Results 41 to 50 of about 140,081 (117)
Background: Mycobacterial α-crystallin (Acr) is a chaperone that prevents misfolding of proteins when Mycobacterium tuberculosis is found in a latent form in the host tissue. Methods: Using insulin as a model substrate and utilizing polynomial graphs, we
Gautam Krishnan, Utpal Roy
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Regulation of Protein Transport Pathways by the Cytosolic Hsp90s
The highly conserved molecular chaperone heat shock protein 90 (Hsp90) is well-known for maintaining metastable proteins and mediating various aspects of intracellular protein dynamics. Intriguingly, high-throughput interactome studies suggest that Hsp90
Anna G. Mankovich, Brian C. Freeman
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Targeting the Hsp90-Cdc37-client protein interaction to disrupt Hsp90 chaperone machinery
Heat shock protein 90 (Hsp90) is a critical molecular chaperone protein that regulates the folding, maturation, and stability of a wide variety of proteins.
Ting Li +3 more
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Background HSPs (Heat shock proteins) are highly conserved ubiquitous proteins among species which are involved in maintaining appropriate folding and conformation of other proteins and are thus referred to as molecular chaperones.
Bisaria Virendra S +6 more
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Hsp70- and Hsp90-mediated proteasomal degradation underlies TPIsugarkill pathogenesis in Drosophila
Triosephosphate isomerase (TPI) deficiency is a severe glycolytic enzymopathy that causes progressive locomotor impairment and neurodegeneration, susceptibility to infection, and premature death. The recessive missense TPIsugarkill mutation in Drosophila
Stacy L. Hrizo, Michael J. Palladino
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Advances in the structures, mechanisms and targeting of molecular chaperones
Molecular chaperones, a class of complex client regulatory systems, play significant roles in the prevention of protein misfolding and abnormal aggregation, the modulation of protein homeostasis, and the protection of cells from damage under constantly ...
Jinying Gu +8 more
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Dr Len Neckers played a pioneering role in establishing that HSP90 is regulated by post-translational modifications (PTMs), fundamentally reshaping how molecular chaperones are understood. This insight laid the foundation for what has become known as the
Chander S. Digwal +2 more
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Loss of proteostasis and cellular senescence are key hallmarks of aging, but direct cause-effect relationships are not well understood. We show that most yeast cells arrest in G1 before death with low nuclear levels of Cln3, a key G1 cyclin extremely ...
David F Moreno +5 more
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Peptide substrate identification for yeast Hsp40 Ydj1 by screening the phage display library
We have identified a peptide substrate for molecular chaperone Hsp40 Ydj1 by utilizing the combination of phage display library screening and isothemol titration calirimetry (ITC).
Li Jingzhi, Sha Bingdong
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Redox‐Dependent Chaperoning of GBF1 Condensates Regulates Seed Germination in Arabidopsis
Reactive oxygen species (ROS) are pivotal signals that trigger the transition from seed dormancy to germination, yet the molecular link between ROS and transcriptional regulation has remained unclear. Here, we uncover a redox‐dependent mechanism focusing
Yunying Wang, Xiaofeng Fang
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