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ATCC yeast extract peptone dextrose ypd medium
Yeast Extract Peptone Dextrose Ypd Medium, supplied by ATCC, used in various techniques. Bioz Stars score: 98/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Formedium growth medium ypd
Growth Medium Ypd, supplied by Formedium, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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ypd  (Difco)
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Difco ypd
Ypd, supplied by Difco, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Formedium yeast extract peptone dextrose ypd medium
Yeast Extract Peptone Dextrose Ypd Medium, supplied by Formedium, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Liofilchem ypd medium plates
Ypd Medium Plates, supplied by Liofilchem, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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86
Bacto Laboratories yeast extract peptone dextrone ypd
(a) Simplified model of the Hsp90 folding pathway. Client (dark gray oval) bound to a chaperone such as Cdc37 (light gray diamond) is targeted to the open conformation of Hsp90 (gray). After ATP binds, Hsp90 shifts to the closed conformation. ATP hydrolysis is associated with a return to the open conformation. The Hsc82-G309S and Cdc37-S14A mutants target early steps in the pathway associated with client loading (1, loading). The Hsc82-Q380K mutant targets reopening (2), and the G424D mutant targets an unknown step in the pathway (other). (b) Growth of yeast strains after 2 days at the indicated temperature on <t>YPD</t> media. ATP, adenosine triphosphate; YPD, yeast extract peptone <t>dextrone.</t>
Yeast Extract Peptone Dextrone Ypd, supplied by Bacto Laboratories, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Qingdao Hope Bio ypd medium
(a) Simplified model of the Hsp90 folding pathway. Client (dark gray oval) bound to a chaperone such as Cdc37 (light gray diamond) is targeted to the open conformation of Hsp90 (gray). After ATP binds, Hsp90 shifts to the closed conformation. ATP hydrolysis is associated with a return to the open conformation. The Hsc82-G309S and Cdc37-S14A mutants target early steps in the pathway associated with client loading (1, loading). The Hsc82-Q380K mutant targets reopening (2), and the G424D mutant targets an unknown step in the pathway (other). (b) Growth of yeast strains after 2 days at the indicated temperature on <t>YPD</t> media. ATP, adenosine triphosphate; YPD, yeast extract peptone <t>dextrone.</t>
Ypd Medium, supplied by Qingdao Hope Bio, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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ypd  (ATCC)
96
ATCC ypd
(a) Simplified model of the Hsp90 folding pathway. Client (dark gray oval) bound to a chaperone such as Cdc37 (light gray diamond) is targeted to the open conformation of Hsp90 (gray). After ATP binds, Hsp90 shifts to the closed conformation. ATP hydrolysis is associated with a return to the open conformation. The Hsc82-G309S and Cdc37-S14A mutants target early steps in the pathway associated with client loading (1, loading). The Hsc82-Q380K mutant targets reopening (2), and the G424D mutant targets an unknown step in the pathway (other). (b) Growth of yeast strains after 2 days at the indicated temperature on <t>YPD</t> media. ATP, adenosine triphosphate; YPD, yeast extract peptone <t>dextrone.</t>
Ypd, supplied by ATCC, used in various techniques. Bioz Stars score: 96/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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86
Formedium ypd medium
A) Representative immunoblots showing turnover of mNeonGreen-tGnd1-HA following 90 min of acute starvation (0.02% glucose) or in glucose-replete control medium (2% glucose). Protein stability was monitored by cycloheximide chase assay (100 µg/mL) at the indicated time points. Total protein loading was visualized and normalized using Stain-Free technology. Graphs represent mNG-tGnd1-HA protein levels as a percentage of the protein present at the time point 0 min. Data are presented as average ± SD from 2 independent experiments. B) Representative confocal fluorescence microscopy images logarithmically growing <t>S.</t> <t>cerevisiae</t> expressing mNeonGreen-tGnd1-HA, which were cultured in glucose-replete (2%) or glucose-deprived (0.02%) media for 90 min, followed by CHX chase (0 and 60 min) prior to fixation and imaging. Images represent maximum intensity projections of Z-stacks. Scale bar, 10 µ m. The bar chart shows the percentage of cells in the culture that contain inclusions, along with the distribution of cells harboring one and two or more inclusions. Data are presented as average ± SD from 2 independent experiments. C) Representative immunoblots showing turnover of mNeonGreen-stGnd1-HA after 90 min acute starvation (0.02% glucose) or control medium (2% glucose), assessed by cycloheximide chase assay (100 µg/mL) at indicated times (0, 60 min). Total protein loading was visualized using Stain-Free technology. Graphs represent mNG-stGnd1-protein levels as a percentage of the protein present at the time point 0 min, with average values and standard deviation (n = 2). D) Representative confocal fluorescence microscopy images of log-phase yeast cells expressing mNeonGreen-stGnd1-HA under glucose-rich <t>YPD</t> (2%) or glucose-deprived (0.02%) conditions for 90 min. Images represent maximum intensity projections of Z-stacks. Scale bar, 10 µ m.
Ypd Medium, supplied by Formedium, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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99
Beijing Solarbio Science ypd liquid medium
A) Representative immunoblots showing turnover of mNeonGreen-tGnd1-HA following 90 min of acute starvation (0.02% glucose) or in glucose-replete control medium (2% glucose). Protein stability was monitored by cycloheximide chase assay (100 µg/mL) at the indicated time points. Total protein loading was visualized and normalized using Stain-Free technology. Graphs represent mNG-tGnd1-HA protein levels as a percentage of the protein present at the time point 0 min. Data are presented as average ± SD from 2 independent experiments. B) Representative confocal fluorescence microscopy images logarithmically growing <t>S.</t> <t>cerevisiae</t> expressing mNeonGreen-tGnd1-HA, which were cultured in glucose-replete (2%) or glucose-deprived (0.02%) media for 90 min, followed by CHX chase (0 and 60 min) prior to fixation and imaging. Images represent maximum intensity projections of Z-stacks. Scale bar, 10 µ m. The bar chart shows the percentage of cells in the culture that contain inclusions, along with the distribution of cells harboring one and two or more inclusions. Data are presented as average ± SD from 2 independent experiments. C) Representative immunoblots showing turnover of mNeonGreen-stGnd1-HA after 90 min acute starvation (0.02% glucose) or control medium (2% glucose), assessed by cycloheximide chase assay (100 µg/mL) at indicated times (0, 60 min). Total protein loading was visualized using Stain-Free technology. Graphs represent mNG-stGnd1-protein levels as a percentage of the protein present at the time point 0 min, with average values and standard deviation (n = 2). D) Representative confocal fluorescence microscopy images of log-phase yeast cells expressing mNeonGreen-stGnd1-HA under glucose-rich <t>YPD</t> (2%) or glucose-deprived (0.02%) conditions for 90 min. Images represent maximum intensity projections of Z-stacks. Scale bar, 10 µ m.
Ypd Liquid Medium, supplied by Beijing Solarbio Science, used in various techniques. Bioz Stars score: 99/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Image Search Results


