. ( B ) Alignments of human Slo1 and Slo3 from various species are shown for the cytosolic gating ring domain beginning with the conserved sequence at the beginning of the first RCK domain. Blue highlights residue differences between human Slo1 and human Slo3. Yellow highlights differences of Slo3 of various species to human Slo3. Alignments were generated by Clustal 1.2.0 and minor adjustments were made based on structural considerations ( Leonetti et al., 2012 ). Above the residues, the correspondence of particular amino acid segments to structurally defined α-helical and β-strand segments is shown based on Leonetti et al. (2012) . In red, residues or segments identified in Slo1 or Slo3 isoforms which are implicated in ligand-sensing or species-specific functional differences are highlighted. Although extensive information is available regarding loci important in ligand-sensing in Slo1, such information for Slo3 remains lacking. Numbers identify the following: 1, the sequence of residues termed the Ca 2+ bowl ( Schreiber and Salkoff, 1997 ), for which there is good correspondence of mutations affecting <t>Ca2+-dependent</t> function ( Bao et al., 2004 ) and coordination of density in a crystal structure ( Yuan et al., 2012 ); 2, the D367 residue implicated in the role of the RCK1 domain in Ca 2+ -dependent activation ( Xia et al., 2002 ) which is clearly distinct from Ca 2+ -bowl dependent activation ( Zeng et al., 2005 ); 3, the M513 residue, which also affects Ca 2+− dependent activation involving the RCK1 domain ( Bao et al., 2002 ), but probably is not involved in ligand coordination; 4, residues E374 and E399 which have been implicated in low affinity effects of divalent cations, specifically Mg 2+ ( Shi et al., 2002 ; Xia et al., 2002 ; Yang et al., 2006 ); 5, residue E535 which may also be involved in Ca 2+ coordination in RCK1 ( Zhang et al., 2010 ); 6, residues H365 and H394, which have been implicated in proton-dependent activation of Slo1 and also influence Ca 2+ -dependent activation when protonated ( Hou et al., 2008 ); 7, H417 and segment 368–475, which influence pH-sensing in mouse Slo3 (Zhang et al., 2006); 8, segment 495–515 in bovine Slo3 which accounts for part of the different in functional properties between mouse Slo3 and bovine Slo3 ( Santi et al., 2009 ). Illustrated sequences and accession numbers include: HsSlo1 ( Homo sapiens ), NP_001154824, Gene ID 3778; HsSlo3 ( Homo sapiens ), NP_001027006, Gene ID 157855; MmSlo3 ( Mus musculus ), NP_032458, Gene ID 16532; RnSlo3 ( Rattus norvegicus ), XP_006253398, Gene ID 680912; TcSlo3 (Tupaia chinensis, Chinese tree shrew), XP_006171561, Gene ID 102493286; CcSlo3 ( Condylura cristata , star-nosed mole), XP_004682520, Gene ID 101620543; CfSlo3 (Canis lupus familiaris), XP_539971, Gene ID 482856; BtSlo3 (Bos taurus), NP_001156721, Gene ID 524144; OaSlo3 ( Ovis aries , sheep), XP_004021821, Gene ID 10110209. DOI: http://dx.doi.org/10.7554/eLife.01438.019
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    Novoprotein ca 2 dependent mechanism
    Lack of homology among Slo3 sequences in the ligand-sensing cytosolic domain. ( A ) Alignments of human Slo1 and Slo3 from various species are shown for the membrane-associated, pore-forming part of the channels, indicating the relatively high extent of conservation through this part of the Slo3 protein. The Slo1 N-terminus is omitted to minimize effects of S0–S1 linker gaps on the alignment. Slo1 numbering starts from amino acids MDAL. Tick marks below each segment of residues counts every 10 residues in human Slo3. ( B ) Alignments of human Slo1 and Slo3 from various species are shown for the cytosolic gating ring domain beginning with the conserved sequence at the beginning of the first RCK domain. Blue highlights residue differences between human Slo1 and human Slo3. Yellow highlights differences of Slo3 of various species to human Slo3. Alignments were generated by Clustal 1.2.0 and minor adjustments were made based on structural considerations ( Leonetti et al., 2012 ). Above the residues, the correspondence of particular amino acid segments to structurally defined α-helical and β-strand segments is shown based on Leonetti et al. (2012) . In red, residues or segments identified in Slo1 or Slo3 isoforms which are implicated in ligand-sensing or species-specific functional differences are highlighted. Although extensive information is available regarding loci important in ligand-sensing in Slo1, such information for Slo3 remains lacking. Numbers identify the following: 1, the sequence of residues termed the Ca 2+ bowl ( Schreiber and Salkoff, 1997 ), for which there is good correspondence of mutations affecting <t>Ca2+-dependent</t> function ( Bao et al., 2004 ) and coordination of density in a crystal structure ( Yuan et al., 2012 ); 2, the D367 residue implicated in the role of the RCK1 domain in Ca 2+ -dependent activation ( Xia et al., 2002 ) which is clearly distinct from Ca 2+ -bowl dependent activation ( Zeng et al., 2005 ); 3, the M513 residue, which also affects Ca 2+− dependent activation involving the RCK1 domain ( Bao et al., 2002 ), but probably is not involved in ligand coordination; 4, residues E374 and E399 which have been implicated in low affinity effects of divalent cations, specifically Mg 2+ ( Shi et al., 2002 ; Xia et al., 2002 ; Yang et al., 2006 ); 5, residue E535 which may also be involved in Ca 2+ coordination in RCK1 ( Zhang et al., 2010 ); 6, residues H365 and H394, which have been implicated in proton-dependent activation of Slo1 and also influence Ca 2+ -dependent activation when protonated ( Hou et al., 2008 ); 7, H417 and segment 368–475, which influence pH-sensing in mouse Slo3 (Zhang et al., 2006); 8, segment 495–515 in bovine Slo3 which accounts for part of the different in functional properties between mouse Slo3 and bovine Slo3 ( Santi et al., 2009 ). Illustrated sequences and accession numbers include: HsSlo1 ( Homo sapiens ), NP_001154824, Gene ID 3778; HsSlo3 ( Homo sapiens ), NP_001027006, Gene ID 157855; MmSlo3 ( Mus musculus ), NP_032458, Gene ID 16532; RnSlo3 ( Rattus norvegicus ), XP_006253398, Gene ID 680912; TcSlo3 (Tupaia chinensis, Chinese tree shrew), XP_006171561, Gene ID 102493286; CcSlo3 ( Condylura cristata , star-nosed mole), XP_004682520, Gene ID 101620543; CfSlo3 (Canis lupus familiaris), XP_539971, Gene ID 482856; BtSlo3 (Bos taurus), NP_001156721, Gene ID 524144; OaSlo3 ( Ovis aries , sheep), XP_004021821, Gene ID 10110209. DOI: http://dx.doi.org/10.7554/eLife.01438.019
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    Cytoskeleton Inc ca 2 dependent translocation
