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Journal of Biological Chemistry ca2
Ca2, supplied by Journal of Biological Chemistry, 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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Activation Assay:

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Article Snippet: .. Mitochondria suppress local feedback activation of inositol 1,4, 5-trisphosphate receptors by Ca2+ The Journal of biological chemistry. ..

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Activity Assay:

Article Title:
Article Snippet: .. Nitric oxide induces Ca2+-independent activity of the Ca2+/calmodulin-dependent protein kinase II (CaMKII) Journal of Biological Chemistry. .. [ ] [ ] Coultrap SJ, Freund RK, O’Leary H, Sanderson JL, Roche KW, Dell'Acqua ML, Bayer KU.

Expressing:

Article Title:
Article Snippet: .. [ ] Guerini D, Garcia-Martin E, Gerber A, Volbracht C, Leist M, Merino CG, Carafoli E. The expression of plasma membrane Ca2+ pump isoforms in cerebellar granule neurons is modulated by Ca2+ Journal of Biological Chemistry. .. [ ] Hammes A, Oberdorf S, Strehler EE, Stauffer T, Carafoli E, Vetter H, Neyses L. Differentiation-specific isoform mRNA expression of the calmodulin-dependent plasma membrane Ca(2+) -ATPase.

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  • 88
    Journal of Biological Chemistry ca2 activation
    Nox family members and their regulatory subunits Although no 3-dimensional crystallization of Nox proteins has been performed, they are believed to contain six transmembrane domains based on hydrophobicity analysis (seven for Duox1/2). Oxidase activity occurs when NADPH binds to Nox on the cytosolic side, where it transfers electrons to FAD and the heme centers (not shown) and finally to oxygen on the outer membrane surface, resulting in O 2 •− formation. In Nox1-4, the transmembrane subunit p22phox associates with active and inactive Nox. It is believed to have between two and four transmembrane segments. Nox1 is believed to primarily interact with the cytosolic subunits NoxO1, NoxA1 and GTP-Rac upon activation; however p47phox and p67phox can replace NoxO1 and NoxA1, respectively. Nox2 activation involves association with GTP-Rac, p47phox, p67phox and p40phox. Nox3 activation is less well defined, but is believed to primarily involve GTP-Rac, p47phox and NoxA1 in the inner ear. Nox4 is constitutively active when associating with the cytosolic p22phox subunit. Nox5 and Duox1/2 activation involves <t>Ca2</t> + binding to EF-hand domains in the cytosol. Duox1/2 require the association of DuoxA1/2, respectively, for localization to the plasma membrane.
    Ca2 Activation, supplied by Journal of Biological Chemistry, used in various techniques. Bioz Stars score: 88/100, based on 6 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    90
    Journal of Biological Chemistry apical ca2 channel
    The A563T variation increases the radius of the Ca 2+ -selective filter. (A) Pore radius (Å) for A563 (in black) and T563 (in red) along the pore axis. To give a clear view of the pore, the solvent-accessible pathway is shown. The residues for the selective filter (D542) and the lower gate (M578) are also shown. In the pathway, the size of the pore radius is shown by different colors (red for a radius smaller than 1.15 Å, green for a radius between 1.15 Å and 2.30 Å, and blue for a radius larger than 2.30 Å). ( B ) Radial distribution functions (RDFs) of Ca 2+ ions (Ca1, <t>Ca2</t> and Ca3) with the Cα atoms of TRPV5 for A563 (in black) and T563 (in red).
    Apical Ca2 Channel, supplied by Journal of Biological Chemistry, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    80
    Journal of Biological Chemistry epithelial ca2 channel
    The A563T variation increases the radius of the Ca 2+ -selective filter. (A) Pore radius (Å) for A563 (in black) and T563 (in red) along the pore axis. To give a clear view of the pore, the solvent-accessible pathway is shown. The residues for the selective filter (D542) and the lower gate (M578) are also shown. In the pathway, the size of the pore radius is shown by different colors (red for a radius smaller than 1.15 Å, green for a radius between 1.15 Å and 2.30 Å, and blue for a radius larger than 2.30 Å). ( B ) Radial distribution functions (RDFs) of Ca 2+ ions (Ca1, <t>Ca2</t> and Ca3) with the Cα atoms of TRPV5 for A563 (in black) and T563 (in red).
    Epithelial Ca2 Channel, supplied by Journal of Biological Chemistry, used in various techniques. Bioz Stars score: 80/100, based on 0 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    90
    Journal of Biological Chemistry ca2 dissociation
    Comparison of Ca 2+ dissociation rates from cardiac TnC in systems of increasing complexity with that of muscle relaxation The rate of Ca 2+ ]. This figure highlights the fact that the loop sequence alone is not the dominating factor that determines the <t>Ca2+</t> binding properties of an EF-hand or its system.
    Ca2 Dissociation, supplied by Journal of Biological Chemistry, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Nox family members and their regulatory subunits Although no 3-dimensional crystallization of Nox proteins has been performed, they are believed to contain six transmembrane domains based on hydrophobicity analysis (seven for Duox1/2). Oxidase activity occurs when NADPH binds to Nox on the cytosolic side, where it transfers electrons to FAD and the heme centers (not shown) and finally to oxygen on the outer membrane surface, resulting in O 2 •− formation. In Nox1-4, the transmembrane subunit p22phox associates with active and inactive Nox. It is believed to have between two and four transmembrane segments. Nox1 is believed to primarily interact with the cytosolic subunits NoxO1, NoxA1 and GTP-Rac upon activation; however p47phox and p67phox can replace NoxO1 and NoxA1, respectively. Nox2 activation involves association with GTP-Rac, p47phox, p67phox and p40phox. Nox3 activation is less well defined, but is believed to primarily involve GTP-Rac, p47phox and NoxA1 in the inner ear. Nox4 is constitutively active when associating with the cytosolic p22phox subunit. Nox5 and Duox1/2 activation involves Ca2 + binding to EF-hand domains in the cytosol. Duox1/2 require the association of DuoxA1/2, respectively, for localization to the plasma membrane.

