Results 51 to 60 of about 34,140 (152)

Heat shock protein 90 chaperone activity is required for hepatitis A virus replication

Journal of Virology
HSP90 heat shock chaperones are essential for maintaining cellular proteostasis, as well as the ATP-dependent folding and functional maturation of many viral proteins. As a result, inhibitors of HSP90 have broad antiviral activity, disrupting replication
You Li, Xin Zheng, Ling Xie, Maryna Kapustina, Takayoshi Shirasaki, Bryan Yonish, Xian Chen, Asuka Hirai-Yuki, Noriyo Nagata, Ryosuke Suzuki, Masanori Isogawa, Matthew R. Vogt, Masamichi Muramatsu, Stanley M. Lemon   +13 more
doaj   +1 more source

Heat shock protein 90 (Hsp90) [PDF]

Science-Business eXchange, 2009
  +6 more sources

Withanolides-induced breast cancer cell death is correlated with their ability to inhibit heat protein 90.

PLoS ONE, 2012
Withanolides are a large group of steroidal lactones found in Solanaceae plants that exhibit potential anticancer activities. We have previously demonstrated that a withanolide, tubocapsenolide A, induced cycle arrest and apoptosis in human breast cancer
Hui-Chun Wang, Yi-Ling Tsai, Yang-Chang Wu, Fang-Rong Chang, Mei-Hsin Liu, Wen-Ying Chen, Chin-Chung Wu   +6 more
doaj   +1 more source

The Expression Levels of Heat Shock Protein 90 (HSP90) in Galleria mellonella Following Infection with the Entomopathogenic Nematode Steinernema carpocapsae and Its Symbiotic Bacteria Xenorhabdus nematophila

Insects
Heat shock proteins (HSPs), particularly HSP90, play a vital role in insect responses to environmental and biotic stresses by maintaining protein stability and supporting immune defenses. This study explores HSP90 regulation in Galleria mellonella larvae
Davide Banfi, Maristella Mastore, Tommaso Bianchi, Maurizio Francesco Brivio   +3 more
doaj   +1 more source

Human, vector and parasite Hsp90 proteins: A comparative bioinformatics analysis

FEBS Open Bio, 2015
The treatment of protozoan parasitic diseases is challenging, and thus identification and analysis of new drug targets is important. Parasites survive within host organisms, and some need intermediate hosts to complete their life cycle.
Ngonidzashe Faya, David L. Penkler, Özlem Tastan Bishop   +2 more
doaj   +1 more source

Heat shock protein 90 (HSP90AA1; Hsp90) [PDF]

Science-Business eXchange, 2009
  +6 more sources

HSP90 multi-functionality in cancer

Frontiers in Immunology
The 90-kDa heat shock proteins (HSP90s) are molecular chaperones essential for folding, unfolding, degradation and activity of a wide range of client proteins. HSP90s and their cognate co-chaperones are subject to various post-translational modifications,
Zarema Albakova, Zarema Albakova
doaj   +1 more source

Mechanisms of Resistance to Hsp90 Inhibitor Drugs: A Complex Mosaic Emerges

Pharmaceuticals, 2011
The molecular chaperone Hsp90 holds great promise as a cancer drug target, despite some of the initial clinical trials of Hsp90 inhibitor drugs having not lived up to expectation.
Peter W. Piper, Stefan H. Millson
doaj   +1 more source

Changes in HSP gene and protein expression in natural scrapie with brain damage

Veterinary Research, 2011
Heat shock proteins (Hsp) perform cytoprotective functions such as apoptosis regulation and inflammatory response control. These proteins can also be secreted to the extracellular medium, acting as inflammatory mediators, and their chaperone activity ...
Serrano Carmen, Bolea Rosa, Lyahyai Jaber, Filali Hicham, Varona Luis, Marcos-Carcavilla Ane, Acín Cristina, Calvo Jorge H, Serrano Magdalena, Badiola Juan J, Zaragoza Pilar, Martín-Burriel Inmaculada   +11 more
doaj   +1 more source

New Insights into Hsp90 Structural Plasticity Revealed by cryoEM

BioChem
Heat Shock Protein 90 (Hsp90) acts as a crucial molecular chaperone, playing an essential role in activating numerous signaling proteins. The intricate mechanism of Hsp90 involving ATPase-coupled conformational changes and interactions with cochaperone ...
Karine Minari, Vitor Hugo Balasco Serrão, Júlio César Borges   +2 more
doaj   +1 more source