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部分热休克蛋白90（HSP90）高引（>700次）论文
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部分热休克蛋白90（HSP90）高引（>700次）论文
诸平
将部分与热休克蛋白90（heat-shock protein 90，HSP90）相关的高引（被引超过700次）论文，摘引如下，仅供参考。
Hsp90 as a capacitor for morphological evolution
1998 in Nature [IF: 40.14]
(Howard Hughes Medical Institute), Susan Lindquist
(University of California, Irvine)
The heat-shock protein Hsp90 supports diverse but specific signal transducers and lies at the interface of several developmental pathways. We report here that when Drosophila Hsp90 is mutant or pharmacologically impaired, phenotypic variation affecting nearly any adult structure is produced, with specific variants depending on the genetic background and occurring both in laboratory strains and in ...
Ref 34Cited 1490SourceCite this paperAdd Collection
HSP90 and the chaperoning of cancer
2005 in Nature Reviews Cancer [IF: 37.15]
(Massachusetts Institute of Technology), Susan Lindquist
(Massachusetts Institute of Technology)
Standing watch over the proteome, molecular chaperones are an ancient and evolutionarily conserved class of proteins that guide the normal folding, intracellular disposition and proteolytic turnover of many of the key regulators of cell growth, differentiation and survival. This essential guardian function is subverted during oncogenesis to allow malignant transformation and to facilitate rapid so...
Ref 148Cited 1457SourceCite this paperAdd Collection
Hsp70 chaperones: cellular functions and molecular mechanism.
2005 in Cellular and Molecular Life Sciences [IF: 5.79]
(Heidelberg University), Bernd Bukau
(Heidelberg University)
Hsp70 proteins are central components of the cellular network of molecular chaperones and folding catalysts. They assist a large variety of protein folding processes in the cell by transient association of their substrate binding domain with short hydrophobic peptide segments within their substrate proteins. The substrate binding and release cycle is driven by the switching of Hsp70 between the lo...
Ref 126Cited 1401Download PdfCite this paperAdd Collection
Steroid receptor interactions with heat shock protein and immunophilin chaperones
1997 in Endocrine Reviews [IF: 15.74]
(University of Michigan), David O. Toft
(Mayo Clinic)
I. Introduction II. 9S Receptors A. Estrogen receptors (ERs) B. Progesterone receptors (PRs) C. Androgen receptors (ARs) D. Glucocorticoid receptors (GRs) E. Mineralocorticoid receptors (MRs) F. Dioxin receptors (DRs) G. Antheridiol receptors III. Receptor Transformation A. Transformed receptors bind polyanions B. Artifactual transforming conditions C. Models of cytosolic receptor transformation D...
Cited 1241SourceCite this paperAdd Collection
1994 in Proceedings of the National Academy of Sciences of the United States of America [IF: 9.66]
Abstract The molecular mechanisms by which oncogenic tyrosine kinases induce cellular transformation are unclear. Herbimycin A, geldanamycin, and certain other benzoquinone ansamycins display an unusual capacity to revert tyrosine kinase-induced oncogenic transformation. As an approach to the study of v-src-mediated transformation, we examined ansamycin action in transformed cells and found that d...
Cited 1093SourceCite this paperAdd Collection
Small heat shock proteins are molecular chaperones.
1993 in Journal of Biological Chemistry [IF: 4.13]
(University of Michigan), Matthias Gaestel
(Technische Universität München), K Engel
Abstract Small heat shock proteins (sHsp) with a molecular mass of 15-30 kDa are ubiquitous and conserved. Up to now their function has remained enigmatic. Increased expression under heat shock conditions and their protective effect on cell viability at elevated temperatures suggest that they may have a function in the formation or maintenance of the native conformation of cytosolic proteins. To t...
Cited 1061Download PdfAdd Collection
2003 in Experimental Biology and Medicine [IF: 2.69]
(University of Michigan), David O. Toft
(University of Rochester)
Nearly 100 proteins are known to be regulated by hsp90. Most of these substrates or “client proteins” are involved in signal transduction, and they are brought into complex with hsp90 by a multlprotein hsp90/hsp70-based chaperone machinery. In addition to binding substrate proteins at the chaperone site(s), hsp90 binds cofactors at other sites that are part of the heterocomplex assembly machinery ...