    Journal: Free radical biology & medicine

    Article Title: Nox proteins in signal transduction

    doi: 10.1016/j.freeradbiomed.2009.07.023

    Figure Lengend Snippet: Nox family members and their regulatory subunits Although no 3-dimensional crystallization of Nox proteins has been performed, they are believed to contain six transmembrane domains based on hydrophobicity analysis (seven for Duox1/2). Oxidase activity occurs when NADPH binds to Nox on the cytosolic side, where it transfers electrons to FAD and the heme centers (not shown) and finally to oxygen on the outer membrane surface, resulting in O 2 •− formation. In Nox1-4, the transmembrane subunit p22phox associates with active and inactive Nox. It is believed to have between two and four transmembrane segments. Nox1 is believed to primarily interact with the cytosolic subunits NoxO1, NoxA1 and GTP-Rac upon activation; however p47phox and p67phox can replace NoxO1 and NoxA1, respectively. Nox2 activation involves association with GTP-Rac, p47phox, p67phox and p40phox. Nox3 activation is less well defined, but is believed to primarily involve GTP-Rac, p47phox and NoxA1 in the inner ear. Nox4 is constitutively active when associating with the cytosolic p22phox subunit. Nox5 and Duox1/2 activation involves Ca2 + binding to EF-hand domains in the cytosol. Duox1/2 require the association of DuoxA1/2, respectively, for localization to the plasma membrane.

    Article Snippet: Mechanism of Ca2+ activation of the NADPH oxidase 5 (NOX5) The Journal of biological chemistry.

