Results 41 to 50 of about 109,885 (301)

Therapeutic Potential of Heat Shock Protein 90 Inhibitors, Geldanamycin, and Analog Compounds in Precision Cancer Therapy

open access: yesBioMed Target Journal, 2023
Heat shock protein (HSP90) is a molecular chaperone involved in numerous physiological processes. The primary role of this is to assist in the process of protein folding and to restore misfolded proteins to their correct shape.
Atta Mohammed Alzebari   +3 more
doaj   +1 more source

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

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

Mutation of the co-chaperone Tsc1 in bladder cancer diminishes Hsp90 acetylation and reduces drug sensitivity and selectivity [PDF]

open access: yes, 2019
The molecular chaperone Heat shock protein 90 (Hsp90) is essential for the folding, stability, and activity of several drivers of oncogenesis. Hsp90 inhibitors are currently under clinical evaluation for cancer treatment, however their efficacy is ...
Backe, Sarah J   +11 more
core   +1 more source

The HSP90 complex of plants

open access: yesBiochimica et Biophysica Acta (BBA) - Molecular Cell Research, 2012
Heat shock protein 90 (HSP90) is a highly conserved and essential molecular chaperone involved in maturation and activation of signaling proteins in eukaryotes. HSP90 operates as a dimer in a conformational cycle driven by ATP binding and hydrolysis. HSP90 often functions together with co-chaperones that regulate the conformational cycle and/or load a ...
Kadota, Yasuhiro, Shirasu, Ken
openaire   +2 more sources

Engineering of Glioblastoma‐Derived Biomimetic Vesicles and Their Structural and Molecular Features

open access: yesAdvanced Healthcare Materials, EarlyView.
ABSTRACT Biomimetic nanosystems and vesicles have arisen as a novel approach to design vesicular transport systems with diverse therapeutic potential. The ‘biomimetic’ strategy involves the integration of cell membrane components into lipid bilayers, conferring them with biological properties originating from the cell of origin. Until now, most studies
Noelia Hernández‐Lobato   +6 more
wiley   +1 more source

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

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

Nanotherapies for Atherosclerosis: Targeting, Catalysis, and Energy Transduction

open access: yesAdvanced Healthcare Materials, EarlyView.
Atherosclerosis management is hindered by poor drug targeting and plaque heterogeneity. Nanotechnology overcomes these barriers via three core strategies: (1) target‐engineered nanocarriers that achieve lesion‐specific precision via ligand modification, biomimetic camouflage, stimuli‐responsive release, and self‐propelling nanomotors; (2) catalytic ...
Yuqi Yang   +4 more
wiley   +1 more source

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

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