Results 51 to 60 of about 6,022 (190)

Mechanisms of resistance to Hsp90 inhibitor drugs: a complex mosaic emerges [PDF]

, 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.
Akerfelt, Altieri, Arya, Bagatell, Balch, Basso, Benchekroun, Bonvini, Brough, Chadli, Chatterjee, Chen, Cheung, Chiosis, Citri, Costantino, Cowen, Dai, Dai, Davenport, David, de Billy, Dias, Donze, Douglas, Eccles, Ehrlich, Floris, Forafonov, Gaspar, Gausdal, Georgakis, Grad, Guo, Guo, Guo, Guo, Haendeler, Harris, Holmes, Isaacs, Kamal, Kang, Kang, Kawazoe, Kayani, Kelland, Kim, Kim, Kim, Koga, Kurokawa, Landriscina, Lee, Lee, Li, Lin, Lundgren, Luo, McCollum, McCollum, McCollum, McDonald, McDonald, McLellan, Meng, Menzella, Millson, Mollapour, Mollapour, Morimoto, Nagai, Neef, Pandey, Pearl, Pearl, Peng, Peter W. Piper, Piper, Piper, Poksay, Porter, Powers, Powers, Powers, Prodromou, Rao, Roe, Roe, Schwarze, Scroggins, Sharp, Shelton, Simpson, Smith, Stebbins, Stefan H. Millson, Stepanova, Stepanova, Taldone, Tariq, Trepel, Trisciuoglio, Trott, Vali, Workman, Xie, Yamano, Yokota, Zha, Zhang, Zhang, Zhang, Zhang, Zhang, Zou, Zurawska   +116 more
core   +2 more sources

Interaction between Cdc37 and Cdk4 in human cells [PDF]

Oncogene, 1997
Using the yeast two-hybrid system we have identified novel potential Cdk4 interacting proteins. Here we described the interaction of Cdk4 with a human homologue of the yeast Drosophila CDC37 gene products. Cdc37 protein specifically interacts with Cdk4 and Cdk6, but not with Cdc2, Cdk2, Cdk3, Cdk5 and any of a number of cyclins tested.
L, Lamphere, F, Fiore, X, Xu, L, Brizuela, S, Keezer, C, Sardet, G F, Draetta, J, Gyuris   +7 more
openaire   +2 more sources

Induction of human Cdc37 in prostate cancer correlates with the ability of targeted Cdc37 expression to promote prostatic hyperplasia [PDF]

Oncogene, 2000
The Cdc37 gene encodes a 50 kDa protein which targets intrinsically unstable oncoprotein kinases such as Cdk4, Raf-1, and src to the molecular chaperone Hsp90. This activity is thought to play an important role in the establishment of signaling pathways controlling cell proliferation.
L, Stepanova, G, Yang, F, DeMayo, T M, Wheeler, M, Finegold, T C, Thompson, J W, Harper   +6 more
openaire   +2 more sources

Mutation of the Ser18 phosphorylation site on the sole Saccharomyces cerevisiae UCS protein, She4, can compromise high-temperature survival. [PDF]

, 2016
Folding of the myosin head often requires the joint actions of Hsp90 and a dedicated UNC45, Cro1, She4 (UCS) domain-containing cochaperone protein. Relatively weak sequence conservation exists between the single UCS protein of simple eukaryotes (She4 in ...
Gomez-Escalante, S., Millson, S.H., Piper, P.W.   +2 more
core   +1 more source

Gene-expression changes in cerium chloride-induced injury of mouse hippocampus. [PDF]

PLoS ONE, 2013
Cerium is widely used in many aspects of modern society, including agriculture, industry and medicine. It has been demonstrated to enter the ecological environment, is then transferred to humans through food chains, and causes toxic actions in several ...
Zhe Cheng, Haiquan Zhao, Yuguan Ze, Junju Su, Bing Li, Lei Sheng, Liyuan Zhu, Ning Guan, Suxin Gui, Xuezi Sang, Xiaoyang Zhao, Qingqing Sun, Ling Wang, Jie Cheng, Renping Hu, Fashui Hong   +15 more
doaj   +1 more source

Mechanisms of Hsp90 regulation [PDF]

