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  • 99
    Thermo Fisher complete protease inhibitor cocktail
    Complete Protease Inhibitor Cocktail, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 99/100, based on 388 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Millipore protease inhibitor cocktail
    Protease Inhibitor Cocktail, supplied by Millipore, used in various techniques. Bioz Stars score: 99/100, based on 135500 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    92
    Millipore complete protease inhibitor cocktail
    TA systems do not inhibit growth following diverse stress conditions. (A) Experimental design for panels A-J to measure the growth of wild-type and Δ10TA strains following stress exposure. (B-C) Growth curves for WT and Δ10TA strains grown at 30 °C to OD 600 of ∼0.3, then maintained at 30 °C (B) or shifted to 45 °C (C) for 60 min before dilution and growth rate measurement at 37 °C in flasks. (D-I) Growth curves for WT and Δ10TA strains grown at 37 °C and left untreated (D) or treated with the indicated stress for one hour then washed and diluted into fresh media, as described in (A). For <t>complete</t> description of stress conditions, see Methods. (J) Wild-type and Δ10TA strains labeled with YFP and CFP, respectively, were mixed at a 1:1 ratio. This mixture was propagated and treated with two cycles of chloramphenicol as depicted in the schematic. Samples were taken points indicated by numbers on left, and colony forming units (c.f.u.) of the two strains were determined. The resulting competitive index is graphed on the right where individual symbols indicate independent replicates; black bar represents mean. (K) Growth curve of WT and Δ10TA strains grown at 44 °C. (L-M) Growth curve of WT and Δ10TA strains grown to OD600 ∼0.3, then treated with the indicated stress throughout growth measurements. (N) Growth curves for WT and Δ10TA strains grown at 37 °C and treated with chloramphenicol for four hours, then washed and diluted into fresh media, as described in (A).
    Complete Protease Inhibitor Cocktail, supplied by Millipore, used in various techniques. Bioz Stars score: 92/100, based on 1874 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/complete protease inhibitor cocktail/product/Millipore
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    90
    Millipore complete mini protease inhibitor cocktail
    SH3 domains shuffling impacts Sla1 PPIs, cells growth in different stress conditions and clathrin-mediated endocytosis. A) Sla1 SH3-deleted or -shuffled PPIs as detected by DHFR-PCA. The color code represents PPI strength as detected by DHFR-PCA (PCA score). All PPIs were measured in quadruplicate. A is for Abp1 SH3 and * is for the reinsertion of the WT domain as control strains. A scaled cartoon of Sla1 is also illustrated. B) Cophenetic correlation for the similarity of Sla1 SH3-shuffled PPI clusters with the growth phenotype clusters. Empirical p-value obtained from data permutation is p = 0.00002. C) Representative fluorescence microscopy timeframe analysis of a yeast cell expressing WT Sla1-GFP. The calculated trajectories for every Sla1-GFP foci detected are shown. Cell membrane is delimited with a dashed line and each Sla1-GFP particle colors represent its position in time. D) Sla1-GFP particles average effective distance travelled towards the cell center through time. Sla1 SH3-deleted strains are shown. The proportion of events that are not completed yet is represented by the color transparency of the curves (+ represent the time point when 95% of foci have disassembled). E) <t>Complete</t> or incomplete Sla1-GFP endocytosis events are shown (average per cell) for Sla1 SH3-deleted strains. F) Representation of the linearity of Sla1-GFP particle trajectories for each SH3 deletion or shuffling. G) Sla1-GFP particle lifetime (in seconds) are shown for the same strains as in F). See also Data S5.
    Complete Mini Protease Inhibitor Cocktail, supplied by Millipore, used in various techniques. Bioz Stars score: 90/100, based on 3181 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Cell Signaling Technology Inc complete protease inhibitor cocktail
    SH3 domains shuffling impacts Sla1 PPIs, cells growth in different stress conditions and clathrin-mediated endocytosis. A) Sla1 SH3-deleted or -shuffled PPIs as detected by DHFR-PCA. The color code represents PPI strength as detected by DHFR-PCA (PCA score). All PPIs were measured in quadruplicate. A is for Abp1 SH3 and * is for the reinsertion of the WT domain as control strains. A scaled cartoon of Sla1 is also illustrated. B) Cophenetic correlation for the similarity of Sla1 SH3-shuffled PPI clusters with the growth phenotype clusters. Empirical p-value obtained from data permutation is p = 0.00002. C) Representative fluorescence microscopy timeframe analysis of a yeast cell expressing WT Sla1-GFP. The calculated trajectories for every Sla1-GFP foci detected are shown. Cell membrane is delimited with a dashed line and each Sla1-GFP particle colors represent its position in time. D) Sla1-GFP particles average effective distance travelled towards the cell center through time. Sla1 SH3-deleted strains are shown. The proportion of events that are not completed yet is represented by the color transparency of the curves (+ represent the time point when 95% of foci have disassembled). E) <t>Complete</t> or incomplete Sla1-GFP endocytosis events are shown (average per cell) for Sla1 SH3-deleted strains. F) Representation of the linearity of Sla1-GFP particle trajectories for each SH3 deletion or shuffling. G) Sla1-GFP particle lifetime (in seconds) are shown for the same strains as in F). See also Data S5.
    Complete Protease Inhibitor Cocktail, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 99/100, based on 33 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Roche protease inhibitors cocktail complete protease inhibitor cocktail
    SH3 domains shuffling impacts Sla1 PPIs, cells growth in different stress conditions and clathrin-mediated endocytosis. A) Sla1 SH3-deleted or -shuffled PPIs as detected by DHFR-PCA. The color code represents PPI strength as detected by DHFR-PCA (PCA score). All PPIs were measured in quadruplicate. A is for Abp1 SH3 and * is for the reinsertion of the WT domain as control strains. A scaled cartoon of Sla1 is also illustrated. B) Cophenetic correlation for the similarity of Sla1 SH3-shuffled PPI clusters with the growth phenotype clusters. Empirical p-value obtained from data permutation is p = 0.00002. C) Representative fluorescence microscopy timeframe analysis of a yeast cell expressing WT Sla1-GFP. The calculated trajectories for every Sla1-GFP foci detected are shown. Cell membrane is delimited with a dashed line and each Sla1-GFP particle colors represent its position in time. D) Sla1-GFP particles average effective distance travelled towards the cell center through time. Sla1 SH3-deleted strains are shown. The proportion of events that are not completed yet is represented by the color transparency of the curves (+ represent the time point when 95% of foci have disassembled). E) <t>Complete</t> or incomplete Sla1-GFP endocytosis events are shown (average per cell) for Sla1 SH3-deleted strains. F) Representation of the linearity of Sla1-GFP particle trajectories for each SH3 deletion or shuffling. G) Sla1-GFP particle lifetime (in seconds) are shown for the same strains as in F). See also Data S5.
    Protease Inhibitors Cocktail Complete Protease Inhibitor Cocktail, supplied by Roche, used in various techniques. Bioz Stars score: 85/100, based on 4 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Image Search Results