    Lack of homology among Slo3 sequences in the ligand-sensing cytosolic domain. ( A ) Alignments of human Slo1 and Slo3 from various species are shown for the membrane-associated, pore-forming part of the channels, indicating the relatively high extent of conservation through this part of the Slo3 protein. The Slo1 N-terminus is omitted to minimize effects of S0–S1 linker gaps on the alignment. Slo1 numbering starts from amino acids MDAL. Tick marks below each segment of residues counts every 10 residues in human Slo3. ( B ) Alignments of human Slo1 and Slo3 from various species are shown for the cytosolic gating ring domain beginning with the conserved sequence at the beginning of the first RCK domain. Blue highlights residue differences between human Slo1 and human Slo3. Yellow highlights differences of Slo3 of various species to human Slo3. Alignments were generated by Clustal 1.2.0 and minor adjustments were made based on structural considerations ( Leonetti et al., 2012 ). Above the residues, the correspondence of particular amino acid segments to structurally defined α-helical and β-strand segments is shown based on Leonetti et al. (2012) . In red, residues or segments identified in Slo1 or Slo3 isoforms which are implicated in ligand-sensing or species-specific functional differences are highlighted. Although extensive information is available regarding loci important in ligand-sensing in Slo1, such information for Slo3 remains lacking. Numbers identify the following: 1, the sequence of residues termed the Ca 2+ bowl ( Schreiber and Salkoff, 1997 ), for which there is good correspondence of mutations affecting <t>Ca2+-dependent</t> function ( Bao et al., 2004 ) and coordination of density in a crystal structure ( Yuan et al., 2012 ); 2, the D367 residue implicated in the role of the RCK1 domain in Ca 2+ -dependent activation ( Xia et al., 2002 ) which is clearly distinct from Ca 2+ -bowl dependent activation ( Zeng et al., 2005 ); 3, the M513 residue, which also affects Ca 2+− dependent activation involving the RCK1 domain ( Bao et al., 2002 ), but probably is not involved in ligand coordination; 4, residues E374 and E399 which have been implicated in low affinity effects of divalent cations, specifically Mg 2+ ( Shi et al., 2002 ; Xia et al., 2002 ; Yang et al., 2006 ); 5, residue E535 which may also be involved in Ca 2+ coordination in RCK1 ( Zhang et al., 2010 ); 6, residues H365 and H394, which have been implicated in proton-dependent activation of Slo1 and also influence Ca 2+ -dependent activation when protonated ( Hou et al., 2008 ); 7, H417 and segment 368–475, which influence pH-sensing in mouse Slo3 (Zhang et al., 2006); 8, segment 495–515 in bovine Slo3 which accounts for part of the different in functional properties between mouse Slo3 and bovine Slo3 ( Santi et al., 2009 ). Illustrated sequences and accession numbers include: HsSlo1 ( Homo sapiens ), NP_001154824, Gene ID 3778; HsSlo3 ( Homo sapiens ), NP_001027006, Gene ID 157855; MmSlo3 ( Mus musculus ), NP_032458, Gene ID 16532; RnSlo3 ( Rattus norvegicus ), XP_006253398, Gene ID 680912; TcSlo3 (Tupaia chinensis, Chinese tree shrew), XP_006171561, Gene ID 102493286; CcSlo3 ( Condylura cristata , star-nosed mole), XP_004682520, Gene ID 101620543; CfSlo3 (Canis lupus familiaris), XP_539971, Gene ID 482856; BtSlo3 (Bos taurus), NP_001156721, Gene ID 524144; OaSlo3 ( Ovis aries , sheep), XP_004021821, Gene ID 10110209. DOI: http://dx.doi.org/10.7554/eLife.01438.019
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    Cayman Chemical piezo1 ca 2
    Lack of homology among Slo3 sequences in the ligand-sensing cytosolic domain. ( A ) Alignments of human Slo1 and Slo3 from various species are shown for the membrane-associated, pore-forming part of the channels, indicating the relatively high extent of conservation through this part of the Slo3 protein. The Slo1 N-terminus is omitted to minimize effects of S0–S1 linker gaps on the alignment. Slo1 numbering starts from amino acids MDAL. Tick marks below each segment of residues counts every 10 residues in human Slo3. ( B ) Alignments of human Slo1 and Slo3 from various species are shown for the cytosolic gating ring domain beginning with the conserved sequence at the beginning of the first RCK domain. Blue highlights residue differences between human Slo1 and human Slo3. Yellow highlights differences of Slo3 of various species to human Slo3. Alignments were generated by Clustal 1.2.0 and minor adjustments were made based on structural considerations ( Leonetti et al., 2012 ). Above the residues, the correspondence of particular amino acid segments to structurally defined α-helical and β-strand segments is shown based on Leonetti et al. (2012) . In red, residues or segments identified in Slo1 or Slo3 isoforms which are implicated in ligand-sensing or species-specific functional differences are highlighted. Although extensive information is available regarding loci important in ligand-sensing in Slo1, such information for Slo3 remains lacking. Numbers identify the following: 1, the sequence of residues termed the Ca 2+ bowl ( Schreiber and Salkoff, 1997 ), for which there is good correspondence of mutations affecting <t>Ca2+-dependent</t> function ( Bao et al., 2004 ) and coordination of density in a crystal structure ( Yuan et al., 2012 ); 2, the D367 residue implicated in the role of the RCK1 domain in Ca 2+ -dependent activation ( Xia et al., 2002 ) which is clearly distinct from Ca 2+ -bowl dependent activation ( Zeng et al., 2005 ); 3, the M513 residue, which also affects Ca 2+− dependent activation involving the RCK1 domain ( Bao et al., 2002 ), but probably is not involved in ligand coordination; 4, residues E374 and E399 which have been implicated in low affinity effects of divalent cations, specifically Mg 2+ ( Shi et al., 2002 ; Xia et al., 2002 ; Yang et al., 2006 ); 5, residue E535 which may also be involved in Ca 2+ coordination in RCK1 ( Zhang et al., 2010 ); 6, residues H365 and H394, which have been implicated in proton-dependent activation of Slo1 and also influence Ca 2+ -dependent activation when protonated ( Hou et al., 2008 ); 7, H417 and segment 368–475, which influence pH-sensing in mouse Slo3 (Zhang et al., 2006); 8, segment 495–515 in bovine Slo3 which accounts for part of the different in functional properties between mouse Slo3 and bovine Slo3 ( Santi et al., 2009 ). Illustrated sequences and accession numbers include: HsSlo1 ( Homo sapiens ), NP_001154824, Gene ID 3778; HsSlo3 ( Homo sapiens ), NP_001027006, Gene ID 157855; MmSlo3 ( Mus musculus ), NP_032458, Gene ID 16532; RnSlo3 ( Rattus norvegicus ), XP_006253398, Gene ID 680912; TcSlo3 (Tupaia chinensis, Chinese tree shrew), XP_006171561, Gene ID 102493286; CcSlo3 ( Condylura cristata , star-nosed mole), XP_004682520, Gene ID 101620543; CfSlo3 (Canis lupus familiaris), XP_539971, Gene ID 482856; BtSlo3 (Bos taurus), NP_001156721, Gene ID 524144; OaSlo3 ( Ovis aries , sheep), XP_004021821, Gene ID 10110209. DOI: http://dx.doi.org/10.7554/eLife.01438.019
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    Effect of NaHS on <t>[Ca2+]</t> i in cultured gastric fundus smooth muscles. Aa: The time-dependent effects of different concentrations of NaHS on [Ca2+] i . Ab: Summary graph showing the effects of the NaHS-induced increase in intracellular calcium; Ba: Raw traces
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    Effect of NaHS on <t>[Ca2+]</t> i in cultured gastric fundus smooth muscles. Aa: The time-dependent effects of different concentrations of NaHS on [Ca2+] i . Ab: Summary graph showing the effects of the NaHS-induced increase in intracellular calcium; Ba: Raw traces
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    Effect of NaHS on <t>[Ca2+]</t> i in cultured gastric fundus smooth muscles. Aa: The time-dependent effects of different concentrations of NaHS on [Ca2+] i . Ab: Summary graph showing the effects of the NaHS-induced increase in intracellular calcium; Ba: Raw traces
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    Effect of NaHS on <t>[Ca2+]</t> i in cultured gastric fundus smooth muscles. Aa: The time-dependent effects of different concentrations of NaHS on [Ca2+] i . Ab: Summary graph showing the effects of the NaHS-induced increase in intracellular calcium; Ba: Raw traces
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    Image Search Results