Ref 298Cited 1049Download PdfCite this paperAdd Collection
1997 in Cell [IF: 30.41]
(Cornell University), Alicia A. Russo
(Memorial Sloan Kettering Cancer Center), Christine Schneider
(Memorial Sloan Kettering Cancer Center)
Abstract The Hsp90 chaperone is required for the activation of several families of eukaryotic protein kinases and nuclear hormone receptors, many of which are proto-oncogenic and play a prominent role in cancer. The geldanamycin antibiotic has antiproliferative and antitumor effects, as it binds to Hsp90, inhibits the Hsp90-mediated conformational maturation/refolding reaction, and results in the ...
Ref 58Cited 1006Download PdfCite this paperAdd Collection
A high-affinity conformation of Hsp90 confers tumour selectivity on Hsp90 inhibitors.
2003 in Nature [IF: 40.14]
(University of California, San Diego), Lia Thao
(Chiron Corporation)
Heat shock protein 90 (Hsp90) is a molecular chaperone that plays a key role in the conformational maturation of oncogenic signalling proteins, including HER-2/ErbB2, Akt, Raf-1, Bcr-Abl and mutated p53 1-7 . Hsp90 inhibitors bind to Hsp90, and induce the proteasomal degradation of Hsp90 client proteins 6,8-11 . Although Hsp90 is highly expressed in most cells, Hsp90 inhibitors selectively kill ca...
Ref 30Cited 942SourceCite this paperAdd Collection
1997 in Cell [IF: 30.41]
(University College London), S. Mark Roe
(University College London), Ronan O'Brien
(University College London)
Hsp90 molecular chaperones in eukaryotic cells play essential roles in the folding and activation of a range of client proteins involved in cell cycle regulation, steroid hormone responsiveness, and signal transduction. The biochemical mechanism of Hsp90 is poorly understood, and the involvement of ATP in particular is controversial. Crystal structures of complexes between the N-terminal domain of...
Ref 56Cited 929SourceCite this paperAdd Collection
CD91 Is a Common Receptor for Heat Shock Proteins gp96, hsp90, hsp70, and Calreticulin
2001 in Immunity [IF: 22.84]
(University of Connecticut), Robert J. Binder
(University of Connecticut), Thirumalai R. Ramalingam
(University of Connecticut)
Abstract Complexes of the heat shock protein gp96 and antigenic peptides are taken up by antigen-presenting cells and presented by MHC class I molecules. In order to explain the unusual efficiency of this process, the uptake of gp96 had been postulated to occur through a receptor, identified recently as CD91. We show here that complexes of peptides with heat shock proteins hsp90, calreticulin, and...
Ref 32Cited 883SourceCite this paperAdd Collection
Hsp90 as a capacitor of phenotypic variation.
2002 in Nature [IF: 40.14]
(Massachusetts Institute of Technology), Todd A. Sangster
(Massachusetts Institute of Technology), Susan Lindquist
(Massachusetts Institute of Technology)
Heat-shock protein 90 (Hsp90) chaperones the maturation of many regulatory proteins and, in the fruitfly Drosophila melanogaster, buffers genetic variation in morphogenetic pathways. Levels and patterns of genetic variation differ greatly between obligatorily outbreeding species such as fruitflies and self-fertilizing species such as the plant Arabidopsis thaliana. Also, plant development is more ...
Ref 27Cited 877Download PdfCite this paperAdd Collection
2000 in Cell [IF: 30.41]
(Max Planck Society), Achim Brinker
(Max Planck Society), Gleb P. Bourenkov
(Max Planck Society)
Abstract The adaptor protein Hop mediates the association of the molecular chaperones Hsp70 and Hsp90. The TPR1 domain of Hop specifically recognizes the C-terminal heptapeptide of Hsp70 while the TPR2A domain binds the C-terminal pentapeptide of Hsp90. Both sequences end with the motif EEVD. The crystal structures of the TPR–peptide complexes show the peptides in an extended conformation, spannin...