    Techniques: Crystallization Assay, Activity Assay, Activation Assay, Binding Assay

    The A563T variation increases the radius of the Ca 2+ -selective filter. (A) Pore radius (Å) for A563 (in black) and T563 (in red) along the pore axis. To give a clear view of the pore, the solvent-accessible pathway is shown. The residues for the selective filter (D542) and the lower gate (M578) are also shown. In the pathway, the size of the pore radius is shown by different colors (red for a radius smaller than 1.15 Å, green for a radius between 1.15 Å and 2.30 Å, and blue for a radius larger than 2.30 Å). ( B ) Radial distribution functions (RDFs) of Ca 2+ ions (Ca1, Ca2 and Ca3) with the Cα atoms of TRPV5 for A563 (in black) and T563 (in red).

    Journal: Journal of biomolecular structure & dynamics

    Article Title: Modeling the structural and dynamical changes of the epithelial calcium channel TRPV5 caused by the A563T variation based on the structure of TRPV6

    doi: 10.1080/07391102.2018.1518790

    Figure Lengend Snippet: The A563T variation increases the radius of the Ca 2+ -selective filter. (A) Pore radius (Å) for A563 (in black) and T563 (in red) along the pore axis. To give a clear view of the pore, the solvent-accessible pathway is shown. The residues for the selective filter (D542) and the lower gate (M578) are also shown. In the pathway, the size of the pore radius is shown by different colors (red for a radius smaller than 1.15 Å, green for a radius between 1.15 Å and 2.30 Å, and blue for a radius larger than 2.30 Å). ( B ) Radial distribution functions (RDFs) of Ca 2+ ions (Ca1, Ca2 and Ca3) with the Cα atoms of TRPV5 for A563 (in black) and T563 (in red).

    Article Snippet: 91 , 508–517. doi: 10.1529/biophysj.106.082313 [ ] [ ] [ ] [ ] Hoenderop JG, van der Kemp AWCM, Hartog A, van de Graaf SFJ, van Os CH, Willems PHGM, & Bindels RJM (1999) Molecular identification of the apical Ca2+ channel in 1,25-dihydroxyvitamin D-3-responsive epithelia , Journal of Biological Chemistry , 274 , 8375–8378. doi: 10.1074/jbc.274.13.8375 [ ] [ ] [ ] Hoenderop JG, van Leeuwen JP, van der Eerden BC, Kersten FF, van der Kemp AW, Merillat AM, Waarsing JH, Rossier BC, Vallon V, Hummler E, & Bindels RJ (2003) Renal Ca2+ wasting, hyperabsorption, and reduced bone thickness in mice lacking TRPV5 , Journal of Clinical Investigation , 112 , 1906–1914. doi:10.1172/JCI19826 [ ] [ ] [ ] [ ] Hooft RWW, Vriend G, Sander C, and Abola EE (1996) Errors in protein structures .

    Techniques:

    The A563T variation increases the radius of the Ca 2+ -selective filter. (A) Pore radius (Å) for A563 (in black) and T563 (in red) along the pore axis. To give a clear view of the pore, the solvent-accessible pathway is shown. The residues for the selective filter (D542) and the lower gate (M578) are also shown. In the pathway, the size of the pore radius is shown by different colors (red for a radius smaller than 1.15 Å, green for a radius between 1.15 Å and 2.30 Å, and blue for a radius larger than 2.30 Å). ( B ) Radial distribution functions (RDFs) of Ca 2+ ions (Ca1, Ca2 and Ca3) with the Cα atoms of TRPV5 for A563 (in black) and T563 (in red).

    Journal: Journal of biomolecular structure & dynamics

    Article Title: Modeling the structural and dynamical changes of the epithelial calcium channel TRPV5 caused by the A563T variation based on the structure of TRPV6

    doi: 10.1080/07391102.2018.1518790

    Figure Lengend Snippet: The A563T variation increases the radius of the Ca 2+ -selective filter. (A) Pore radius (Å) for A563 (in black) and T563 (in red) along the pore axis. To give a clear view of the pore, the solvent-accessible pathway is shown. The residues for the selective filter (D542) and the lower gate (M578) are also shown. In the pathway, the size of the pore radius is shown by different colors (red for a radius smaller than 1.15 Å, green for a radius between 1.15 Å and 2.30 Å, and blue for a radius larger than 2.30 Å). ( B ) Radial distribution functions (RDFs) of Ca 2+ ions (Ca1, Ca2 and Ca3) with the Cα atoms of TRPV5 for A563 (in black) and T563 (in red).