    PF384 and PD901 in combination induces apoptosis in PDAC cell lines. a) BxPC-3, MIA-Pa-Ca-2, b) Panc-1 and Panc05.04 cells were treated as indicated for 24 hours after which fold-apoptosis was determined as caspase-3/7 activity normalised to MTT cell viability data. All data shown are the mean ± SEM for 3 independent experiments. *p ≤ 0.05, **p ≤ 0.01, ****p ≤ 0.0001, one-way ANOVA. CI

    Journal: Cancer Biology & Therapy

    Article Title: Combined inhibition of the PI3K/mTOR/MEK pathway induces Bim/Mcl-1-regulated apoptosis in pancreatic cancer cells

    doi: 10.1080/15384047.2018.1504718

    Figure Lengend Snippet: PF384 and PD901 in combination induces apoptosis in PDAC cell lines. a) BxPC-3, MIA-Pa-Ca-2, b) Panc-1 and Panc05.04 cells were treated as indicated for 24 hours after which fold-apoptosis was determined as caspase-3/7 activity normalised to MTT cell viability data. All data shown are the mean ± SEM for 3 independent experiments. *p ≤ 0.05, **p ≤ 0.01, ****p ≤ 0.0001, one-way ANOVA. CI

    Article Snippet: BxPC-3 and PEA2 cells were maintained in RPMI-1640 (Sigma, R5886), and Mia-Pa-Ca-2 and Panc-1 in DMEM (Sigma, D5546), supplemented with 10% fetal calf serum (First Link UK, 02–00–850), 2 mM L-glutamine (Thermo Fisher, 25030–024) and penicillin/streptomycin (50 units/ml and 50 μg/ml respectively; Thermo Fisher, 15070–063).

    Techniques: Activity Assay, MTT Assay

    PF384 and PD901 effectively target PI3K and MEK signalling pathways and enhance apoptotic induction when combined. BxPC-3 and MIA-Pa-Ca-2 cells were treated as indicated for 6 hours after which whole cell lysates were processed for a) RPPA analysis, and normalised Log2 median-centred values used to calculate relative expression of PI3K/mTOR/MEK signalling pathway components and b) fold-apoptosis was determined as caspase-3/7 activity normalised to MTT cell viability data. All data shown are the mean ± standard error of the mean (SEM) for 3 independent experiments. *p ≤ 0.05, ****p ≤ 0.0001, one-way ANOVA. CI

    Journal: Cancer Biology & Therapy

    Article Title: Combined inhibition of the PI3K/mTOR/MEK pathway induces Bim/Mcl-1-regulated apoptosis in pancreatic cancer cells

    doi: 10.1080/15384047.2018.1504718

    Figure Lengend Snippet: PF384 and PD901 effectively target PI3K and MEK signalling pathways and enhance apoptotic induction when combined. BxPC-3 and MIA-Pa-Ca-2 cells were treated as indicated for 6 hours after which whole cell lysates were processed for a) RPPA analysis, and normalised Log2 median-centred values used to calculate relative expression of PI3K/mTOR/MEK signalling pathway components and b) fold-apoptosis was determined as caspase-3/7 activity normalised to MTT cell viability data. All data shown are the mean ± standard error of the mean (SEM) for 3 independent experiments. *p ≤ 0.05, ****p ≤ 0.0001, one-way ANOVA. CI

    Article Snippet: BxPC-3 and PEA2 cells were maintained in RPMI-1640 (Sigma, R5886), and Mia-Pa-Ca-2 and Panc-1 in DMEM (Sigma, D5546), supplemented with 10% fetal calf serum (First Link UK, 02–00–850), 2 mM L-glutamine (Thermo Fisher, 25030–024) and penicillin/streptomycin (50 units/ml and 50 μg/ml respectively; Thermo Fisher, 15070–063).

