scholarly article | Q13442814 |
P819 | ADS bibcode | 2011PLoSO...628211F |
P356 | DOI | 10.1371/JOURNAL.PONE.0028211 |
P932 | PMC publication ID | 3227642 |
P698 | PubMed publication ID | 22140548 |
P5875 | ResearchGate publication ID | 51852674 |
P50 | author | Amie J McClellan | Q59679229 |
Eric Franzosa | Q60056921 | ||
Judith Frydman | Q61960999 | ||
Véronique Albanèse | Q37375701 | ||
Yu Xia | Q37375723 | ||
P2860 | cites work | SGT1 encodes an essential component of the yeast kinetochore assembly pathway and a novel subunit of the SCF ubiquitin ligase complex | Q22003770 |
In vivo function of Hsp90 is dependent on ATP binding and ATP hydrolysis | Q22008008 | ||
Interaction of Hsp90 with ribosomal proteins protects from ubiquitination and proteasome-dependent degradation | Q24297095 | ||
Disassembly of transcriptional regulatory complexes by molecular chaperones | Q24300055 | ||
Activation of the ATPase activity of hsp90 by the stress-regulated cochaperone aha1 | Q24337678 | ||
Cytoscape: a software environment for integrated models of biomolecular interaction networks | Q24515682 | ||
BioGRID: a general repository for interaction datasets | Q24538650 | ||
The ATPase cycle of Hsp90 drives a molecular 'clamp' via transient dimerization of the N-terminal domains | Q24599484 | ||
Structures of GRP94-nucleotide complexes reveal mechanistic differences between the hsp90 chaperones | Q24671703 | ||
Structural and functional analysis of the middle segment of hsp90: implications for ATP hydrolysis and client protein and cochaperone interactions | Q27640863 | ||
Human Sgt1 binds HSP90 through the CHORD-Sgt1 domain and not the tetratricopeptide repeat domain | Q27643082 | ||
CNS1 encodes an essential p60/Sti1 homolog in Saccharomyces cerevisiae that suppresses cyclophilin 40 mutations and interacts with Hsp90. | Q27930607 | ||
Mapping pathways and phenotypes by systematic gene overexpression | Q27930674 | ||
Navigating the chaperone network: an integrative map of physical and genetic interactions mediated by the hsp90 chaperone | Q27930871 | ||
Sgt1p is a unique co-chaperone that acts as a client adaptor to link Hsp90 to Skp1p | Q27931036 | ||
A novel HSP90 chaperone complex regulates intracellular vesicle transport. | Q51791368 | ||
Diverse cellular functions of the Hsp90 molecular chaperone uncovered using systems approaches. | Q53523033 | ||
Common and divergent peptide binding specificities of hsp70 molecular chaperones. | Q54622492 | ||
Peptide-binding specificity of the molecular chaperone BiP | Q59071395 | ||
Localization of Heat Shock Proteins in Mouse Male Germ Cells: An Immunoelectron Microscopical Study | Q61978110 | ||
Conservation of Hsp90 macromolecular complexes in Saccharomyces cerevisiae | Q72724151 | ||
Folding and quality control of the VHL tumor suppressor proceed through distinct chaperone pathways | Q81813867 | ||
Cns1 is an essential protein associated with the hsp90 chaperone complex in Saccharomyces cerevisiae that can restore cyclophilin 40-dependent functions in cpr7Delta cells | Q27931200 | ||
Bms1p, a novel GTP-binding protein, and the related Tsr1p are required for distinct steps of 40S ribosome biogenesis in yeast | Q27931503 | ||
A two-hybrid screen of the yeast proteome for Hsp90 interactors uncovers a novel Hsp90 chaperone requirement in the activity of a stress-activated mitogen-activated protein kinase, Slt2p (Mpk1p). | Q27932386 | ||
Mutational analysis of Hsp90 function: interactions with a steroid receptor and a protein kinase | Q27932967 | ||
An essential GTPase promotes assembly of preribosomal RNA processing complexes | Q27933643 | ||
A well-connected and conserved nucleoplasmic helicase is required for production of box C/D and H/ACA snoRNAs and localization of snoRNP proteins. | Q27935012 | ||