    TA systems do not inhibit growth following diverse stress conditions. (A) Experimental design for panels A-J to measure the growth of wild-type and Δ10TA strains following stress exposure. (B-C) Growth curves for WT and Δ10TA strains grown at 30 °C to OD 600 of ∼0.3, then maintained at 30 °C (B) or shifted to 45 °C (C) for 60 min before dilution and growth rate measurement at 37 °C in flasks. (D-I) Growth curves for WT and Δ10TA strains grown at 37 °C and left untreated (D) or treated with the indicated stress for one hour then washed and diluted into fresh media, as described in (A). For complete description of stress conditions, see Methods. (J) Wild-type and Δ10TA strains labeled with YFP and CFP, respectively, were mixed at a 1:1 ratio. This mixture was propagated and treated with two cycles of chloramphenicol as depicted in the schematic. Samples were taken points indicated by numbers on left, and colony forming units (c.f.u.) of the two strains were determined. The resulting competitive index is graphed on the right where individual symbols indicate independent replicates; black bar represents mean. (K) Growth curve of WT and Δ10TA strains grown at 44 °C. (L-M) Growth curve of WT and Δ10TA strains grown to OD600 ∼0.3, then treated with the indicated stress throughout growth measurements. (N) Growth curves for WT and Δ10TA strains grown at 37 °C and treated with chloramphenicol for four hours, then washed and diluted into fresh media, as described in (A).

