Results 121 to 130 of about 94,343 (283)
The integration of ROS‐generating systems with H2S depletion strategies effectively overcomes the limitations imposed by endogenous antioxidant defenses on ROS‐based antimicrobial therapies. In this study, the Cu‐MOF is incorporated into pillararene‐embedded COF, achieving a “three‐in‐one” antimicrobial effect that markedly alleviated periodontal ...
Shuang Liang +9 more
wiley +1 more source
In biological systems, molecular assembly primarily relies on the assistance of molecular chaperones. Inspired by nature, strategies like ‘chaperone‐assisted assembly’ and ‘catalyzed assembly’ have been proposed for the sophisticated control of molecular
Wang Li +10 more
doaj +1 more source
SIRT6‐mediated ATF3 acetylation drives MGARP transcription and mitochondrial dysfunction in macrophages, promoting macrophage senescence and pulmonary fibrosis. Mechanistically, HSP70/Importin α competitively binds to ATF3, modulating its nuclear translocation.
Demin Cheng +18 more
wiley +1 more source
The known unknowns of the Hsp90 chaperone
Molecular chaperones are vital proteins that maintain protein homeostasis by assisting in protein folding, activation, degradation, and stress protection. Among them, heat-shock protein 90 (Hsp90) stands out as an essential proteostasis hub in eukaryotes,
Laura-Marie Silbermann +3 more
doaj +1 more source
Heat Shock Protein 90: From Molecular Chaperone Function to Therapeutic Targeting in Malignancies
In this review, an integrated conceptual framework linking HSP90's molecular chaperone functions to its pathological roles in cancer is proposed. HSP90 serves as a central node that integrates oncogenic signaling, buffers proteotoxic stress, maintains cancer stem cell plasticity, and shapes tumor‐immune interactions, all of which converge to drive ...
Beibei Zhang +4 more
wiley +1 more source
Chaperone dependency during biogenesis does not correlate with chaperone dependency during refolding
Many proteins require molecular chaperones to fold into their functional native forms. However, the roles of chaperones during primary biogenesis in vivo can differ from the functions they play during in vitro refolding experiments.
Divya Yadav +3 more
doaj +1 more source
Ubiquilin (UBQLN), like many other human proteins, contains both well‐folded and disordered regions. Here, we show that intramolecular interactions between disordered regions and folded domains modulate between open and closed topologies of UBQLN proteins, altering their structure and function.
Jessica K. Niblo +4 more
wiley +1 more source
CCT2 Promotes Prostate Cancer Progression Through EIF3F‐Dependent Stabilization of FASN
ABSTRACT Prostate cancer (PCa) is increasingly recognized to be driven by dysregulated lipid metabolism. Although fatty acid synthase (FASN) is highly expressed in PCa, the mechanisms governing FASN protein stability and its functional integration into oncogenic lipid metabolism remain poorly defined.
Shun Xu +13 more
wiley +1 more source
PDIA6–SCD1 Axis Rewires Lipid Metabolism to Drive Gastric Cancer Progression
Protein disulfide isomerase A6 (PDIA6) is identified as an oncogenic driver in gastric cancer. PDIA6 directly binds and stabilizes SCD1 by limiting its ubiquitin–proteasome‐mediated degradation, thereby sustaining monounsaturated fatty acid (MUFA)‐enriched lipid homeostasis and lipid metabolic reprogramming.
Zhen Tian +13 more
wiley +1 more source
The role of molecular chaperones in the mechanisms of epileptogenesis. [PDF]
Davletshin AI +4 more
europepmc +1 more source