Mixed Hsp90-cochaperone complexes are important for the progression of the reaction cycle | Q27935652 | ||
Bms1p, a G-domain-containing protein, associates with Rcl1p and is required for 18S rRNA biogenesis in yeast. | Q27935958 | ||
Characterization of Saccharomyces cerevisiae Nop17p, a novel Nop58p-interacting protein that is involved in Pre-rRNA processing. | Q27936232 | ||
Regulation of Hsp90 ATPase activity by tetratricopeptide repeat (TPR)-domain co-chaperones | Q27938505 | ||
The S. cerevisiae SEC65 gene encodes a component of yeast signal recognition particle with homology to human SRP19 | Q27938687 | ||
The signal recognition particle in S. cerevisiae | Q27939104 | ||
SEC65 gene product is a subunit of the yeast signal recognition particle required for its integrity | Q27939906 | ||
Identification of SSF1, CNS1, and HCH1 as multicopy suppressors of a Saccharomyces cerevisiae Hsp90 loss-of-function mutation | Q27940260 | ||
Designer deletion strains derived from Saccharomyces cerevisiae S288C: a useful set of strains and plasmids for PCR-mediated gene disruption and other applications | Q28131600 | ||
Global analysis of protein activities using proteome chips | Q28209011 | ||
A proteomic snapshot of the human heat shock protein 90 interactome | Q28279879 | ||
HSP90 at the hub of protein homeostasis: emerging mechanistic insights | Q29616824 | ||
Crystal structure of an Hsp90-nucleotide-p23/Sba1 closed chaperone complex | Q29617515 | ||
Evidence for reversible, non-microtubule and non-microfilament-dependent nuclear translocation of hsp90 after heat shock in human fibroblasts | Q30996996 | ||
Hsp90 nuclear accumulation in quiescence is linked to chaperone function and spore development in yeast | Q33571657 | ||
Novel Hsp90 partners discovered using complementary proteomic approaches | Q33838809 | ||
ATP binding and hydrolysis are essential to the function of the Hsp90 molecular chaperone in vivo | Q33889333 | ||
Hsp90 binds and regulates Gcn2, the ligand-inducible kinase of the alpha subunit of eukaryotic translation initiation factor 2 [corrected] | Q33960774 | ||
Heat shock protein 90 in neurodegenerative diseases | Q33961301 | ||
Stimulation of the weak ATPase activity of human hsp90 by a client protein | Q34111347 | ||
Regulation of Hsp90 ATPase activity by the co-chaperone Cdc37p/p50cdc37. | Q34120745 | ||
Hsp-90-associated oncoproteins: multiple targets of geldanamycin and its analogs | Q34124337 | ||
Transient interaction of Hsp90 with early unfolding intermediates of citrate synthase. Implications for heat shock in vivo | Q34307813 | ||
Chaperones increase association of tau protein with microtubules | Q34470626 | ||
Structure of an Hsp90-Cdc37-Cdk4 complex. | Q34562863 | ||
Structural Analysis of E. coli hsp90 reveals dramatic nucleotide-dependent conformational rearrangements | Q34575808 | ||
The Hsp90 chaperone complex regulates GDI-dependent Rab recycling | Q34885982 | ||
Convergence of heat shock protein 90 with ubiquitin in filamentous alpha-synuclein inclusions of alpha-synucleinopathies | Q35088093 | ||
Hsp90 and chromatin: where is the link? | Q35122656 | ||
A chemical genomics approach to understanding drug action | Q35216436 | ||
Evolutionary constraints on chaperone-mediated folding provide an antiviral approach refractory to development of drug resistance | Q35589164 | ||
Rab11a and HSP90 regulate recycling of extracellular alpha-synuclein | Q35621972 | ||
Role of hsp90 and the hsp90-binding immunophilins in signalling protein movement | Q35780995 | ||
Hsp90 and Cdc37 -- a chaperone cancer conspiracy. | Q36015525 | ||
The Hsp90 chaperone controls the biogenesis of L7Ae RNPs through conserved machinery | Q36446601 | ||
Hsp90 is required for pheromone signaling in yeast | Q36919284 | ||