    Journal: bioRxiv

    Article Title: Stress induces the transcription of toxin-antitoxin systems but does not activate toxin

    doi: 10.1101/2020.03.02.972737

    Figure Lengend Snippet: TA systems do not inhibit growth following diverse stress conditions. (A) Experimental design for panels A-J to measure the growth of wild-type and Δ10TA strains following stress exposure. (B-C) Growth curves for WT and Δ10TA strains grown at 30 °C to OD 600 of ∼0.3, then maintained at 30 °C (B) or shifted to 45 °C (C) for 60 min before dilution and growth rate measurement at 37 °C in flasks. (D-I) Growth curves for WT and Δ10TA strains grown at 37 °C and left untreated (D) or treated with the indicated stress for one hour then washed and diluted into fresh media, as described in (A). For complete description of stress conditions, see Methods. (J) Wild-type and Δ10TA strains labeled with YFP and CFP, respectively, were mixed at a 1:1 ratio. This mixture was propagated and treated with two cycles of chloramphenicol as depicted in the schematic. Samples were taken points indicated by numbers on left, and colony forming units (c.f.u.) of the two strains were determined. The resulting competitive index is graphed on the right where individual symbols indicate independent replicates; black bar represents mean. (K) Growth curve of WT and Δ10TA strains grown at 44 °C. (L-M) Growth curve of WT and Δ10TA strains grown to OD600 ∼0.3, then treated with the indicated stress throughout growth measurements. (N) Growth curves for WT and Δ10TA strains grown at 37 °C and treated with chloramphenicol for four hours, then washed and diluted into fresh media, as described in (A).

    Article Snippet: Pellets were resuspended in 500 µL lysis buffer (PBS supplemented with 0.05% Tween-20, 1 µL/mL benzonase, 1 µL/mL ReadyLyse (Novagen), and cOmplete protease inhibitor cocktail (Sigma)).

    Techniques: Labeling

    Two regions in the Mup1 N-terminal cytosolic tail are critical for endocytic down-regulation. (A) Top, sequence of the cytosolic N-tail (residues 1–60) of the yeast methionine transporter Mup1. The two regions critical for endocytosis are underlined. Bottom, a collection of GFP-tagged Mup1 mutants was stably integrated into yeast cells expressing Vph1-mCherry as vacuolar marker. In each mutant, five consecutive residues of the N-tail were mutated to alanines. Cells were grown to mid log phase in synthetic medium at 30°C, stimulated with 20 μg/ml methionine for 90 min, and analyzed by fluorescence microscopy. Average Mup1 sorting was calculated as the ratio of vacuolar GFP to total cell GFP and normalized to wild type before (0% sorting) and after methionine stimulation (100% sorting). The numbers below each bar of the graph correspond to the position of the substituted residues within Mup1. Error bars indicate SD between fields. (B) Representative images from cells quantified in A. Cells expressing GFP-tagged Mup1 or the indicated Mup1 alanine substitutions were grown to mid log phase in synthetic medium at 30°C and subjected to fluorescence microscopy after treatment with methionine for 90 min. A complete set of images is shown in Supplemental Figure S2. Dashed lines indicate cell outlines. Scale bar, 2.5 μm; vacuolar marker: Vph1-mCherry. (C) Yeast cells expressing GFP-tagged Mup1 or the indicated Mup1 alanine substitutions were grown to mid log phase in synthetic medium at 30°C and stimulated with 20 μg/ml methionine. Equal volumes of culture were harvested at the indicated time points after stimulation, and total cell lysates were prepared and analyzed by SDS–PAGE and immunoblot. G6PDH serves as a control for equal loading.

