Contributions of co-chaperones and post-translational modifications towards Hsp90 drug sensitivity.
Contributions of co-chaperones and post-translational modifications towards Hsp90 drug sensitivity.
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DOI：
10.4155/fmc.13.88
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发表时间：
2013-06
影响因子：
4.2
通讯作者：
Mollapour M
中科院分区：
文献类型：
--
作者：
Walton-Diaz A;Khan S;Bourboulia D;Trepel JB;Neckers L;Mollapour M
Hsp90是一种分子伴侣，是几种参与肿瘤细胞恶性转化的致癌蛋白稳定和激活的重要驱动因素。因此，Hsp90被报道为治疗多种肿瘤（如非小细胞肺癌和her2阳性乳腺癌）的有希望的靶点也就不足为奇了。Hsp90伴侣的功能取决于其结合和水解ATP的能力，Hsp90抑制剂已被证明与核苷酸竞争与Hsp90的结合。Hsp90 atp酶活性的调控涉及多种因素，如共伴侣、翻译后修饰等。本文综述了翻译后修饰和共伴蛋白对Hsp90抑制剂疗效的影响。
Hsp90 is a molecular chaperone and important driver of stabilization and activation of several oncogenic proteins that are involved in the malignant transformation of tumor cells. Therefore, it is not surprising that Hsp90 has been reported to be a promising target for the treatment of several neoplasias, such as non-small-cell lung cancer and HER2-positive breast cancer. Hsp90 chaperone function depends on its ability to bind and hydrolyze ATP and Hsp90 inhibitors have been shown to compete with nucleotides for binding to Hsp90. Multiple factors, such as co-chaperones and post-translational modification, are involved in regulating Hsp90 ATPase activity. Here, the impact of post-translational modifications and co-chaperones on the efficacy of Hsp90 inhibitors are reviewed.
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影响因子：
5.3
作者：
Forafonov, Fedor;Toogun, Oyetunji A.;Picard, Didier
通讯作者：
Picard, Didier
DOI：
10.1073/pnas.0903392106
发表时间：
2009-05-19
影响因子：
11.1
作者：
Caldas-Lopes, Eloisi;Cerchietti, Leandro;Chiosis, Gabriela
通讯作者：
Chiosis, Gabriela
共伴侣HCH1调节HSP90的功能不同于其同源物AHA1，并且对酵母对HSP90抑制剂NVP-AUY922的敏感性赋予了敏感性。
影响因子：
3.7
作者：
Armstrong H;Wolmarans A;Mercier R;Mai B;LaPointe P
通讯作者：
LaPointe P
影响因子：
4.8
作者：
Bali, P;Pranpat, M;Bhalla, K
通讯作者：
Bhalla, K
影响因子：
2.5
作者：
Alarcon SV;Mollapour M;Lee MJ;Tsutsumi S;Lee S;Kim YS;Prince T;Apolo AB;Giaccone G;Xu W;Neckers LM;Trepel JB
通讯作者：
Trepel JB