, 2016
Heat shock protein 90 (Hsp90) is a molecular chaperone that is involved in the activation of disparate client proteins. This implicates Hsp90 in diverse biological processes that require a variety of co-ordinated regulatory mechanisms to control its ...
Ahn, Akira, Ali, Ali, Amin, Ammirante, Anckar, Anckar, Azevedo, Bali, Bandhakavi, Bansal, Bansal, Bansal, Barlev, Bharadwaj, Blank, Boellmann, Bonizzi, Bonner, Broemer, Brown, Bruce, Budzynski, Bulman, Catlett, Chen, Chen, Chen, Chen, Cho, Chrisostomos Prodromou, Combates, Cotto, Csermely, Cunningham, da Silva Correia, Deb, Dunn, Echeverria, Ehret, Espinosa, Farkas, Field, Finka, Frey, Geiss-Friedlander, Gerondakis, Ghosh, Gomez, Grad, Graf, Gugasyan, Gupta, Hashikawa, Hashikawa, Heimberger, Hensold, Hessling, Hickey, Hietakangas, Holmberg, Holmberg, Holt, Horejsi, Hubert, Ito, Jakob, Johnson, Jurivich, Kadota, Kekatpure, Kettenbach, Kitagawa, Kline, Knauf, Kobayashi, Kugel, Legagneux, Lei, Leskovar, Li, Li, Lindquist, Lingelbach, Liu, Liu, Longshaw, Lu, Makhnevych, Martinez-Ruiz, Mayor, McConnell, McLaughlin, Meyer, Meyer, Meyer, Mitsiades, Miyata, Miyata, Mollapour, Mollapour, Mollapour, Mollapour, Mollapour, Mollapour, Morimoto, Muller, Murphy, Murtagh, Napetschnig, Neef, Newton, Nieto-Sotelo, Oeckinghaus, Ogiso, Onuoha, Panaretou, Park, Pattaramanon, Pearl, Pearl, Pelham, Peteranderl, Picard, Pirkkala, Pittet, Pratt, Pratt, Prodromou, Prodromou, Prodromou, Prodromou, Prodromou, Qing, Quanz, Rabindran, Rebbe, Retzlaff, Retzlaff, Richter, Roe, Rutherford, Sakurai, Sbroggio, Scheufler, Schuler, Scroggins, Shamovsky, Shao, Shen, Shi, Shiau, Shirasu, Siligardi, Siligardi, Smale, Smith, Solier, Sorger, Sorger, Sorger, Southworth, Steensgaard, Stephanou, Stephanou, Taipale, Takahashi, Takai, Vaughan, Vaughan, Verghese, Voellmy, Voss, Vujanac, Wandinger, Wang, Weikl, Westerheide, Whitesell, Wiederrecht, Williams, Xiao, Xu, Xu, Yahara, Yamamoto, Yang, Zhang, Zhang, Zhang, Zhao, Zhao, Zhao, Zhong, Zhou, Zou, Zuehlke, Zuo, Zuo   +199 more
core   +1 more source

Protein Expression and Purification of the Hsp90-Cdc37-Cdk4 Kinase Complex from Saccharomyces cerevisiae

Bio-Protocol, 2017
Interactions between Hsp90, its co-chaperone Cdc37 and kinases have been biochemically studied for over three decades and have been shown to be functionally important in organisms from yeast to humans.
Kliment Verba, David Agard
doaj   +1 more source

A primate specific extra domain in the molecular chaperone Hsp90. [PDF]

PLoS ONE, 2013
Hsp90 (heat shock protein 90) is an essential molecular chaperone that mediates folding and quality control of client proteins. Many of them such as protein kinases, steroid receptors and transcription factors are involved in cellular signaling processes.
Vishwadeepak Tripathi, Wolfgang M J Obermann   +1 more
doaj   +1 more source

Hsp90 S-nitrosylation at Cys521, as a conformational switch, modulates cycling of Hsp90-AHA1-CDC37 chaperone machine to aggravate atherosclerosis

Redox Biology, 2022
Endothelial dysfunction is the initial process of atherosclerosis. Heat shock protein 90 (Hsp90), as a molecular chaperone, plays a crucial role in various cardiovascular diseases. Hsp90 function is regulated by S-nitrosylation (SNO).
Shuang Zhao, Xin Tang, Zian Miao, Yurong Chen, Jiawei Cao, Tianyu Song, Daiting You, Yanqing Zhong, Zhe Lin, Dan Wang, Zhiguang Shi, Xinlong Tang, Dongjin Wang, Shaoliang Chen, Liansheng Wang, Aihua Gu, Feng Chen, Liping Xie, Zhengrong Huang, Hong Wang, Yong Ji   +20 more
doaj   +1 more source

[Pemetrexed + Sorafenib] lethality is increased by inhibition of ERBB1/2/3-PI3K-NFκB compensatory survival signaling [PDF]

, 2016
In the completed phase I trial NCT01450384 combining the anti-folate pemetrexed and the multi-kinase inhibitor sorafenib it was observed that 20 of 33 patients had prolonged stable disease or tumor regression, with one complete response and multiple ...
Boone, David L., Booth, Laurence, Chuckalovcak, John, Dent, Paul, Koromilas, Antonis E., McGuire, William P., Poklepovic, Andrew, Roberts, Jane L., Stringer, Daniel K., Tavallai, Mehrad   +9 more
core   +1 more source