Results 101 to 110 of about 138,190 (352)

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

Hsp90 depletion goes wild [PDF]

open access: yesBMC Biology, 2012
Hsp90 reveals phenotypic variation in the laboratory, but is Hsp90 depletion important in the wild? Recent work from Chen and Wagner in BMC Evolutionary Biology has discovered a naturally occurring Drosophila allele that downregulates Hsp90, creating sensitivity to cryptic genetic variation.
Siegal Mark L, Masel Joanna
openaire   +3 more sources

Ubiquitination‐Driven Reprogramming of Proteostasis in Metastasis

open access: yesAdvanced Science, EarlyView.
The DCAF12–TRiC/CCT axis is a key regulator of metastasis in cancer. By reprogramming proteostasis to ensure efficient protein folding, it drives progression through a dual mechanism: enhancing cancer cell motility and invasiveness while concurrently activating pro‐growth and survival pathways.
Dongping Wei, Jiayan Chen, Yaping Xu
wiley   +1 more source

Expression of HSP90 Gene in the Cryopreserved Bovine Spermatozoa

open access: yesScientific Papers Animal Science and Biotechnologies, 2023
Cryopreservation is a technique, commonly used for a long-term storage of male gametes as an effective way to preserve their longevity and vitality. During cryopreservation and following the thawing process, sperm cells are exposed to thermal stress ...
Filip Benko   +4 more
doaj  

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

Expressed in the yeast Saccharomyces cerevisiae, human ERK5 is a client of the Hsp90 chaperone that complements loss of the Slt2p (Mpk1p) cell integrity stress-activated protein kinase [PDF]

open access: yes, 2006
ERK5 is a mitogen-activated protein (MAP) kinase regulated in human cells by diverse mitogens and stresses but also suspected of mediating the effects of a number of oncogenes.
King, Victoria   +7 more
core   +2 more sources

Structural basis for species-selective targeting of Hsp90 in a pathogenic fungus

open access: yesNature Communications, 2019
New strategies are needed to counter the escalating threat posed by drug-resistant fungi. The molecular chaperone Hsp90 affords a promising target because it supports survival, virulence and drug-resistance across diverse pathogens.
L. Whitesell   +19 more
semanticscholar   +1 more source

Modulation of Network Plasticity Opens Novel Therapeutic Possibilities in Cancer, Diabetes, and Neurodegeneration

open access: yesAdvanced Science, EarlyView.
Plasticity changes of molecular networks form a cellular learning process. Signaling network plasticity promotes cancer, metastasis, and drug resistance development. 55 plasticity‐related cancer drug targets are listed (20 having already approved drugs, 9 investigational drugs, and 26 being drug target candidates).
Márk Kerestély   +5 more
wiley   +1 more source

The HSP90 Inhibitor, 17-AAG, Influences the Activation and Proliferation of T Lymphocytes via AKT/GSK3β Signaling in MRL/lpr Mice

open access: yesDrug Design, Development and Therapy, 2020
Liang-Jian Hong, Ai-Jun Chen, Feng-Zeng Li, Ke-Jun Chen, Sheng Fang Department of Dermatology, The First Affiliated Hospital of Chongqing Medical University, Chongqing 400016, People’s Republic of ChinaCorrespondence: Sheng FangDepartment of ...
Hong LJ, Chen AJ, Li FZ, Chen KJ, Fang S
doaj  

Virulence of HtpG+ and HtpG strains of Yersinia pestis for Mice and Guinea Pigs

open access: yesПроблемы особо опасных инфекций, 2020
HtpG (high-temperature protein G) is a bacterial homologue of the highly conserved molecular chaperone Hsp90 of eukaryotes, which plays an important role in protection against stress in many bacterial species.
E. A. Krasil’nikova   +7 more
doaj   +1 more source

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