Results 61 to 70 of about 109,885 (301)
A novel N-terminal extension in mitochondrial TRAP1 serves as a thermal regulator of chaperone activity. [PDF]
Hsp90 is a conserved chaperone that facilitates protein homeostasis. Our crystal structure of the mitochondrial Hsp90, TRAP1, revealed an extension of the N-terminal β-strand previously shown to cross between protomers in the closed state. In this study,
Agard, David A +5 more
core +2 more sources
The telomere environment requires an efficient means to assemble and disassemble a multitude of structures to operate correctly and to help achieve cellular homeostasis. Telomeres are challenged by a common binding specificity displayed by many of the protein components for telomeric DNA, which could result in competitive DNA interactions, and by a ...
Diane C, DeZwaan, Brian C, Freeman
openaire +2 more sources
Pancreatic neuroendocrine tumors frequently silence MEN1 through epigenetic mechanisms. Here, SIRT7 recruits DNMT1 to the MEN1 promoter, drives hypermethylation, and enhances DNA repair. Inhibiting SIRT7 restores MEN1, reduces MRN complex abundance, impairs double‐strand break repair, and sensitizes PanNET models to radiation, supporting SIRT7 as a ...
Jianyun Jiang +11 more
wiley +1 more source
Discovery of small molecule inhibitors of Leishmania braziliensis Hsp90 chaperone
Leishmaniasis is a neglected disease caused by the protozoa Leishmania ssp. Environmental differences found by the parasites in the vector and the host are translated into cellular stress, leading to the production of heat shock proteins (Hsp). These are
Fernanda A. H. Batista +7 more
doaj +1 more source
Hsp90 interaction with clients
The conserved Hsp90 chaperone is an ATP-controlled machine that assists the folding and controls the stability of select proteins. Emerging data explain how Hsp90 achieves client specificity and its role in the cellular chaperone cascade. Interestingly, Hsp90 has an extended substrate binding interface that crosses domain boundaries, exhibiting ...
Karagoz, Elif, Rüdiger, Stefan G D
openaire +3 more sources
Heat shock protein 90 (Hsp90) is a highly conserved molecular chaperone that assists in the maturation of many client proteins involved in cellular signal transduction. As a regulator of cellular signaling processes, it is vital for the maintenance of cellular proteostasis and adaptation to environmental stresses.
openaire +3 more sources
Environmental cadmium exposure disrupts testicular homeostasis through a novel intercellular communication axis. Stressed Sertoli cells release extracellular vesicles carrying damage‐associated molecular patterns and mitochondrial fragments, which activate macrophages via TLR4/NF‐κB signaling.
Jianfeng Ma +17 more
wiley +1 more source
Protein phosphatase 5 regulates titin phosphorylation and function at a sarcomere-associated mechanosensor complex in cardiomyocytes. [PDF]
Serine/threonine protein phosphatase 5 (PP5) is ubiquitously expressed in eukaryotic cells; however, its function in cardiomyocytes is unknown. Under basal conditions, PP5 is autoinhibited, but enzymatic activity rises upon binding of specific factors ...
Beckendorf, Lisa +10 more
core +3 more sources
The Cell-Cycle Regulatory Protein p21CIP1/WAF1 Is Required for Cytolethal Distending Toxin (Cdt)-Induced Apoptosis. [PDF]
The Aggregatibacter actinomycetemcomitans cytolethal distending toxin (Cdt) induces lymphocytes to undergo cell-cycle arrest and apoptosis; toxicity is dependent upon the active Cdt subunit, CdtB.
Boesze-Battaglia, Kathleen +4 more
core +2 more sources
Mechanisms of Hsp90 regulation [PDF]
Heat shock protein 90 (Hsp90) is a molecular chaperone that is involved in the activation of disparate client proteins. This implicates Hsp90 in diverse biological processes that require a variety of co-ordinated regulatory mechanisms to control its activity.
openaire +3 more sources