    Techniques: Expressing, Activity Assay, MTT Assay

    PF384 induces G1/G0 cell cycle arrest and decreases cell viability in a non-caspase dependent manner in association with the induction of autophagy. a) BxPC-3 and MIA-Pa-Ca-2 cells were treated as indicated for 24 hours after which they were labelled with propidium iodide and the percentage of cells in each stage of the cell cycle determined by flow cytometry. b ) Cells were treated as indicated for 6 hours after which cell viability was determined by MTT assay. Where z.VAD.fmk (100 μM) was used, cells were pre-incubated with this for 1 hour before the addition of other drugs. c) Cells were treated as indicated for 24 hours after which whole cell lysates were assessed for expression of LC3A/B and β-tubulin by western blotting. All data shown are the mean ± SEM for 3 independent experiments. Blots are representative of two biological repeats.

    Journal: Cancer Biology & Therapy

    Article Title: Combined inhibition of the PI3K/mTOR/MEK pathway induces Bim/Mcl-1-regulated apoptosis in pancreatic cancer cells

    doi: 10.1080/15384047.2018.1504718

    Figure Lengend Snippet: PF384 induces G1/G0 cell cycle arrest and decreases cell viability in a non-caspase dependent manner in association with the induction of autophagy. a) BxPC-3 and MIA-Pa-Ca-2 cells were treated as indicated for 24 hours after which they were labelled with propidium iodide and the percentage of cells in each stage of the cell cycle determined by flow cytometry. b ) Cells were treated as indicated for 6 hours after which cell viability was determined by MTT assay. Where z.VAD.fmk (100 μM) was used, cells were pre-incubated with this for 1 hour before the addition of other drugs. c) Cells were treated as indicated for 24 hours after which whole cell lysates were assessed for expression of LC3A/B and β-tubulin by western blotting. All data shown are the mean ± SEM for 3 independent experiments. Blots are representative of two biological repeats.

    Article Snippet: BxPC-3 and PEA2 cells were maintained in RPMI-1640 (Sigma, R5886), and Mia-Pa-Ca-2 and Panc-1 in DMEM (Sigma, D5546), supplemented with 10% fetal calf serum (First Link UK, 02–00–850), 2 mM L-glutamine (Thermo Fisher, 25030–024) and penicillin/streptomycin (50 units/ml and 50 μg/ml respectively; Thermo Fisher, 15070–063).

    Techniques: Flow Cytometry, Cytometry, MTT Assay, Incubation, Expressing, Western Blot

    Dynamics of Ca2+ concentrations on the network

    Journal: PLoS Computational Biology

    Article Title: The Effect of Gap Junctional Coupling on the Spatiotemporal Patterns of Ca2+ Signals and the Harmonization of Ca2+-Related Cellular Responses

    doi: 10.1371/journal.pcbi.1005295

    Figure Lengend Snippet: Dynamics of Ca2+ concentrations on the network

    Article Snippet: Maintaining the low concentrations of Ca2+ in the cytoplasm against a 10,000-fold higher extracellular Ca2+ concentration, i.e. the strong trans-membrane electrochemical gradient of Ca2+ ions needed for proper cell signaling [ ] requires energy.

    Techniques:

    Effect of the gap junctional coupling (d ) on Ca2+ waves in the noise-free models G D

    Journal: PLoS Computational Biology

    Article Title: The Effect of Gap Junctional Coupling on the Spatiotemporal Patterns of Ca2+ Signals and the Harmonization of Ca2+-Related Cellular Responses

    doi: 10.1371/journal.pcbi.1005295

    Figure Lengend Snippet: Effect of the gap junctional coupling (d ) on Ca2+ waves in the noise-free models G D

    Article Snippet: Maintaining the low concentrations of Ca2+ in the cytoplasm against a 10,000-fold higher extracellular Ca2+ concentration, i.e. the strong trans-membrane electrochemical gradient of Ca2+ ions needed for proper cell signaling [ ] requires energy.

    Techniques:

    Effect of the gap junctional coupling (d ) on Ca2+ waves in the noise-free models G D

    Journal: PLoS Computational Biology

    Article Title: The Effect of Gap Junctional Coupling on the Spatiotemporal Patterns of Ca2+ Signals and the Harmonization of Ca2+-Related Cellular Responses

    doi: 10.1371/journal.pcbi.1005295

    Figure Lengend Snippet: Effect of the gap junctional coupling (d ) on Ca2+ waves in the noise-free models G D

    Article Snippet: Maintaining the low concentrations of Ca2+ in the cytoplasm against a 10,000-fold higher extracellular Ca2+ concentration, i.e. the strong trans-membrane electrochemical gradient of Ca2+ ions needed for proper cell signaling [ ] requires energy.

    Techniques:

    Dynamics of Ca2+ concentrations on the network

    Journal: PLoS Computational Biology

    Article Title: The Effect of Gap Junctional Coupling on the Spatiotemporal Patterns of Ca2+ Signals and the Harmonization of Ca2+-Related Cellular Responses

    doi: 10.1371/journal.pcbi.1005295

    Figure Lengend Snippet: Dynamics of Ca2+ concentrations on the network

    Article Snippet: Maintaining the low concentrations of Ca2+ in the cytoplasm against a 10,000-fold higher extracellular Ca2+ concentration, i.e. the strong trans-membrane electrochemical gradient of Ca2+ ions needed for proper cell signaling [ ] requires energy.