    Article Snippet: Journal of Applied Crystallography , 26 , 283–291. doi:10.1107/S0021889892009944 [ ] [ ] Li F, Wang L, Xiao N, Yang M, Jiang L, & Liu M (2010) Dominant conformation of valsartan in sodium dodecyl sulfate micelle environment , Journal of Physical Chemistry B , 114 , 2719–2727. doi:10.1021/jp908958k [ ] [ ] [ ] Loh NY, Bentley L, Dimke H, Verkaart S, Tammaro P, Gorvin CM, Stechman MJ, Ahmad BN, Hannan FM, Piret SE, Evans H, Bellantuono I, Hough TA, Fraser WD, Hoenderop JG, Ashcroft FM, Brown SD, Bindels RJ, Cox RD, & Thakker RV (2013) Autosomal dominant hypercalciuria in a mouse model due to a mutation of the epithelial calcium channel, TRPV5 , PLoS One , 8 , e55412. doi: 10.1371/journal.pone.0055412 [ ] [ ] [ ] [ ] Na T, & Peng JB (2014) TRPV5: A Ca2+ Channel for the Fine-Tuning of Ca2+ Reabsorption , Handbook of Experimental Pharmacology , 222 , 321–357. doi:10.1007/978-3-642-54215-2_13 [ ] [ ] [ ] Na T, Zhang W, Jiang Y, Liang Y, Ma HP, Warnock DG, & Peng JB (2009) The A563T cariation of the renal epithelial calcium channel TRPV5 among African Americans enhances calcium influx , American Journal of Physiology Renal Physiology , 296 , 1042–1051. doi :10.1152/ajprenal.90771.2008 [ ] [ ] [ ] [ ] Nilius B, Vennekens R, Prenen J, Hoenderop JGJ, Droogmans G, & Bindels RJM (2001) The single pore residue Asp542 determines Ca2+ permeation and Mg2+ block of the epithelial Ca2+ channel , Journal of Biological Chemistry , 276 , 1020–1025. doi: 10.1074/jbc.M006184200 [ ] [ ] [ ] Oddsson A, Sulem P, Helgason H, Edvardsson VO, Thorleifsson G, Sveinbjörnsson G, Haraldsdottir E, Eyjolfsson GI, Sigurdardottir O, Olafsson I, Masson G, Holm H, Gudbjartsson DF, Thorsteinsdottir U, Indridason OS, Palsson R, & Stefansson K (2015) Common and rare variants associated with kidney stones and biochemical traits ., Nature Communications , 6 , 7975–7983. doi:10.1038/ncomms8975.

    Techniques:

    Comparison of Ca 2+ dissociation rates from cardiac TnC in systems of increasing complexity with that of muscle relaxation The rate of Ca 2+ ]. This figure highlights the fact that the loop sequence alone is not the dominating factor that determines the Ca2+ binding properties of an EF-hand or its system.

    Journal: Archives of biochemistry and biophysics

    Article Title: Designing Proteins to Combat Disease: Cardiac Troponin C as an Example

    doi: 10.1016/j.abb.2016.02.007

    Figure Lengend Snippet: Comparison of Ca 2+ dissociation rates from cardiac TnC in systems of increasing complexity with that of muscle relaxation The rate of Ca 2+ ]. This figure highlights the fact that the loop sequence alone is not the dominating factor that determines the Ca2+ binding properties of an EF-hand or its system.

    Article Snippet: The rates of Ca2+ dissociation and cross-bridge detachment from ventricular myofibrils as reported by a fluorescent cardiac troponin C. The Journal of biological chemistry.

    Techniques: Sequencing, Binding Assay