Results 41 to 50 of about 76,334 (253)

Towards allosteric modulators of Hsp90

open access: yes, 2014
Hsp90 is an established anti-apoptotic target in cancer therapy.1 Most of the known small-molecule inhibitors that have shown potent antitumor activity target the Hsp90 N-terminal domain and directly inhibit its ATP-ase activity.2 However, many of these
A. Bernardi   +6 more
core   +2 more sources

Silence of STAT3 Enhances SNX-2112-induced Apoptosis of Esophageal Cancer Stem Cells

open access: yesZhongliu Fangzhi Yanjiu, 2019
Objective To investigate the effect of STAT3 silence on SNX-2112-induced apoptosis of esophageal cancer stem cells. Methods shSTAT3 lentiviral vector was designed and constructed. Esophageal cancer stem cells were transfected with shSTAT3 vector and then
XU Dandan, CHEN Suhong, WANG Ying
doaj   +1 more source

Partial depletion of plasminogen activator inhibitor‐1 decreases subcutaneous fat cell hypertrophy and liver cholesterol in high‐fat‐fed female mice

open access: yesFEBS Letters, EarlyView.
Obesity raises blood levels of PAI‐1, a protein linked to metabolic dysfunction‐associated steatotic liver disease in people with obesity. In female mice fed a high‐fat diet, partially lowering PAI‐1 led to smaller subcutaneous fat cells and lower liver cholesterol, without changing body weight or insulin sensitivity.
Claudia E. Ramirez Bustamante   +10 more
wiley   +1 more source

Heat shock protein-90-alpha, a prolactin-STAT5 target gene identified in breast cancer cells, is involved in apoptosis regulation [PDF]

open access: yes, 2008
Introduction The prolactin-Janus-kinase-2-signal transducer and activator of transcription-5 (JAK2-STAT5) pathway is essential for the development and functional differentiation of the mammary gland.
Liu, R.   +26 more
core   +2 more sources

Novel starting points for fragment-based drug design against human heat-shock protein 90 identified using crystallographic fragment screening

open access: yesIUCrJ
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
doaj   +1 more source

Design of Disruptors of the Hsp90–Cdc37 Interface

open access: yesMolecules, 2020
The molecular chaperone Hsp90 is a ubiquitous ATPase-directed protein responsible for the activation and structural stabilization of a large clientele of proteins.
Ilda D’Annessa   +10 more
doaj   +1 more source

Membrane composition and thermodynamic identity as boundaries of life for synthetic cell research

open access: yesFEBS Letters, EarlyView.
What makes a cell a cell? The boundary of a living cell is not just a wall. Read as a Markov blanket, the membrane separates internal from external states, generating identity and non‐equilibrium order. Can this identity be rebuilt from scratch in a synthetic cell?
Caterina Presutti, Bert Poolman
wiley   +1 more source

Hsp90-Induced Evolution: Adaptationist, Neutralist, and Developmentalist Scenarios [PDF]

open access: yes, 2008
Recent work on the heat-shock protein Hsp90 by Rutherford and Lindquist (1998) has been included among the pieces of evidence taken to show the essential role of developmental processes in evolution; Hsp90 acts as a buffer against phenotypic variation ...
Millstein, Roberta L.
core  

FLEXR-MSA: electron-density map comparisons of sequence-diverse structures

open access: yesIUCrJ
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
doaj   +1 more source

SERUM HSP 90 LEVELS OF CHRONIC HEPATITIS B PATIENTS ARE SUBSTANTIALLY CORRELATED WITH HBV DNA VIRAL LOAD [PDF]

open access: yesEuromediterranean Biomedical Journal
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
doaj   +1 more source

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