Results 31 to 40 of about 58,138 (243)
Heat-shock protein 90 (HSP90) is a highly active molecular chaperone that plays a crucial role in cellular function. It facilitates the folding, assembly and stability of various oncogenic proteins, particularly kinases and transcription factors involved
Liqing Huang +9 more
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SERUM HSP 90 LEVELS OF CHRONIC HEPATITIS B PATIENTS ARE SUBSTANTIALLY CORRELATED WITH HBV DNA VIRAL LOAD [PDF]
The highly conserved molecules that make up the mammalian HSP90 family of proteins are engaged in a wide range of cellular functions. HSP90 and its co-chaperones regulate vital physiological processes as apoptosis, hormone signaling, and cell cycle ...
Awaz A. Saadi
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ABSTRACT Brown and beige adipocytes dissipate energy as heat, yet effective strategies to enhance their mitochondrial efficiency remain limited. Here, we identify Agnuside (AGN) as a selective stabilizer of the complex I assembly factor NDUFAF6. AGN directly binds cytosolic NDUFAF6, suppresses its ubiquitination, prolongs its half‐life, and facilitates
Qingwen Zhao +7 more
wiley +1 more source
FLEXR-MSA: electron-density map comparisons of sequence-diverse structures
Proteins with near-identical sequences often share similar static structures. Yet, comparing crystal structures is limited or even biased by what has been included or omitted in the deposited model.
Timothy R. Stachowski, Marcus Fischer
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Overexpression of heat shock protein 90 (Hsp90) is common in various types of cancer. In cutaneous melanoma, a cancer with one of the high levels of Hsp90 overexpression, such expression was correlated with a panel of protein kinases, thus offering an ...
Feifei Qin +8 more
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Heat shock protein 90 (HSP90) possesses critical functions in plant developmental control and defense reactions. The HSP90 gene family has been studied in various plant species.
Kaijing Zhang +6 more
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Nitrosyl heme emerges as an extracellular nitrodilator that dilates arteries without crossing the cell membrane. Instead, heme‐NO mobilizes NO moieties from a preformed intracellular NO store within vascular smooth muscle, providing both functional and chemical evidence for the NANOS model, revealing a previously unrecognized mechanism of arterial ...
Taiming Liu +9 more
wiley +1 more source
Targeting Plasmodium falciparum Hsp90: Towards Reversing Antimalarial Resistance
Malaria continues to exact a great human toll in tropical settings. Antimalarial resistance is rife and the parasite inexorably develops mechanisms to outwit our best drugs, including the now first-line choice, artesunate.
Dea Shahinas +2 more
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In this study, chemoproteomics combined with genetic and functional analyses was integrated to identify SHMT2 as a covalent and functional target of gambogic acid (GA) in triple‐negative breast cancer (TNBC). Further validation demonstrated that GA selectively modifies the Cys241 site of SHMT2, triggering mitochondrial dysfunction, activating the Nrf2 ...
Tong Yang +15 more
wiley +1 more source
Regulation of the Hsp90 system
Hsp90 is a highly conserved and abundant chaperone. It participates in essential cellular activities by supporting the maturation process of its client proteins, many of which are protein kinases and steroid receptors. Client processing is achieved via extensive conformational changes within the dimeric chaperone.
Siyuan, Sima, Klaus, Richter
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