    Techniques:

    Dynamics of Ca2+ concentrations on the network

    Journal: PLoS Computational Biology

    Article Title: The Effect of Gap Junctional Coupling on the Spatiotemporal Patterns of Ca2+ Signals and the Harmonization of Ca2+-Related Cellular Responses

    doi: 10.1371/journal.pcbi.1005295

    Figure Lengend Snippet: Dynamics of Ca2+ concentrations on the network

    Article Snippet: Maintaining the low concentrations of Ca2+ in the cytoplasm against a 10,000-fold higher extracellular Ca2+ concentration, i.e. the strong trans-membrane electrochemical gradient of Ca2+ ions needed for proper cell signaling [ ] requires energy.

    Techniques:

    Supporting Information Circular waves in a noise-free model emerge from highly sensitive cells. Simultaneous changes in ccyt (left panel) and cER (right panel) have been shown. Non-self-oscillating cells synchronize with their oscillating neighbors and produces spiral waves. Independent evolution of the cytoplasmic Ca2+ concentrations ccyt without gap junctional coupling (d = 0) in the random model. Bursting phenomena with moderate gap junctional coupling in the random model. Rapid synchronization with high gap junctional coupling in the random model and appearance of spiraling phenomena. Wave propagation in the random model in a highly linked graph. Wave propagation in the random model in a poorly linked graph. Wave propagation in the random model with holes. Appearance of spirals in a noise-free model with three highly sensitive zones. Appearance of spirals in a noise-free model with two highly sensitive zones. A sensitive random model with low noise evokes spirals. A sensitive random model with low noise and an additional sensitive central zone produces concentric circular waves. Setting one parameter above the “physiological” limit in the random model with low noise results in non-organized wave propagation and spirals. Wave propagation in the random model with Ca2+ coupling and no InsP3 coupling. Wave propagation in the random model with InsP3 coupling and no Ca2+ coupling. Wave propagation in the random model with InsP3 coupling and Ca2+ coupling. Wave propagation in the deterministic model with CR. Adjunction of CR in the random model helps synchronization.

    Journal: PLoS Computational Biology

    Article Title: The Effect of Gap Junctional Coupling on the Spatiotemporal Patterns of Ca2+ Signals and the Harmonization of Ca2+-Related Cellular Responses

    doi: 10.1371/journal.pcbi.1005295

    Figure Lengend Snippet: Supporting Information Circular waves in a noise-free model emerge from highly sensitive cells. Simultaneous changes in ccyt (left panel) and cER (right panel) have been shown. Non-self-oscillating cells synchronize with their oscillating neighbors and produces spiral waves. Independent evolution of the cytoplasmic Ca2+ concentrations ccyt without gap junctional coupling (d = 0) in the random model. Bursting phenomena with moderate gap junctional coupling in the random model. Rapid synchronization with high gap junctional coupling in the random model and appearance of spiraling phenomena. Wave propagation in the random model in a highly linked graph. Wave propagation in the random model in a poorly linked graph. Wave propagation in the random model with holes. Appearance of spirals in a noise-free model with three highly sensitive zones. Appearance of spirals in a noise-free model with two highly sensitive zones. A sensitive random model with low noise evokes spirals. A sensitive random model with low noise and an additional sensitive central zone produces concentric circular waves. Setting one parameter above the “physiological” limit in the random model with low noise results in non-organized wave propagation and spirals. Wave propagation in the random model with Ca2+ coupling and no InsP3 coupling. Wave propagation in the random model with InsP3 coupling and no Ca2+ coupling. Wave propagation in the random model with InsP3 coupling and Ca2+ coupling. Wave propagation in the deterministic model with CR. Adjunction of CR in the random model helps synchronization.

    Article Snippet: Maintaining the low concentrations of Ca2+ in the cytoplasm against a 10,000-fold higher extracellular Ca2+ concentration, i.e. the strong trans-membrane electrochemical gradient of Ca2+ ions needed for proper cell signaling [ ] requires energy.

    Techniques:

    Dynamics of Ca2+ concentrations on the network

    Journal: PLoS Computational Biology

    Article Title: The Effect of Gap Junctional Coupling on the Spatiotemporal Patterns of Ca2+ Signals and the Harmonization of Ca2+-Related Cellular Responses

    doi: 10.1371/journal.pcbi.1005295

    Figure Lengend Snippet: Dynamics of Ca2+ concentrations on the network

    Article Snippet: Maintaining the low concentrations of Ca2+ in the cytoplasm against a 10,000-fold higher extracellular Ca2+ concentration, i.e. the strong trans-membrane electrochemical gradient of Ca2+ ions needed for proper cell signaling [ ] requires energy.

    Techniques:

    Dynamics of Ca2+ concentrations on the network

    Journal: PLoS Computational Biology

    Article Title: The Effect of Gap Junctional Coupling on the Spatiotemporal Patterns of Ca2+ Signals and the Harmonization of Ca2+-Related Cellular Responses

    doi: 10.1371/journal.pcbi.1005295

    Figure Lengend Snippet: Dynamics of Ca2+ concentrations on the network

    Article Snippet: Maintaining the low concentrations of Ca2+ in the cytoplasm against a 10,000-fold higher extracellular Ca2+ concentration, i.e. the strong trans-membrane electrochemical gradient of Ca2+ ions needed for proper cell signaling [ ] requires energy.

    Techniques:

    Effect of the gap junctional coupling (d ) on Ca2+ waves in the noise-free models G D

    Journal: PLoS Computational Biology

    Article Title: The Effect of Gap Junctional Coupling on the Spatiotemporal Patterns of Ca2+ Signals and the Harmonization of Ca2+-Related Cellular Responses

    doi: 10.1371/journal.pcbi.1005295

    Figure Lengend Snippet: Effect of the gap junctional coupling (d ) on Ca2+ waves in the noise-free models G D

    Article Snippet: Maintaining the low concentrations of Ca2+ in the cytoplasm against a 10,000-fold higher extracellular Ca2+ concentration, i.e. the strong trans-membrane electrochemical gradient of Ca2+ ions needed for proper cell signaling [ ] requires energy.

    Techniques:

    Dynamics of Ca2+ concentrations on the network

    Journal: PLoS Computational Biology

    Article Title: The Effect of Gap Junctional Coupling on the Spatiotemporal Patterns of Ca2+ Signals and the Harmonization of Ca2+-Related Cellular Responses

    doi: 10.1371/journal.pcbi.1005295

    Figure Lengend Snippet: Dynamics of Ca2+ concentrations on the network

    Article Snippet: Maintaining the low concentrations of Ca2+ in the cytoplasm against a 10,000-fold higher extracellular Ca2+ concentration, i.e. the strong trans-membrane electrochemical gradient of Ca2+ ions needed for proper cell signaling [ ] requires energy.