    Journal: Molecular Biology of the Cell

    Article Title: Identification of the endocytic sorting signal recognized by the Art1-Rsp5 ubiquitin ligase complex

    doi: 10.1091/mbc.E16-08-0570

    Figure Lengend Snippet: Two regions in the Mup1 N-terminal cytosolic tail are critical for endocytic down-regulation. (A) Top, sequence of the cytosolic N-tail (residues 1–60) of the yeast methionine transporter Mup1. The two regions critical for endocytosis are underlined. Bottom, a collection of GFP-tagged Mup1 mutants was stably integrated into yeast cells expressing Vph1-mCherry as vacuolar marker. In each mutant, five consecutive residues of the N-tail were mutated to alanines. Cells were grown to mid log phase in synthetic medium at 30°C, stimulated with 20 μg/ml methionine for 90 min, and analyzed by fluorescence microscopy. Average Mup1 sorting was calculated as the ratio of vacuolar GFP to total cell GFP and normalized to wild type before (0% sorting) and after methionine stimulation (100% sorting). The numbers below each bar of the graph correspond to the position of the substituted residues within Mup1. Error bars indicate SD between fields. (B) Representative images from cells quantified in A. Cells expressing GFP-tagged Mup1 or the indicated Mup1 alanine substitutions were grown to mid log phase in synthetic medium at 30°C and subjected to fluorescence microscopy after treatment with methionine for 90 min. A complete set of images is shown in Supplemental Figure S2. Dashed lines indicate cell outlines. Scale bar, 2.5 μm; vacuolar marker: Vph1-mCherry. (C) Yeast cells expressing GFP-tagged Mup1 or the indicated Mup1 alanine substitutions were grown to mid log phase in synthetic medium at 30°C and stimulated with 20 μg/ml methionine. Equal volumes of culture were harvested at the indicated time points after stimulation, and total cell lysates were prepared and analyzed by SDS–PAGE and immunoblot. G6PDH serves as a control for equal loading.

    Article Snippet: The frozen pellet was resuspended in 450 μl RIPA buffer (50 mM Tris HCl, pH 7.6, 150 mM NaCl, 20 mM NaF, 1 mM EDTA, 0.5 mM ethylene glycol tetraacetic acid) supplemented with 1 mM DTT, 1 mM PMSF, and cOmplete protease inhibitor (Sigma-Aldrich), and 20 mM N -ethylmaleimide.

    Techniques: Sequencing, Stable Transfection, Expressing, Marker, Mutagenesis, Fluorescence, Microscopy, SDS Page

    SH3 domains shuffling impacts Sla1 PPIs, cells growth in different stress conditions and clathrin-mediated endocytosis. A) Sla1 SH3-deleted or -shuffled PPIs as detected by DHFR-PCA. The color code represents PPI strength as detected by DHFR-PCA (PCA score). All PPIs were measured in quadruplicate. A is for Abp1 SH3 and * is for the reinsertion of the WT domain as control strains. A scaled cartoon of Sla1 is also illustrated. B) Cophenetic correlation for the similarity of Sla1 SH3-shuffled PPI clusters with the growth phenotype clusters. Empirical p-value obtained from data permutation is p = 0.00002. C) Representative fluorescence microscopy timeframe analysis of a yeast cell expressing WT Sla1-GFP. The calculated trajectories for every Sla1-GFP foci detected are shown. Cell membrane is delimited with a dashed line and each Sla1-GFP particle colors represent its position in time. D) Sla1-GFP particles average effective distance travelled towards the cell center through time. Sla1 SH3-deleted strains are shown. The proportion of events that are not completed yet is represented by the color transparency of the curves (+ represent the time point when 95% of foci have disassembled). E) Complete or incomplete Sla1-GFP endocytosis events are shown (average per cell) for Sla1 SH3-deleted strains. F) Representation of the linearity of Sla1-GFP particle trajectories for each SH3 deletion or shuffling. G) Sla1-GFP particle lifetime (in seconds) are shown for the same strains as in F). See also Data S5.