(a) Simplified model of the Hsp90 folding pathway. Client (dark gray oval) bound to a chaperone such as Cdc37 (light gray diamond) is targeted to the open conformation of Hsp90 (gray). After ATP binds, Hsp90 shifts to the closed conformation. ATP hydrolysis is associated with a return to the open conformation. The Hsc82-G309S and Cdc37-S14A mutants target early steps in the pathway associated with client loading (1, loading). The Hsc82-Q380K mutant targets reopening (2), and the G424D mutant targets an unknown step in the pathway (other). (b) Growth of yeast strains after 2 days at the indicated temperature on YPD media. ATP, adenosine triphosphate; YPD, yeast extract peptone dextrone.

Journal: Cell Stress & Chaperones

Article Title: Comparative analysis of the impact of Heat shock protein 90 kDa or Cdc37 mutation on the yeast proteome

doi: 10.1016/j.cstres.2026.100164

Figure Lengend Snippet: (a) Simplified model of the Hsp90 folding pathway. Client (dark gray oval) bound to a chaperone such as Cdc37 (light gray diamond) is targeted to the open conformation of Hsp90 (gray). After ATP binds, Hsp90 shifts to the closed conformation. ATP hydrolysis is associated with a return to the open conformation. The Hsc82-G309S and Cdc37-S14A mutants target early steps in the pathway associated with client loading (1, loading). The Hsc82-Q380K mutant targets reopening (2), and the G424D mutant targets an unknown step in the pathway (other). (b) Growth of yeast strains after 2 days at the indicated temperature on YPD media. ATP, adenosine triphosphate; YPD, yeast extract peptone dextrone.

Article Snippet: Yeast were transformed by lithium acetate methods and were grown in either yeast extract peptone dextrone (YPD) (1% Bacto yeast extract, 2% peptone, and 2% dextrose) or defined synthetic complete media supplemented with 2% dextrose.

Techniques: Mutagenesis

A) Representative immunoblots showing turnover of mNeonGreen-tGnd1-HA following 90 min of acute starvation (0.02% glucose) or in glucose-replete control medium (2% glucose). Protein stability was monitored by cycloheximide chase assay (100 µg/mL) at the indicated time points. Total protein loading was visualized and normalized using Stain-Free technology. Graphs represent mNG-tGnd1-HA protein levels as a percentage of the protein present at the time point 0 min. Data are presented as average ± SD from 2 independent experiments. B) Representative confocal fluorescence microscopy images logarithmically growing S. cerevisiae expressing mNeonGreen-tGnd1-HA, which were cultured in glucose-replete (2%) or glucose-deprived (0.02%) media for 90 min, followed by CHX chase (0 and 60 min) prior to fixation and imaging. Images represent maximum intensity projections of Z-stacks. Scale bar, 10 µ m. The bar chart shows the percentage of cells in the culture that contain inclusions, along with the distribution of cells harboring one and two or more inclusions. Data are presented as average ± SD from 2 independent experiments. C) Representative immunoblots showing turnover of mNeonGreen-stGnd1-HA after 90 min acute starvation (0.02% glucose) or control medium (2% glucose), assessed by cycloheximide chase assay (100 µg/mL) at indicated times (0, 60 min). Total protein loading was visualized using Stain-Free technology. Graphs represent mNG-stGnd1-protein levels as a percentage of the protein present at the time point 0 min, with average values and standard deviation (n = 2). D) Representative confocal fluorescence microscopy images of log-phase yeast cells expressing mNeonGreen-stGnd1-HA under glucose-rich YPD (2%) or glucose-deprived (0.02%) conditions for 90 min. Images represent maximum intensity projections of Z-stacks. Scale bar, 10 µ m.