    Techniques:

    Dynamics of Ca2+ concentrations on the network

    Journal: PLoS Computational Biology

    Article Title: The Effect of Gap Junctional Coupling on the Spatiotemporal Patterns of Ca2+ Signals and the Harmonization of Ca2+-Related Cellular Responses

    doi: 10.1371/journal.pcbi.1005295

    Figure Lengend Snippet: Dynamics of Ca2+ concentrations on the network

    Article Snippet: Maintaining the low concentrations of Ca2+ in the cytoplasm against a 10,000-fold higher extracellular Ca2+ concentration, i.e. the strong trans-membrane electrochemical gradient of Ca2+ ions needed for proper cell signaling [ ] requires energy.

    Techniques:

    Supporting Information Circular waves in a noise-free model emerge from highly sensitive cells. Simultaneous changes in ccyt (left panel) and cER (right panel) have been shown. Non-self-oscillating cells synchronize with their oscillating neighbors and produces spiral waves. Independent evolution of the cytoplasmic Ca2+ concentrations ccyt without gap junctional coupling (d = 0) in the random model. Bursting phenomena with moderate gap junctional coupling in the random model. Rapid synchronization with high gap junctional coupling in the random model and appearance of spiraling phenomena. Wave propagation in the random model in a highly linked graph. Wave propagation in the random model in a poorly linked graph. Wave propagation in the random model with holes. Appearance of spirals in a noise-free model with three highly sensitive zones. Appearance of spirals in a noise-free model with two highly sensitive zones. A sensitive random model with low noise evokes spirals. A sensitive random model with low noise and an additional sensitive central zone produces concentric circular waves. Setting one parameter above the “physiological” limit in the random model with low noise results in non-organized wave propagation and spirals. Wave propagation in the random model with Ca2+ coupling and no InsP3 coupling. Wave propagation in the random model with InsP3 coupling and no Ca2+ coupling. Wave propagation in the random model with InsP3 coupling and Ca2+ coupling. Wave propagation in the deterministic model with CR. Adjunction of CR in the random model helps synchronization. μ i I P 3 , m a x

    Journal: PLoS Computational Biology

    Article Title: The Effect of Gap Junctional Coupling on the Spatiotemporal Patterns of Ca2+ Signals and the Harmonization of Ca2+-Related Cellular Responses

    doi: 10.1371/journal.pcbi.1005295

    Figure Lengend Snippet: Supporting Information Circular waves in a noise-free model emerge from highly sensitive cells. Simultaneous changes in ccyt (left panel) and cER (right panel) have been shown. Non-self-oscillating cells synchronize with their oscillating neighbors and produces spiral waves. Independent evolution of the cytoplasmic Ca2+ concentrations ccyt without gap junctional coupling (d = 0) in the random model. Bursting phenomena with moderate gap junctional coupling in the random model. Rapid synchronization with high gap junctional coupling in the random model and appearance of spiraling phenomena. Wave propagation in the random model in a highly linked graph. Wave propagation in the random model in a poorly linked graph. Wave propagation in the random model with holes. Appearance of spirals in a noise-free model with three highly sensitive zones. Appearance of spirals in a noise-free model with two highly sensitive zones. A sensitive random model with low noise evokes spirals. A sensitive random model with low noise and an additional sensitive central zone produces concentric circular waves. Setting one parameter above the “physiological” limit in the random model with low noise results in non-organized wave propagation and spirals. Wave propagation in the random model with Ca2+ coupling and no InsP3 coupling. Wave propagation in the random model with InsP3 coupling and no Ca2+ coupling. Wave propagation in the random model with InsP3 coupling and Ca2+ coupling. Wave propagation in the deterministic model with CR. Adjunction of CR in the random model helps synchronization. μ i I P 3 , m a x

    Article Snippet: Maintaining the low concentrations of Ca2+ in the cytoplasm against a 10,000-fold higher extracellular Ca2+ concentration, i.e. the strong trans-membrane electrochemical gradient of Ca2+ ions needed for proper cell signaling [ ] requires energy.

    Techniques:

    Dynamics of Ca2+ concentrations on the network

    Journal: PLoS Computational Biology

    Article Title: The Effect of Gap Junctional Coupling on the Spatiotemporal Patterns of Ca2+ Signals and the Harmonization of Ca2+-Related Cellular Responses

    doi: 10.1371/journal.pcbi.1005295

    Figure Lengend Snippet: Dynamics of Ca2+ concentrations on the network

    Article Snippet: Maintaining the low concentrations of Ca2+ in the cytoplasm against a 10,000-fold higher extracellular Ca2+ concentration, i.e. the strong trans-membrane electrochemical gradient of Ca2+ ions needed for proper cell signaling [ ] requires energy.

    Techniques:

    Dynamics of Ca2+ concentrations on the network

    Journal: PLoS Computational Biology

    Article Title: The Effect of Gap Junctional Coupling on the Spatiotemporal Patterns of Ca2+ Signals and the Harmonization of Ca2+-Related Cellular Responses

    doi: 10.1371/journal.pcbi.1005295

    Figure Lengend Snippet: Dynamics of Ca2+ concentrations on the network

    Article Snippet: Maintaining the low concentrations of Ca2+ in the cytoplasm against a 10,000-fold higher extracellular Ca2+ concentration, i.e. the strong trans-membrane electrochemical gradient of Ca2+ ions needed for proper cell signaling [ ] requires energy.

    Techniques:

    Dynamics of Ca2+ concentrations on the network

    Journal: PLoS Computational Biology

    Article Title: The Effect of Gap Junctional Coupling on the Spatiotemporal Patterns of Ca2+ Signals and the Harmonization of Ca2+-Related Cellular Responses

    doi: 10.1371/journal.pcbi.1005295

    Figure Lengend Snippet: Dynamics of Ca2+ concentrations on the network

    Article Snippet: Maintaining the low concentrations of Ca2+ in the cytoplasm against a 10,000-fold higher extracellular Ca2+ concentration, i.e. the strong trans-membrane electrochemical gradient of Ca2+ ions needed for proper cell signaling [ ] requires energy.