    Journal: bioRxiv

    Article Title: The specificity of SRC Homology 3 (SH3) domain interactions is modulated by their protein context in vivo

    doi: 10.1101/2020.05.18.103002

    Figure Lengend Snippet: SH3 domains shuffling impacts Sla1 PPIs, cells growth in different stress conditions and clathrin-mediated endocytosis. A) Sla1 SH3-deleted or -shuffled PPIs as detected by DHFR-PCA. The color code represents PPI strength as detected by DHFR-PCA (PCA score). All PPIs were measured in quadruplicate. A is for Abp1 SH3 and * is for the reinsertion of the WT domain as control strains. A scaled cartoon of Sla1 is also illustrated. B) Cophenetic correlation for the similarity of Sla1 SH3-shuffled PPI clusters with the growth phenotype clusters. Empirical p-value obtained from data permutation is p = 0.00002. C) Representative fluorescence microscopy timeframe analysis of a yeast cell expressing WT Sla1-GFP. The calculated trajectories for every Sla1-GFP foci detected are shown. Cell membrane is delimited with a dashed line and each Sla1-GFP particle colors represent its position in time. D) Sla1-GFP particles average effective distance travelled towards the cell center through time. Sla1 SH3-deleted strains are shown. The proportion of events that are not completed yet is represented by the color transparency of the curves (+ represent the time point when 95% of foci have disassembled). E) Complete or incomplete Sla1-GFP endocytosis events are shown (average per cell) for Sla1 SH3-deleted strains. F) Representation of the linearity of Sla1-GFP particle trajectories for each SH3 deletion or shuffling. G) Sla1-GFP particle lifetime (in seconds) are shown for the same strains as in F). See also Data S5.

    Article Snippet: The equivalent of fifty OD600 of cells were resuspended in ice cold yeast lysis buffer (10 mM Tris-HCl pH 7.4, 150 mM NaCl, 0.5 mM EDTA (Millipore Sigma), 1% triton X-100 (Millipore Sigma) and one cOmplete Mini Protease Inhibitor Cocktail (Millipore Sigma) per 10 mL) with 425–600 M glass beads (Millipore Sigma) and disrupted at 4°C by 10 cycles of 2 min vortexing and 2 min cooldown.

    Techniques: Fluorescence, Microscopy, Expressing

    Sla1 SH3 domain shuffling greatly alters its interactome in vivo with strong impacts on endocytosis. A) PPIs detected by DHFR-PCA relative to Sla1 WT for SH3-shuffling or -deletion per SH3 position. PPIs were measured in quadruplicate. B) Scaled cartoon representation of Sla1 and illustration of Sla1 function as an adaptor linking early proteins with the actin machinery in yeast clathrin-mediated endocytosis. C) PPIs of Sla1 SH3-shuffled or -deleted with partners implicated in clathrin-mediated endocytosis. Each PPI was assessed in quadruplicate by DHFR-PCA. The color code represents the strength of the PPIs detected by DHFR-PCA (PCA score). Sla1 1|2|3 represents the WT protein. D) Schematic representation of Sla1 foci assembled at the cell membrane and their movement toward the center of the cell during internalization before disassembly, in time. E) Representative fluorescence microscopy images of cells expressing different Sla1-GFP proteins at multiple time points. Foci from WT Sla1-GFP, the negative control D|D|D and a Sla1-GFP shuffle (3|1|2) are shown, in time. The first time frame is green and the others are red. A merge with the starting point is shown for each time frame. F) Average effective distance travelled by Sla1-GFP particles towards the centroid of the cell through time for WT Sla1 (1|2|3), SH3-deleted control or shuffled strains. Color transparency represents the proportion of events that are not completed yet that are used to calculate the average distance at the different time points. Plus signs (+) represent the moment in time when 95% of the foci have disassembled. G) Average number of complete or incomplete Sla1-GFP endocytosis events per cell is shown. See also Figure S5 and Data S5.