Journal: bioRxiv

Article Title: Proteasome-dependent degradation and nucleus–vacuole junctions sustain proteostasis during acute glucose starvation

doi: 10.64898/2026.04.22.720209

Figure Lengend Snippet: A) Representative immunoblots showing turnover of mNeonGreen-tGnd1-HA following 90 min of acute starvation (0.02% glucose) or in glucose-replete control medium (2% glucose). Protein stability was monitored by cycloheximide chase assay (100 µg/mL) at the indicated time points. Total protein loading was visualized and normalized using Stain-Free technology. Graphs represent mNG-tGnd1-HA protein levels as a percentage of the protein present at the time point 0 min. Data are presented as average ± SD from 2 independent experiments. B) Representative confocal fluorescence microscopy images logarithmically growing S. cerevisiae expressing mNeonGreen-tGnd1-HA, which were cultured in glucose-replete (2%) or glucose-deprived (0.02%) media for 90 min, followed by CHX chase (0 and 60 min) prior to fixation and imaging. Images represent maximum intensity projections of Z-stacks. Scale bar, 10 µ m. The bar chart shows the percentage of cells in the culture that contain inclusions, along with the distribution of cells harboring one and two or more inclusions. Data are presented as average ± SD from 2 independent experiments. C) Representative immunoblots showing turnover of mNeonGreen-stGnd1-HA after 90 min acute starvation (0.02% glucose) or control medium (2% glucose), assessed by cycloheximide chase assay (100 µg/mL) at indicated times (0, 60 min). Total protein loading was visualized using Stain-Free technology. Graphs represent mNG-stGnd1-protein levels as a percentage of the protein present at the time point 0 min, with average values and standard deviation (n = 2). D) Representative confocal fluorescence microscopy images of log-phase yeast cells expressing mNeonGreen-stGnd1-HA under glucose-rich YPD (2%) or glucose-deprived (0.02%) conditions for 90 min. Images represent maximum intensity projections of Z-stacks. Scale bar, 10 µ m.

Article Snippet: To investigate the cellular response to acute glucose starvation, yeast Saccharomyces cerevisiae cultures were grown in rich YPD medium (1% (w/v) yeast extract, 2% (w/v) peptone, and 2% (w/v) D-glucose; Formedium Ltd.).

Techniques: Western Blot, Control, Staining, Fluorescence, Microscopy, Expressing, Cell Culture, Imaging, Standard Deviation

A) Representative confocal fluorescence microscopy images of log-phase yeast cells expressing HA-mNG-NBD2* under glucose-rich YPD (2%) or glucose-deprived (0.02%) conditions for 90 min. Images represent maximum intensity projections of Z-stacks. Scale bar, 10 µ m. The bar chart depicts the proportion of cells in the culture that contain inclusions. Data are expressed as mean ± SD from two independent experiments. B) Representative immunoblots showing turnover of the model misfolded protein HA-mNG-NBD2*. Log-phase yeast cells were subjected to 90 min acute glucose starvation (0.02% glucose) or control 2% glucose YPD medium, followed by cycloheximide chase assay (100 µ g/mL) at the indicated time points. Total protein loading was visualized using Stain-Free technology.

Journal: bioRxiv

Article Title: Proteasome-dependent degradation and nucleus–vacuole junctions sustain proteostasis during acute glucose starvation

doi: 10.64898/2026.04.22.720209

Figure Lengend Snippet: A) Representative confocal fluorescence microscopy images of log-phase yeast cells expressing HA-mNG-NBD2* under glucose-rich YPD (2%) or glucose-deprived (0.02%) conditions for 90 min. Images represent maximum intensity projections of Z-stacks. Scale bar, 10 µ m. The bar chart depicts the proportion of cells in the culture that contain inclusions. Data are expressed as mean ± SD from two independent experiments. B) Representative immunoblots showing turnover of the model misfolded protein HA-mNG-NBD2*. Log-phase yeast cells were subjected to 90 min acute glucose starvation (0.02% glucose) or control 2% glucose YPD medium, followed by cycloheximide chase assay (100 µ g/mL) at the indicated time points. Total protein loading was visualized using Stain-Free technology.

Article Snippet: To investigate the cellular response to acute glucose starvation, yeast Saccharomyces cerevisiae cultures were grown in rich YPD medium (1% (w/v) yeast extract, 2% (w/v) peptone, and 2% (w/v) D-glucose; Formedium Ltd.).

Techniques: Fluorescence, Microscopy, Expressing, Western Blot, Control, Staining