    Techniques:

    Dynamics of Ca2+ concentrations on the network

    Journal: PLoS Computational Biology

    Article Title: The Effect of Gap Junctional Coupling on the Spatiotemporal Patterns of Ca2+ Signals and the Harmonization of Ca2+-Related Cellular Responses

    doi: 10.1371/journal.pcbi.1005295

    Figure Lengend Snippet: Dynamics of Ca2+ concentrations on the network

    Article Snippet: Maintaining the low concentrations of Ca2+ in the cytoplasm against a 10,000-fold higher extracellular Ca2+ concentration, i.e. the strong trans-membrane electrochemical gradient of Ca2+ ions needed for proper cell signaling [ ] requires energy.

    Techniques:

    Dynamics of Ca2+ concentrations on the network

    Journal: PLoS Computational Biology

    Article Title: The Effect of Gap Junctional Coupling on the Spatiotemporal Patterns of Ca2+ Signals and the Harmonization of Ca2+-Related Cellular Responses

    doi: 10.1371/journal.pcbi.1005295

    Figure Lengend Snippet: Dynamics of Ca2+ concentrations on the network

    Article Snippet: Maintaining the low concentrations of Ca2+ in the cytoplasm against a 10,000-fold higher extracellular Ca2+ concentration, i.e. the strong trans-membrane electrochemical gradient of Ca2+ ions needed for proper cell signaling [ ] requires energy.

    Techniques:

    Dynamics of Ca2+ concentrations on the network

    Journal: PLoS Computational Biology

    Article Title: The Effect of Gap Junctional Coupling on the Spatiotemporal Patterns of Ca2+ Signals and the Harmonization of Ca2+-Related Cellular Responses

    doi: 10.1371/journal.pcbi.1005295

    Figure Lengend Snippet: Dynamics of Ca2+ concentrations on the network

    Article Snippet: Maintaining the low concentrations of Ca2+ in the cytoplasm against a 10,000-fold higher extracellular Ca2+ concentration, i.e. the strong trans-membrane electrochemical gradient of Ca2+ ions needed for proper cell signaling [ ] requires energy.

    Techniques:

    Dynamics of Ca2+ concentrations on the network

    Journal: PLoS Computational Biology

    Article Title: The Effect of Gap Junctional Coupling on the Spatiotemporal Patterns of Ca2+ Signals and the Harmonization of Ca2+-Related Cellular Responses

    doi: 10.1371/journal.pcbi.1005295

    Figure Lengend Snippet: Dynamics of Ca2+ concentrations on the network

    Article Snippet: Maintaining the low concentrations of Ca2+ in the cytoplasm against a 10,000-fold higher extracellular Ca2+ concentration, i.e. the strong trans-membrane electrochemical gradient of Ca2+ ions needed for proper cell signaling [ ] requires energy.

    Techniques:

    Dynamics of Ca2+ concentrations on the network

    Journal: PLoS Computational Biology

    Article Title: The Effect of Gap Junctional Coupling on the Spatiotemporal Patterns of Ca2+ Signals and the Harmonization of Ca2+-Related Cellular Responses

    doi: 10.1371/journal.pcbi.1005295

    Figure Lengend Snippet: Dynamics of Ca2+ concentrations on the network

    Article Snippet: Maintaining the low concentrations of Ca2+ in the cytoplasm against a 10,000-fold higher extracellular Ca2+ concentration, i.e. the strong trans-membrane electrochemical gradient of Ca2+ ions needed for proper cell signaling [ ] requires energy.

    Techniques:

    Lack of homology among Slo3 sequences in the ligand-sensing cytosolic domain. ( A ) Alignments of human Slo1 and Slo3 from various species are shown for the membrane-associated, pore-forming part of the channels, indicating the relatively high extent of conservation through this part of the Slo3 protein. The Slo1 N-terminus is omitted to minimize effects of S0–S1 linker gaps on the alignment. Slo1 numbering starts from amino acids MDAL. Tick marks below each segment of residues counts every 10 residues in human Slo3. ( B ) Alignments of human Slo1 and Slo3 from various species are shown for the cytosolic gating ring domain beginning with the conserved sequence at the beginning of the first RCK domain. Blue highlights residue differences between human Slo1 and human Slo3. Yellow highlights differences of Slo3 of various species to human Slo3. Alignments were generated by Clustal 1.2.0 and minor adjustments were made based on structural considerations ( Leonetti et al., 2012 ). Above the residues, the correspondence of particular amino acid segments to structurally defined α-helical and β-strand segments is shown based on Leonetti et al. (2012) . In red, residues or segments identified in Slo1 or Slo3 isoforms which are implicated in ligand-sensing or species-specific functional differences are highlighted. Although extensive information is available regarding loci important in ligand-sensing in Slo1, such information for Slo3 remains lacking. Numbers identify the following: 1, the sequence of residues termed the Ca 2+ bowl ( Schreiber and Salkoff, 1997 ), for which there is good correspondence of mutations affecting Ca2+-dependent function ( Bao et al., 2004 ) and coordination of density in a crystal structure ( Yuan et al., 2012 ); 2, the D367 residue implicated in the role of the RCK1 domain in Ca 2+ -dependent activation ( Xia et al., 2002 ) which is clearly distinct from Ca 2+ -bowl dependent activation ( Zeng et al., 2005 ); 3, the M513 residue, which also affects Ca 2+− dependent activation involving the RCK1 domain ( Bao et al., 2002 ), but probably is not involved in ligand coordination; 4, residues E374 and E399 which have been implicated in low affinity effects of divalent cations, specifically Mg 2+ ( Shi et al., 2002 ; Xia et al., 2002 ; Yang et al., 2006 ); 5, residue E535 which may also be involved in Ca 2+ coordination in RCK1 ( Zhang et al., 2010 ); 6, residues H365 and H394, which have been implicated in proton-dependent activation of Slo1 and also influence Ca 2+ -dependent activation when protonated ( Hou et al., 2008 ); 7, H417 and segment 368–475, which influence pH-sensing in mouse Slo3 (Zhang et al., 2006); 8, segment 495–515 in bovine Slo3 which accounts for part of the different in functional properties between mouse Slo3 and bovine Slo3 ( Santi et al., 2009 ). Illustrated sequences and accession numbers include: HsSlo1 ( Homo sapiens ), NP_001154824, Gene ID 3778; HsSlo3 ( Homo sapiens ), NP_001027006, Gene ID 157855; MmSlo3 ( Mus musculus ), NP_032458, Gene ID 16532; RnSlo3 ( Rattus norvegicus ), XP_006253398, Gene ID 680912; TcSlo3 (Tupaia chinensis, Chinese tree shrew), XP_006171561, Gene ID 102493286; CcSlo3 ( Condylura cristata , star-nosed mole), XP_004682520, Gene ID 101620543; CfSlo3 (Canis lupus familiaris), XP_539971, Gene ID 482856; BtSlo3 (Bos taurus), NP_001156721, Gene ID 524144; OaSlo3 ( Ovis aries , sheep), XP_004021821, Gene ID 10110209. DOI: http://dx.doi.org/10.7554/eLife.01438.019