    Journal: bioRxiv

    Article Title: The specificity of SRC Homology 3 (SH3) domain interactions is modulated by their protein context in vivo

    doi: 10.1101/2020.05.18.103002

    Figure Lengend Snippet: Sla1 SH3 domain shuffling greatly alters its interactome in vivo with strong impacts on endocytosis. A) PPIs detected by DHFR-PCA relative to Sla1 WT for SH3-shuffling or -deletion per SH3 position. PPIs were measured in quadruplicate. B) Scaled cartoon representation of Sla1 and illustration of Sla1 function as an adaptor linking early proteins with the actin machinery in yeast clathrin-mediated endocytosis. C) PPIs of Sla1 SH3-shuffled or -deleted with partners implicated in clathrin-mediated endocytosis. Each PPI was assessed in quadruplicate by DHFR-PCA. The color code represents the strength of the PPIs detected by DHFR-PCA (PCA score). Sla1 1|2|3 represents the WT protein. D) Schematic representation of Sla1 foci assembled at the cell membrane and their movement toward the center of the cell during internalization before disassembly, in time. E) Representative fluorescence microscopy images of cells expressing different Sla1-GFP proteins at multiple time points. Foci from WT Sla1-GFP, the negative control D|D|D and a Sla1-GFP shuffle (3|1|2) are shown, in time. The first time frame is green and the others are red. A merge with the starting point is shown for each time frame. F) Average effective distance travelled by Sla1-GFP particles towards the centroid of the cell through time for WT Sla1 (1|2|3), SH3-deleted control or shuffled strains. Color transparency represents the proportion of events that are not completed yet that are used to calculate the average distance at the different time points. Plus signs (+) represent the moment in time when 95% of the foci have disassembled. G) Average number of complete or incomplete Sla1-GFP endocytosis events per cell is shown. See also Figure S5 and Data S5.

    Article Snippet: The equivalent of fifty OD600 of cells were resuspended in ice cold yeast lysis buffer (10 mM Tris-HCl pH 7.4, 150 mM NaCl, 0.5 mM EDTA (Millipore Sigma), 1% triton X-100 (Millipore Sigma) and one cOmplete Mini Protease Inhibitor Cocktail (Millipore Sigma) per 10 mL) with 425–600 M glass beads (Millipore Sigma) and disrupted at 4°C by 10 cycles of 2 min vortexing and 2 min cooldown.

