Results 21 to 30 of about 310,958 (294)

The hexameric structures of human heat shock protein 90. [PDF]

open access: yesPLoS ONE, 2011
The human 90-kDa heat shock protein (HSP90) functions as a dimeric molecular chaperone. HSP90 identified on the cell surface has been found to play a crucial role in cancer invasion and metastasis, and has become a validated anti-cancer target for drug ...
Cheng-Chung Lee   +3 more
doaj   +1 more source

A secreted Heat shock protein 90 of Trichomonas vaginalis. [PDF]

open access: yesPLoS Neglected Tropical Diseases, 2018
Trichomonas vaginalis is a causative agent of Trichomoniasis, a leading non-viral sexually transmitted disease worldwide. In the current study, we show Heat shock protein 90 is essential for its growth. Upon genomic analysis of the parasite, it was found
Meetali Singh   +7 more
doaj   +1 more source

Purification of Mg2+-dependent phosphatidate phosphohydrolase from rat liver: new steps and aspects [PDF]

open access: yes, 2005
A new procedure for the partial purification of Mg2+-dependent, N-ethylmaleimide-sensitive phosphatidate phosphohydrolase (Mg2+-PAP; EC 3.1.3.4) from rat liver cytosol is described, using protein precipitation with MgCl2, gel filtration on Sephacryl S ...
Butterwith   +10 more
core   +1 more source

Conformational dynamics of a single protein monitored for 24 hours at video rate [PDF]

open access: yes, 2018
We use plasmon rulers to follow the conformational dynamics of a single protein for up to 24 h at a video rate. The plasmon ruler consists of two gold nanospheres connected by a single protein linker.
Ahijado-Guzmán, Rubén   +10 more
core   +3 more sources

Bioresistive identification of heat shock protein 90 [PDF]

open access: yesBiomicrofluidics, 2008
90 kDa heat shock protein (HSP90) is a ubiquitous molecular chaperone and is one of the abundant proteins present in a cell under normal and stressed conditions. The adenosine triphosphate (ATP) binding region of HSP90 is currently under a great degree of study because of the interest of its role in cancer and protein maintenance; the binding of ATP to
Arvind, Chandrasekaran   +5 more
openaire   +2 more sources

Mechanisms of Hsp90 regulation [PDF]

open access: yes, 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 ...
Ahn   +199 more
core   +1 more source

Evaluation of antioxidant property of heat shock protein 90 from duck muscle [PDF]

open access: yesAnimal Bioscience, 2021
Objective The objectives of this study were to investigate the direct antioxidative effect of 90 Kda heat shock protein (Hsp90) obtained from duck muscle.
Muhan Zhang   +3 more
doaj   +1 more source

Aspirin relieves the calcification of aortic smooth muscle cells by enhancing the heat shock response

open access: yesPharmaceutical Biology, 2022
Context Vascular calcification is a major complication of chronic renal failure, which has been identified as an active process partly driven by osteogenic transition of vascular smooth muscle cells (VSMCs).
Quanquan Shen   +7 more
doaj   +1 more source

Vectors for N- or C-terminal positioning of the yeast Gal4p DNA binding or activator domains [PDF]

open access: yes, 2003
EMTREE drug terms: fungal protein; heat shock protein 90; hybrid protein; transcription factor EMTREE medical terms: amino terminal sequence; article; carboxy terminal sequence; DNA binding; DNA binding domain; expression vector; Gal4p domain; gene ...
Millson, S. H.   +2 more
core   +1 more source

Unleashing the full potential of Hsp90 inhibitors as cancer therapeutics through simultaneous inactivation of Hsp90, Grp94, and TRAP1 [PDF]

open access: yes, 2020
Cancer therapeutics: Extending a drug's reach A new drug that blocks heat shock proteins (HSPs), helper proteins that are co-opted by cancer cells to promote tumor growth, shows promise for cancer treatment.
Chae, Young Chan   +10 more
core   +1 more source

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