    Journal: eLife

    Article Title: The Ca2+-activated K+ current of human sperm is mediated by Slo3

    doi: 10.7554/eLife.01438

    Figure Lengend Snippet: Lack of homology among Slo3 sequences in the ligand-sensing cytosolic domain. ( A ) Alignments of human Slo1 and Slo3 from various species are shown for the membrane-associated, pore-forming part of the channels, indicating the relatively high extent of conservation through this part of the Slo3 protein. The Slo1 N-terminus is omitted to minimize effects of S0–S1 linker gaps on the alignment. Slo1 numbering starts from amino acids MDAL. Tick marks below each segment of residues counts every 10 residues in human Slo3. ( B ) Alignments of human Slo1 and Slo3 from various species are shown for the cytosolic gating ring domain beginning with the conserved sequence at the beginning of the first RCK domain. Blue highlights residue differences between human Slo1 and human Slo3. Yellow highlights differences of Slo3 of various species to human Slo3. Alignments were generated by Clustal 1.2.0 and minor adjustments were made based on structural considerations ( Leonetti et al., 2012 ). Above the residues, the correspondence of particular amino acid segments to structurally defined α-helical and β-strand segments is shown based on Leonetti et al. (2012) . In red, residues or segments identified in Slo1 or Slo3 isoforms which are implicated in ligand-sensing or species-specific functional differences are highlighted. Although extensive information is available regarding loci important in ligand-sensing in Slo1, such information for Slo3 remains lacking. Numbers identify the following: 1, the sequence of residues termed the Ca 2+ bowl ( Schreiber and Salkoff, 1997 ), for which there is good correspondence of mutations affecting Ca2+-dependent function ( Bao et al., 2004 ) and coordination of density in a crystal structure ( Yuan et al., 2012 ); 2, the D367 residue implicated in the role of the RCK1 domain in Ca 2+ -dependent activation ( Xia et al., 2002 ) which is clearly distinct from Ca 2+ -bowl dependent activation ( Zeng et al., 2005 ); 3, the M513 residue, which also affects Ca 2+− dependent activation involving the RCK1 domain ( Bao et al., 2002 ), but probably is not involved in ligand coordination; 4, residues E374 and E399 which have been implicated in low affinity effects of divalent cations, specifically Mg 2+ ( Shi et al., 2002 ; Xia et al., 2002 ; Yang et al., 2006 ); 5, residue E535 which may also be involved in Ca 2+ coordination in RCK1 ( Zhang et al., 2010 ); 6, residues H365 and H394, which have been implicated in proton-dependent activation of Slo1 and also influence Ca 2+ -dependent activation when protonated ( Hou et al., 2008 ); 7, H417 and segment 368–475, which influence pH-sensing in mouse Slo3 (Zhang et al., 2006); 8, segment 495–515 in bovine Slo3 which accounts for part of the different in functional properties between mouse Slo3 and bovine Slo3 ( Santi et al., 2009 ). Illustrated sequences and accession numbers include: HsSlo1 ( Homo sapiens ), NP_001154824, Gene ID 3778; HsSlo3 ( Homo sapiens ), NP_001027006, Gene ID 157855; MmSlo3 ( Mus musculus ), NP_032458, Gene ID 16532; RnSlo3 ( Rattus norvegicus ), XP_006253398, Gene ID 680912; TcSlo3 (Tupaia chinensis, Chinese tree shrew), XP_006171561, Gene ID 102493286; CcSlo3 ( Condylura cristata , star-nosed mole), XP_004682520, Gene ID 101620543; CfSlo3 (Canis lupus familiaris), XP_539971, Gene ID 482856; BtSlo3 (Bos taurus), NP_001156721, Gene ID 524144; OaSlo3 ( Ovis aries , sheep), XP_004021821, Gene ID 10110209. DOI: http://dx.doi.org/10.7554/eLife.01438.019

    Article Snippet: DMNP-EDTA and Ca2+ indicators were purchased from Invitrogen (Carlsbad, CA, USA).

    Techniques: Sequencing, Generated, Functional Assay, Activation Assay

    Effect of NaHS on [Ca2+] i in cultured gastric fundus smooth muscles. Aa: The time-dependent effects of different concentrations of NaHS on [Ca2+] i . Ab: Summary graph showing the effects of the NaHS-induced increase in intracellular calcium; Ba: Raw traces

    Journal: World Journal of Gastroenterology : WJG

    Article Title: Hydrogen sulfide-induced enhancement of gastric fundus smooth muscle tone is mediated by voltage-dependent potassium and calcium channels in mice

    doi: 10.3748/wjg.v21.i16.4840

    Figure Lengend Snippet: Effect of NaHS on [Ca2+] i in cultured gastric fundus smooth muscles. Aa: The time-dependent effects of different concentrations of NaHS on [Ca2+] i . Ab: Summary graph showing the effects of the NaHS-induced increase in intracellular calcium; Ba: Raw traces

    Article Snippet: [Ca2+ ]i was measured in cells loaded with 1 μmol/L fura-3 acetoxymethyl ester (fura-3AM) (Sigma-Aldrich, St. Louis, MO, United States) dissolved in PSS containing 1 μmol/L F127 in a carbon dioxide incubator for 1 h. After fura-3AM loading, the cells were washed three times in PSS and placed under a fluorescence microscope (BX3, Olympus, Tokyo, Japan).

    Techniques: Cell Culture