Results 71 to 80 of about 109,885 (301)

Detecting HSP90 Phosphorylation [PDF]

open access: yes, 2011
Heat-shock protein 90 (HSP90) is an essential molecular chaperone in eukaryotes. It is important for chaperoning proteins that are important determinants of multistep carcinogenesis. HSP90's ATPase activity is associated with its chaperone function.
Mehdi, Mollapour, Len, Neckers
openaire   +2 more sources

hsp90: Twist and Fold [PDF]

open access: yesCell, 2006
Molecular chaperones are cellular machines that facilitate protein folding. The crystal structures of HtpG, the Escherichia coli homolog of hsp90, reported in this issue (Shiau et al., 2006) together with the recently published structures of an hsp90-cochaperone complex (Ali et al., 2006) and an hsp90-client protein complex (Vaughan et al., 2006 ...
Richter, Klaus, Buchner, Johannes
openaire   +2 more sources

Cars2‐Mediated Cysteine Catabolism Drives Brown Fat Development and Thermogenesis Through Persulfidating EBF2

open access: yesAdvanced Science, EarlyView.
We demonstrate that Cars2, a cysteine catabolic enzyme in mouse iBAT, is critical for cold tolerance and brown adipocyte differentiation. Through its CPERS activity, Cars2 produces CysSSH/H2S to induce EBF2 persulfidation, promoting its interaction with PPARγ and BRG1 to enhance thermogenic gene expression.
Xin Peng   +8 more
wiley   +1 more source

Molecular and morphological characterization of Avenae-group cyst nematodes (Heteroderidae) from Greece

open access: yesJournal of Nematology
Cyst nematodes of the genus Heterodera comprise 87 nominal species of economically important plant parasites, with the Avenae-group one of the largest, consisting of 12 species. Samplings for cyst nematode studies were carried out from multiple locations
Skantar Andrea M.   +5 more
doaj   +1 more source

Hsp90 is involved in apoptosis of Candida albicans by regulating the calcineurin-caspase apoptotic pathway. [PDF]

open access: yesPLoS ONE, 2012
Candida albicans is the most common human fungal pathogen. Recent evidence has revealed the occurrence of apoptosis in C. albicans that is inducible by environmental stresses such as hydrogen peroxide, acetic acid, and amphotericin B.
BaoDi Dai   +8 more
doaj   +1 more source

HSP90 inhibitors stimulate DNAJB4 protein expression through a mechanism involving N6-methyladenosine. [PDF]

open access: yes, 2019
Small-molecule inhibitors for the 90-kDa heat shock protein (HSP90) have been extensively exploited in preclinical studies for the therapeutic interventions of human diseases accompanied with proteotoxic stress.
Chen, Xuemei   +5 more
core   +1 more source

Early redox activities modulate Xenopus tail regeneration. [PDF]

open access: yes, 2018
Redox state sustained by reactive oxygen species (ROS) is crucial for regeneration; however, the interplay between oxygen (O2), ROS and hypoxia-inducible factors (HIF) remains elusive.
Ferreira, Fernando   +4 more
core   +2 more sources

Dynamic Shifts in ER–Plasma Membrane Junctions Signaling Define Pro‐Metastatic N‐Glycosylation and Predict Prostate Cancer Progression

open access: yesAdvanced Science, EarlyView.
Prostate cancer remains a leading cause of male cancer death, yet screening cannot reliably identify aggressive disease, underscoring the need for tissue biomarkers. It is shown that primary tumors increase ER–plasma membrane junction signaling via STIM1/ORP5, whereas metastasis features their loss, Golgi dispersal, and rapid conversion of high‐mannose
Amanda J. Macke   +14 more
wiley   +1 more source

RNAi knockdown of heat shock proteins affects thermotolerance of Ephestia kuehniella (Lepidoptera: Pyralidae) [PDF]

open access: yesJournal of Crop Protection
The Mediterranean flour moth, Ephestia kueheniella is one of the most severe pests in stores worldwide. Like many other stored product pests, chemical pesticides are often used to control this insect.
Ali Reza Bandani, Saeed Farahani
doaj   +1 more source

Heat-shock protein 90 promotes nuclear transport of herpes simplex virus 1 capsid protein by interacting with acetylated tubulin. [PDF]

open access: yesPLoS ONE, 2014
Although it is known that inhibitors of heat shock protein 90 (Hsp90) can inhibit herpes simplex virus type 1 (HSV-1) infection, the role of Hsp90 in HSV-1 entry and the antiviral mechanisms of Hsp90 inhibitors remain unclear.
Meigong Zhong   +10 more
doaj   +1 more source

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