    Techniques: In Vivo, Fluorescence, Microscopy, Expressing, Negative Control

    ZCCHC8 complete loss causes progressive and fatal neurodevelopmental phenotype. ( A , top row) Images showing head profile of Zcchc8 wild-type, heterozygous, and homozygous null mice (41–46 d-old). The labels show the genotype with a male ( left ) and a female ( right ) for each genotype. Zcchc8 −/− mice have abnormal head profiles with domed crania, as outlined by the dashed line. ( Middle row ) CT head mid-sagittal images show Zcchc8 −/− mice have dome-shaped crania. ( Bottom row). Volume-rendered (VR) CT images of mouse calvaria show widened cranial sutures in Zcchc8 −/− mice (seen in three of six imaged). None of Zcchc8 +/+ or Zcchc8 +/− mice (four mice imaged/genotype) had this feature. Each vertical image group is from the same mouse except the last column (two different females). ( B ) Representative H E coronal sections from 8-wk-old heads (all male) show no differences in Zcchc8 +/− mice (11 examined) compared with Zcchc8 +/+ mice (10 examined). In contrast, Zcchc8 −/− mice had severe ventricular dilation (nine of 11 examined). ( C ) E12.5 brain sections show Zcchc8 −/− have microcephaly but intact brain structures with no ventriculomegaly in utero. ( D ) Image of E12.5 embryos from a single dam showing expected Mendelian ratios but Zcchc8 −/− embryos have small crania. ( E ) Cranial area of newborn (P0) pups measured on VR CT images and corrected to left femur length on the same images ( Zcchc8 +/+ n = 7, 3M/4F; Zcchc8 +/− n = 10, 3M/7F; Zcchc8 −/− n = 4, 3M/1F). ( F ) Mean cranial area ± SEM relative to age for all three genotypes showing that Zcchc8 −/− mice develop macrocephy after birth. Newborn mice include those listed in E and older mice ( Zcchc8 +/+ , n = 4, 3M/1F; Zcchc8 +/− , n = 4, 3M/1F; Zcchc8 −/− , n = 5, 3M/2F). Dashed lines denote 95% confidence intervals. (**) P

    Journal: Genes & Development

    Article Title: ZCCHC8, the nuclear exosome targeting component, is mutated in familial pulmonary fibrosis and is required for telomerase RNA maturation

    doi: 10.1101/gad.326785.119

    Figure Lengend Snippet: ZCCHC8 complete loss causes progressive and fatal neurodevelopmental phenotype. ( A , top row) Images showing head profile of Zcchc8 wild-type, heterozygous, and homozygous null mice (41–46 d-old). The labels show the genotype with a male ( left ) and a female ( right ) for each genotype. Zcchc8 −/− mice have abnormal head profiles with domed crania, as outlined by the dashed line. ( Middle row ) CT head mid-sagittal images show Zcchc8 −/− mice have dome-shaped crania. ( Bottom row). Volume-rendered (VR) CT images of mouse calvaria show widened cranial sutures in Zcchc8 −/− mice (seen in three of six imaged). None of Zcchc8 +/+ or Zcchc8 +/− mice (four mice imaged/genotype) had this feature. Each vertical image group is from the same mouse except the last column (two different females). ( B ) Representative H E coronal sections from 8-wk-old heads (all male) show no differences in Zcchc8 +/− mice (11 examined) compared with Zcchc8 +/+ mice (10 examined). In contrast, Zcchc8 −/− mice had severe ventricular dilation (nine of 11 examined). ( C ) E12.5 brain sections show Zcchc8 −/− have microcephaly but intact brain structures with no ventriculomegaly in utero. ( D ) Image of E12.5 embryos from a single dam showing expected Mendelian ratios but Zcchc8 −/− embryos have small crania. ( E ) Cranial area of newborn (P0) pups measured on VR CT images and corrected to left femur length on the same images ( Zcchc8 +/+ n = 7, 3M/4F; Zcchc8 +/− n = 10, 3M/7F; Zcchc8 −/− n = 4, 3M/1F). ( F ) Mean cranial area ± SEM relative to age for all three genotypes showing that Zcchc8 −/− mice develop macrocephy after birth. Newborn mice include those listed in E and older mice ( Zcchc8 +/+ , n = 4, 3M/1F; Zcchc8 +/− , n = 4, 3M/1F; Zcchc8 −/− , n = 5, 3M/2F). Dashed lines denote 95% confidence intervals. (**) P

    Article Snippet: Total protein was isolated from cells in RIPA buffer (Cell Signaling Technology) with cOmplete Mini protease inhibitor (Sigma-Aldrich) and lysates were quantified using Pierce BCA protein assay kit (Thermo Fisher Scientific).

    Techniques: Mouse Assay, In Utero