Results 41 to 50 of about 58,138 (243)
Advanced Science, EarlyView.Molecular, genetic, virological, and biochemical analysis in combination with global proteome and phosphoproteome profiling and functional assays were applied to study the role of PR130 in the context of HSV‐1 replication. The observations reveal that host‐intrinsic mechanisms regulate HSV‐1 replication and highlight PR130 as a susceptibility factor of
Johannes Jungwirth +10 more
wiley +1 more source
Autoimmunity, 1994 The heat shock proteins are a group of evolutionarily conserved proteins with important physiological functions, whose synthesis is enhanced by elevated temperature or other stresses. A role for one or more of these proteins in human autoimmune disease has been extensively discussed.
D S, Latchman, D A, Isenberg
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Advanced Science, EarlyView.This study reveals the dual role of celecoxib in intervertebral disc degeneration. While low concentrations are protective, high concentrations induce toxicity by upregulating HSP90, which synergizes with USP15 to deubiquitinate and stabilize RBX1. This leads to degradation of COMMD1/ATP7B, copper dyshomeostasis, and ultimately, cuproptosis.
Youfeng Guo +11 more
wiley +1 more source
Trends in Biochemical Sciences, 2010 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
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Discovery of small molecule inhibitors of Leishmania braziliensis Hsp90 chaperone
Journal of Enzyme Inhibition and Medicinal Chemistry, 2020 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
NMI Regulates Adipose Adaptive Thermogenesis Through TLR4/IRF3 Signaling to Promote Obesity
Advanced Science, EarlyView.Adipose tissue‐derived NMI is secreted under metabolic stress and suppresses adaptive thermogenesis through TLR4/IRF3 signaling, repressing the PPARα/PGC‐1α/UCP1 thermogenic transcriptional program. Genetic ablation or anti ‐ NMI monoclonal antibody treatment enhances energy expenditure, protects against DIO, and ameliorates adipose tissue inflammation,
Ting‐Ting Li +7 more
wiley +1 more source
Hsp90 interaction with clients
Trends in Biochemical Sciences, 2015 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
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Biomolecules, 2023 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.
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Advanced Science, EarlyView.Umbilical cord stem cell‐derived exosomes encapsulated in an immunomodulatory bioadhesive hydrogel spray enable localized therapy, sustained vesicle delivery, macrophage polarization, suppress systemic inflammation, and mitigate glucose and insulin homeostasis impairments in MAFLD.
Triya Saha +4 more
wiley +1 more source
Mechanisms of Hsp90 regulation [PDF]
Biochemical Journal, 2016 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.
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