Ref 54Cited 831SourceCite this paperAdd Collection
Dynamic activation of endothelial nitric oxide synthase by Hsp90
1998 in Nature [IF: 40.14]
(Harvard University), Roger Fan
(Yale University), Vijay Shah
(Yale University)
Heat-shock protein 90 (Hsp90) coordinates the trafficking and regulation of diverse signalling proteins, but its precise role in regulating specific cellular targets is not known 1,2 . Here we show that Hsp90 associates with endothelial nitric oxide synthase (eNOS) and is rapidly recruited to the eNOS complex by agonists that stimulate production of nitric oxide, namely vascular endothelial growth...
Ref 31Cited 796SourceCite this paperAdd Collection
1998 in Cell [IF: 30.41]
(University of Miami), Yongle Guo
(University of Miami), Toumy Guettouche
(University of Miami)
Abstract Heat shock and other proteotoxic stresses cause accumulation of nonnative proteins that trigger activation of heat shock protein (Hsp) genes. A chaperone/Hsp functioning as repressor of heat shock transcription factor (HSF) could make activation of hsp genes dependent on protein unfolding. In a novel in vitro system, in which human HSF1 can be activated by nonnative protein, heat, and gel...
Ref 54Cited 791SourceCite this paperAdd Collection
HSP90 at the hub of protein homeostasis: emerging mechanistic insights
2010 in Nature Reviews Molecular Cell Biology [IF: 46.60]
(Massachusetts Institute of Technology), Daniel F. Jarosz
(Massachusetts Institute of Technology), Susan Lindquist
(Massachusetts Institute of Technology)
HSP90 is a highly conserved chaperone that facilitates the maturation of a wide range of proteins. Recent studies have provided insight into the regulation of the HSP90 chaperone cycle and revealed numerous processes that HSP90 regulates directly or indirectly.
Ref 180Cited 790SourceCite this paperAdd Collection
1998 in Pharmacology & Therapeutics [IF: 11.13]
(Semmelweis University), Tamás Schnaider
(Semmelweis University), Csaba Soti
(Semmelweis University)
The 90-kDa molecular chaperone family (which comprises, among other proteins, the 90-kDa heat-shock protein, hsp90 and the 94-kDa glucose-regulated protein, grp94, major molecular chaperones of the cytosol and of the endoplasmic reticulum, respectively) has become an increasingly active subject of research in the past couple of years. These ubiquitous, well-conserved proteins account for 1–2% of a...
Ref 516Cited 742Download PdfCite this paperAdd Collection
Targeting the dynamic HSP90 complex in cancer
2010 in Nature Reviews Cancer [IF: 37.15]
(National Institutes of Health), Mehdi Mollapour
(National Institutes of Health), Giuseppe Giaccone
(National Institutes of Health)
Numerous oncoproteins depend on the molecular chaperone heat shock protein 90 (HSP90). However, the optimal use of HSP90-targeted therapeutics will depend on understanding the complexity of HSP90 regulation and the degree to which the chaperone participates in both neoplastic and normal cellular physiology.
Ref 176Cited 738Download PdfCite this paperAdd Collection
The co-chaperone CHIP regulates protein triage decisions mediated by heat-shock proteins.
2001 in Nature Cell Biology [IF: 20.06]
(University of Texas Medical Branch), Carol A. Ballinger
(University of Texas Medical Branch), Jihong Jiang
(University of Texas Medical Branch)
To maintain quality control in cells, mechanisms distinguish among improperly folded peptides, mature and functional proteins, and proteins to be targeted for degradation. The molecular chaperones, including heat-shock protein Hsp90, have the ability to recognize misfolded proteins and assist in their conversion to a functional conformation. Disruption of Hsp90 heterocomplexes by the Hsp90 inhibit...
Cited 710SourceCite this paperAdd Collection
Structure and Mechanism of the Hsp90 Molecular Chaperone Machinery
2006 in Annual Review of Biochemistry [IF: 19.94]
(University of Sussex), Chrisostomos Prodromou
(University of Sussex)
Heat shock protein 90 (Hsp90) is a molecular chaperone essential for activating many signaling proteins in the eukaryotic cell. Biochemical and structural analysis of Hsp90 has revealed a complex mechanism of ATPase-coupled conformational changes and interactions with cochaperone proteins, which facilitate activation of Hsp90's diverse "clientele." Despite recent progress, key aspects of the ATPas...
Ref 120Cited 695Download PdfCite this paperAdd Collection
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