Biological and Structural Basis for Aha1 Regulation of Hsp90 ATPase Activity in Maintaining Proteostasis in the Human Disease Cystic Fibrosis
出版年份 2010 全文链接
标题
Biological and Structural Basis for Aha1 Regulation of Hsp90 ATPase Activity in Maintaining Proteostasis in the Human Disease Cystic Fibrosis
作者
关键词
-
出版物
MOLECULAR BIOLOGY OF THE CELL
Volume 21, Issue 6, Pages 871-884
出版商
American Society for Cell Biology (ASCB)
发表日期
2010-01-21
DOI
10.1091/mbc.e09-12-1017
参考文献
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注意:仅列出部分参考文献,下载原文获取全部文献信息。- Biological and Chemical Approaches to Diseases of Proteostasis Deficiency
- (2009) Evan T. Powers et al. Annual Review of Biochemistry
- The proteostasis boundary in misfolding diseases of membrane traffic
- (2009) Darren M. Hutt et al. FEBS LETTERS
- The Mammalian Hsp40 ERdj3 Requires Its Hsp70 Interaction and Substrate-binding Properties to Complement Various Yeast Hsp40-dependent Functions
- (2009) Shruthi S. Vembar et al. JOURNAL OF BIOLOGICAL CHEMISTRY
- Protein Homeostasis and Aging: Taking Care of Proteins From the Cradle to the Grave
- (2009) R. I. Morimoto et al. JOURNALS OF GERONTOLOGY SERIES A-BIOLOGICAL SCIENCES AND MEDICAL SCIENCES
- Visualizing the twists and turns of a molecular chaperone
- (2009) Len Neckers et al. NATURE STRUCTURAL & MOLECULAR BIOLOGY
- The large conformational changes of Hsp90 are only weakly coupled to ATP hydrolysis
- (2009) Moritz Mickler et al. NATURE STRUCTURAL & MOLECULAR BIOLOGY
- Dissection of the ATP-induced conformational cycle of the molecular chaperone Hsp90
- (2009) Martin Hessling et al. NATURE STRUCTURAL & MOLECULAR BIOLOGY
- CFTR Function and Prospects for Therapy
- (2008) John R. Riordan Annual Review of Biochemistry
- The Hsp90 molecular chaperone: an open and shut case for treatment
- (2008) Laurence H. Pearl et al. BIOCHEMICAL JOURNAL
- Structural and Functional Diversities between Members of the Human HSPB, HSPH, HSPA, and DNAJ Chaperone Families†
- (2008) Michel J. Vos et al. BIOCHEMISTRY
- Silencing of HSP90 Cochaperone AHA1 Expression Decreases Client Protein Activation and Increases Cellular Sensitivity to the HSP90 Inhibitor 17-Allylamino-17-Demethoxygeldanamycin
- (2008) J. L. Holmes et al. CANCER RESEARCH
- Targeting Hsp90: small-molecule inhibitors and their clinical development
- (2008) Tony Taldone et al. CURRENT OPINION IN PHARMACOLOGY
- Chaperone displacement from mutant cystic fibrosis transmembrane conductance regulator restores its function in human airway epithelia
- (2008) Fei Sun et al. FASEB JOURNAL
- A common conformationally coupled ATPase mechanism for yeast and human cytoplasmic HSP90s
- (2008) Cara K. Vaughan et al. FEBS Journal
- Intra- and Intermonomer Interactions Are Required to Synergistically Facilitate ATP Hydrolysis in Hsp90
- (2008) Christian N. Cunningham et al. JOURNAL OF BIOLOGICAL CHEMISTRY
- The Hsp90 Chaperone Machinery
- (2008) Sebastian Karl Wandinger et al. JOURNAL OF BIOLOGICAL CHEMISTRY
- Conserved Conformational Changes in the ATPase Cycle of Human Hsp90
- (2008) Klaus Richter et al. JOURNAL OF BIOLOGICAL CHEMISTRY
- Structural Studies on the Co-chaperone Hop and Its Complexes with Hsp90
- (2008) S.C. Onuoha et al. JOURNAL OF MOLECULAR BIOLOGY
- Assembly and Misassembly of Cystic Fibrosis Transmembrane Conductance Regulator: Folding Defects Caused by Deletion of F508 Occur Before and After the Calnexin-dependent Association of Membrane Spanning Domain (MSD) 1 and MSD2
- (2008) Meredith F. N. Rosser et al. MOLECULAR BIOLOGY OF THE CELL
- Adapting Proteostasis for Disease Intervention
- (2008) William E. Balch et al. SCIENCE
- Multiple Conformations of E. coli Hsp90 in Solution: Insights into the Conformational Dynamics of Hsp90
- (2008) Kristin A. Krukenberg et al. STRUCTURE
- Chemical and Biological Folding Contribute to Temperature-Sensitive ΔF508 CFTR Trafficking
- (2008) Xiaodong Wang et al. TRAFFIC
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