Results 121 to 130 of about 109,885 (301)

In silico and in vitro drug screening identifies new therapeutic approaches for Ewing sarcoma. [PDF]

, 2016
The long-term overall survival of Ewing sarcoma (EWS) patients remains poor; less than 30% of patients with metastatic or recurrent disease survive despite aggressive combinations of chemotherapy, radiation and surgery.
Alturkmani, Hani, Baltezor, Michael, Butte, Atul J, Chen, Bin, Flynn, Colleen A, Godwin, Andrew K, Hyter, Stephen, Ma, Yan, Neville, Kathleen A, Pessetto, Ziyan Y, Rosenthal, Howard G, Weir, Scott J   +11 more
core   +3 more sources

Mosaic activation of the zebrafish hsp70l heat shock promoter: Implications for interpreting transgenes

Developmental Dynamics, EarlyView.
Abstract Background The promoters and enhancers of heat shock genes, such as the 1.5‐kb promoter of the zebrafish hsp70l gene, are valuable tools for temporal activation of transgenes. It has been widely purported that heat shock treatments result in ubiquitous expression of hsp70l‐driven transgenes.
Jong‐Su Park, Xiangyun Wei
wiley   +1 more source

Targeting the Hsp90-Cdc37-client protein interaction to disrupt Hsp90 chaperone machinery

Journal of Hematology & Oncology, 2018
Heat shock protein 90 (Hsp90) is a critical molecular chaperone protein that regulates the folding, maturation, and stability of a wide variety of proteins.
Ting Li, Hu-Lin Jiang, Yun-Guang Tong, Jin-Jian Lu   +3 more
doaj   +1 more source

Ligand-driven modulation of chaperone-cochaperone networks shapes proteostasis outcomes. [PDF]

Protein Sci
Abstract Protein homeostasis depends on a delicate interplay between folding and degradation, orchestrated by molecular chaperones. Among them, Hsp90 is a central hub, regulating nearly 10% of the proteome through ATP‐driven conformational cycles and selective interactions with cochaperones.
Magni A, Bonollo G, Trèves G, Frigerio F, Cinquini F, Pavoni S, Oliveira ASF, Mulholland AJ, Serapian SA, Colombo G.   +9 more
europepmc   +2 more sources

Role of hsp90 and the hsp90-binding immunophilins in signalling protein movement

Cellular Signalling, 2004
The ubiquitous protein chaperone hsp90 has been shown to regulate more than 100 proteins involved in cellular signalling. These proteins are called 'client proteins' for hsp90, and a multiprotein hsp90/hsp70-based chaperone machinery forms client protein.hsp90 heterocomplexes in the cytoplasm and the nucleus. In the case of signalling proteins that act
Pratt, William B., Galigniana, Mario Daniel, Harrell, Jennifer M., de Franco, Donald B.   +3 more
openaire   +3 more sources

Transcriptomic signatures reveal systemic adaptations and immune modulation in response to training and competitive racing in horses

Equine Veterinary Journal, EarlyView.
Abstract Background The molecular mechanisms underlying adaptation to physical exertion and racing stress in horses remain incompletely understood. Peripheral blood transcriptomics offers a minimally invasive method to monitor systemic responses to exercise and identify biomarkers of adaptation or overload. Objectives To evaluate transcriptomic changes
Izabela Dąbrowska, Jowita Grzędzicka‐Agko, Paula Kiełbik, Michał Trela, Olga Witkowska‐Piłaszewicz   +4 more
wiley   +1 more source

Discovery and development of natural heat shock protein 90 inhibitors in cancer treatment

Acta Pharmaceutica Sinica B, 2012
Heat shock protein 90 (Hsp90) is a highly conserved molecular chaperone that plays a vital role in the signal transduction of cancers. Hsp90 inhibitors are able to inhibit Hsp90 or the complex of Hsp90 and co-chaperones resulting in the degradation of ...
Yong Li, Dongmei Zhang, Jun Xu, Junmin Shi, Lei Jiang, Nan Yao, Wencai Ye   +6 more
doaj   +1 more source

Calcium binding to a remote site can replace magnesium as cofactor for mitochondrial Hsp90 (TRAP1) ATPase activity. [PDF]

, 2018
The Hsp90 molecular chaperones are ATP-dependent enzymes that maintain protein homeostasis and regulate many essential cellular processes. Higher eukaryotes have organelle-specific Hsp90 paralogs that are adapted to each subcellular environment.
Agard, David A, Elnatan, Daniel
core  

Aging cellular networks: chaperones as major participants

, 2006
We increasingly rely on the network approach to understand the complexity of cellular functions. Chaperones (heat shock proteins) are key "networkers", which have among their functions to sequester and repair damaged protein. In order to link the network
Agoston, Barabasi, Blais, Borodina, C. Sőti, Chan, Cherian, Cowen, Csermely, Csermely, Csermely, Csermely, Donaldson, Dorogovtsev, Dukan, Fares, Ferrarini, Gavin, Goldberger, Hayflick, He, Herndon, Heydari, Himmelstein, Imai, Irish, Macario, Morimoto, Mukai, Nardai, Nardai, Nollen, P. Csermely, Paulsson, Promislow, Pál, Queitsch, Rual, Rutherford, Schwarzer, Song, Stadtman, Stelzl, Sőti, Sőti, Sőti, Sőti, von Mering, Werner-Washburne, Westerheide, White, Yam, Young, Young, Zhao, Zhu, Zou   +56 more
core   +1 more source

Salt‐induced nutritional and metabolic shifts in halophytes: implications for food security

Journal of the Science of Food and Agriculture, EarlyView.
Abstract Plant species vary in their response to salinity: some crops show a degree of salt tolerance, while halophytes – whether wild or cultivated – are characterized by a high capacity to thrive under saline conditions. Halophytes are considered a source of valuable secondary metabolites with potential economic value, yet they might also produce ...
Giulia Atzori, Pedro Garcia Caparros, Antonella Castagna, Luisa Custódio, Valentina Lazazzara, Claus Krogh Madsen, Felicia Menicucci, Maria João Rodrigues, Katalin Solymosi, Jose Ramon Acosta Motos   +9 more
wiley   +1 more source