Pharmacologic shifting of a balance between protein refolding and degradation mediated by Hsp90 | Q37044062 | ||
Heat shock protein 90 as a drug target: some like it hot. | Q37360814 | ||
TorsinA and heat shock proteins act as molecular chaperones: suppression of alpha-synuclein aggregation | Q40691639 | ||
Polyubiquitination and proteasomal degradation of the p185c-erbB-2 receptor protein-tyrosine kinase induced by geldanamycin | Q41168181 | ||
Disruption of the Raf-1-Hsp90 Molecular Complex Results in Destabilization of Raf-1 and Loss of Raf-1-Ras Association | Q41282697 | ||
The hsp90-based chaperone system: involvement in signal transduction from a variety of hormone and growth factor receptors | Q41729150 | ||
Factors governing the substrate recognition by GroEL chaperone: a sequence correlation approach | Q42112473 | ||
GroEL Recognizes an Amphipathic Helix and Binds to the Hydrophobic Side | Q42123947 | ||
Stable and specific binding of heat shock protein 90 by geldanamycin disrupts glucocorticoid receptor function in intact cells | Q42554487 | ||
Species-dependent ensembles of conserved conformational states define the Hsp90 chaperone ATPase cycle | Q42605486 | ||
Intracellular localization of the 90 kDA heat shock protein (HSP90α) determined by expression of a EGFP—HSP90α‐fusion protein in unstressed and heat stressed 3T3 cells | Q42802682 | ||
A common conformationally coupled ATPase mechanism for yeast and human cytoplasmic HSP90s | Q43106040 | ||
The co-chaperone p23 arrests the Hsp90 ATPase cycle to trap client proteins | Q46887356 | ||
Microglial activation and amyloid-beta clearance induced by exogenous heat-shock proteins | Q48648401 | ||
P275 | copyright license | Creative Commons Attribution 4.0 International | Q20007257 |
P6216 | copyright status | copyrighted | Q50423863 |
P4510 | describes a project that uses | Cytoscape | Q3699942 |
P433 | issue | 11 | |
P407 | language of work or name | English | Q1860 |
P921 | main subject | heterozygosity | Q124059385 |
P304 | page(s) | e28211 | |
P577 | publication date | 2011-01-01 | |
P1433 | published in | PLOS One | Q564954 |
P1476 | title | Heterozygous yeast deletion collection screens reveal essential targets of Hsp90 | |
P478 | volume | 6 |
Q90091087 | A methylated lysine is a switch point for conformational communication in the chaperone Hsp90 |
Q28542869 | A proteomic approach to investigating gene cluster expression and secondary metabolite functionality in Aspergillus fumigatus |
Q36496566 | Aneuploidy causes proteotoxic stress in yeast |
Q38176349 | Aneuploidy: implications for protein homeostasis and disease |
Q47362455 | Evidence for Hsp90 Co-chaperones in Regulating Hsp90 Function and Promoting Client Protein Folding |
Q88886422 | Evidence for interaction between Hsp90 and the ER membrane complex |
Q59792115 | Glucose intake hampers PKA-regulated HSP90 chaperone activity |
Q34963787 | Involvement of yeast HSP90 isoforms in response to stress and cell death induced by acetic acid |
Q37542238 | Predicting complex phenotype-genotype interactions to enable yeast engineering: Saccharomyces cerevisiae as a model organism and a cell factory. |
Q36701055 | Systematic identification and correction of annotation errors in the genetic interaction map of Saccharomyces cerevisiae |
Q27934900 | The Hsp90 cochaperones Cpr6, Cpr7, and Cns1 interact with the intact ribosome |
Q34472616 | The Hsp90-dependent proteome is conserved and enriched for hub proteins with high levels of protein-protein connectivity |
Q35125386 | The ribosomal biogenesis protein Utp21 interacts with Hsp90 and has differing requirements for Hsp90-associated proteins. |
Q34414198 | The yeast sphingolipid signaling landscape |
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