Results 11 to 20 of about 76,334 (253)

Salmonella enterica serovar typhi limits the potency of typhoid toxin and ADP-ribosylating toxin AB to establish a persistent infection. [PDF]

open access: yesFEBS Open Bio
The two catalytic subunits of typhoid toxin dissociate from the holotoxin in the ER of an intoxicated cell, but only CdtB exits the ER to generate immunosuppressive effects. PltA is retained in the ER and sequestered from its cytosolic target, thus allowing the anti‐inflammatory effects of CdtB to promote intestinal colonization.
Zabala-Rodriguez MC   +4 more
europepmc   +2 more sources

Hsp90 as a molecular target [PDF]

open access: yes
Heat shock protein 90 (Hsp90), a highly conserved molecular chaperone, has been proposed to play a vital role in tumorigenesis. Hsp90 has two isoforms, of which Hsp90α is the major isoform of the Hsp90 complex and has an inducible expression profile. The
Munje, Chinmay
core   +6 more sources

Feasibility and safety of targeting mitochondria for cancer therapy – preclinical characterization of gamitrinib, a first-in-class, mitochondriaL-targeted small molecule Hsp90 inhibitor

open access: yesCancer Biology & Therapy, 2022
Mitochondria are key tumor drivers, but their suitability as a therapeutic target is unknown. Here, we report on the preclinical characterization of Gamitrinib (GA mitochondrial matrix inhibitor), a first-in-class anticancer agent that couples the Heat ...
Umar Hayat   +3 more
doaj   +1 more source

A novel yeast model detects Nrf2 and Keap1 interactions with Hsp90

open access: yesDisease Models & Mechanisms, 2022
Nrf2 is the master transcriptional regulator of cellular responses against oxidative stress. It is chiefly regulated by Keap1, a substrate adaptor protein that mediates Nrf2 degradation. Nrf2 activity is also influenced by many other protein interactions
Vy Ngo   +5 more
doaj   +1 more source

Discovery of novel Hsp90 C-terminal domain inhibitors that disrupt co-chaperone binding. [PDF]

open access: yes, 2021
Heat shock protein 90 (Hsp90) is an essential molecular chaperone that performs vital stress-related and housekeeping functions in cells and is a current therapeutic target for diseases such as cancers.
Reynisson
core   +1 more source

HSP90-CDC37-PP5 forms a structural platform for kinase dephosphorylation

open access: yes, 2022
Activation of client protein kinases by the HSP90 molecular chaperone system is affected by phosphorylation at multiple sites on HSP90, the kinase-specific co-chaperone CDC37, and the kinase client itself.
Xavier Aran Guiu (5369765)   +6 more
core   +2 more sources

Pioglitazone restores phosphorylation of downregulated caveolin-1 in right ventricle of monocrotaline-induced pulmonary hypertension

open access: yesClinical and Experimental Hypertension, 2022
Background Caveolin-1 (cav-1) plays a role in pulmonary arterial hypertension (PAH). Monocrotaline (MCT)-induced PAH is characterized by a loss of cav-1 in pulmonary arteries; however, less is known regarding its role in the hypertrophied right ventricle
Eva Malikova   +8 more
doaj   +1 more source

Aspirin Enhances the Protection of Hsp90 from Heat-Stressed Injury in Cardiac Microvascular Endothelial Cells Through PI3K-Akt and PKM2 Pathways

open access: yesCells, 2020
Heat stress (HS) often causes sudden death of humans and animals due to heart failure, mainly resulting from the contraction of cardiac microvasculature followed by myocardial ischemia.
Xiaohui Zhang   +8 more
doaj   +1 more source

Hsp90 governs dispersion and drug resistance of fungal biofilms [PDF]

open access: yes, 2011
Fungal biofilms are a major cause of human mortality and are recalcitrant to most treatments due to intrinsic drug resistance. These complex communities of multiple cell types form on indwelling medical devices and their eradication often requires ...
Ramage Gordon   +25 more
core   +2 more sources

Universal primers for amplifying the complete coding sequence of cytoplasmic heat shock protein 90 (HSP90) in Lepidoptera

open access: yesEuropean Journal of Entomology, 2011
Using sequence alignment, a conserved domain in the 3' untranslated region (UTR) of the cytoplasmic heat shock protein 90 (HSP90) of Lepidoptera was found. This region is highly variable in other insect groups.
Peng Jun XU   +4 more
doaj   +1 more source

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