Hsp31 Is a Stress Response Chaperone That Intervenes in the Protein Misfolding Process
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Schizosaccharomyces pombe Homologs of Human DJ-1 Are Stationary Phase-Associated Proteins That Are Involved in Autophagy and Oxidative Stress ResistanceStructural and biochemical studies on Vibrio cholerae Hsp31 reveals a novel dimeric form and Glutathione-independent Glyoxalase activity.Hsp31, a member of the DJ-1 superfamily, is a multitasking stress responder with chaperone activity.Methylglyoxal detoxification by a DJ-1 family protein provides dual abiotic and biotic stress tolerance in transgenic plants.The small heat shock protein Hsp31 cooperates with Hsp104 to modulate Sup35 prion aggregation.Randomized CRISPR-Cas Transcriptional Perturbation Screening Reveals Protective Genes against Alpha-Synuclein Toxicity.Oxidative stress triggers aggregation of GFP-tagged Hsp31p, the budding yeast environmental stress response chaperone, and glyoxalase III.
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Hsp31 Is a Stress Response Chaperone That Intervenes in the Protein Misfolding Process
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Hsp31 Is a Stress Response Chaperone That Intervenes in the Protein Misfolding Process
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Hsp31 Is a Stress Response Chaperone That Intervenes in the Protein Misfolding Process
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Hsp31 Is a Stress Response Chaperone That Intervenes in the Protein Misfolding Process
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Hsp31 Is a Stress Response Chaperone That Intervenes in the Protein Misfolding Process
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Hsp31 Is a Stress Response Chaperone That Intervenes in the Protein Misfolding Process
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Hsp31 Is a Stress Response Chaperone That Intervenes in the Protein Misfolding Process
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P2093
P2860
P356
P1476
Hsp31 Is a Stress Response Chaperone That Intervenes in the Protein Misfolding Process
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P2093
Chai-Jui Tsai
Holli M Drendel
Jean-Christophe Rochet
Josephat M Asiago
Kiran Aslam
Kourtney M Goode
Lake N Paul
P2860
P304
24816-24834
P356
10.1074/JBC.M115.678367
P407
P577
2015-08-25T00:00:00Z