| scholarly article | Q13442814 |
| P50 | author | Kenneth M. Scaglione | Q42386382 |
| Saurav Misra | Q57421650 | ||
| Richard C Page | Q59095929 | ||
| P2093 | author name string | Jay C Nix | |
| Dennis J Stuehr | |||
| Huaqun Zhang | |||
| Cameron McGlone | |||
| Joseph Amick | |||
| Michelle Dare | |||
| Ritu Chakravarti | |||
| Simon Schlanger | |||
| Stephanie Santarriaga | |||
| P2860 | cites work | The co-chaperone CHIP regulates protein triage decisions mediated by heat-shock proteins | Q24290709 |
| Chaperoned ubiquitylation--crystal structures of the CHIP U box E3 ubiquitin ligase and a CHIP-Ubc13-Uev1a complex | Q24296990 | ||
| Ubiquitylation of neuronal nitric-oxide synthase by CHIP, a chaperone-dependent E3 ligase | Q24306256 | ||
| Identification and characterization of a novel human methyltransferase modulating Hsp70 protein function through lysine methylation | Q24315705 | ||
| Rapid E2-E3 assembly and disassembly enable processive ubiquitylation of cullin-RING ubiquitin ligase substrates | Q24322903 | ||
| CHIP participates in protein triage decisions by preferentially ubiquitinating Hsp70-bound substrates | Q24338386 | ||
| Hsp70 chaperones: cellular functions and molecular mechanism | Q24644472 | ||
| MolProbity: all-atom structure validation for macromolecular crystallography | Q24649111 | ||
| PHENIX: a comprehensive Python-based system for macromolecular structure solution | Q24654617 | ||
| Building and remodelling Cullin-RING E3 ubiquitin ligases | Q27027816 | ||
| Structure of TPR domain-peptide complexes: critical elements in the assembly of the Hsp70-Hsp90 multichaperone machine | Q27622332 | ||
| Structure of the TPR domain of p67phox in complex with Rac.GTP | Q27628646 | ||
| Two structures of cyclophilin 40: folding and fidelity in the TPR domains | Q27632191 | ||
| Interactions between the quality control ubiquitin ligase CHIP and ubiquitin conjugating enzymes | Q27650632 | ||
| Structural and functional characterization of human SGT and its interaction with Vpu of the human immunodeficiency virus type 1 | Q27651876 | ||
| Structural basis of nucleotide exchange and client binding by the Hsp70 cochaperone Bag2 | Q27652982 | ||
| Solution conformation of wild-type E. coli Hsp70 (DnaK) chaperone complexed with ADP and substrate | Q27655465 | ||
| Molecular Mechanism of the Negative Regulation of Smad1/5 Protein by Carboxyl Terminus of Hsc70-interacting Protein (CHIP) | Q27667356 | ||
| Structure of a RING E3 ligase and ubiquitin-loaded E2 primed for catalysis | Q27670947 | ||
| BIRC7–E2 ubiquitin conjugate structure reveals the mechanism of ubiquitin transfer by a RING dimer | Q27671574 | ||
| The architecture of functional modules in the Hsp90 co-chaperone Sti1/Hop | Q27676637 | ||
| Allosteric opening of the polypeptide-binding site when an Hsp70 binds ATP | Q27678317 | ||
| Structure and dynamics of the ATP-bound open conformation of Hsp70 chaperones | Q27683212 | ||
| An autoinhibited conformation of LGN reveals a distinct interaction mode between GoLoco motifs and TPR motifs | Q27684596 | ||
| Structure and function of Hip, an attenuator of the Hsp70 chaperone cycle | Q27685147 | ||
| XDS | Q27860472 | ||
| SOLVE and RESOLVE: automated structure solution and density modification | Q27860481 | ||
| Phasercrystallographic software | Q27860930 | ||
| Features and development of Coot | Q27861079 | ||
| Scaling and assessment of data quality | Q27861107 | ||
| CHIP is a chaperone-dependent E3 ligase that ubiquitylates unfolded protein | Q41776375 | ||
| Definition of the minimal fragments of Sti1 required for dimerization, interaction with Hsp70 and Hsp90 and in vivo functions | Q42791206 | ||
| The E3 ubiquitin ligase CHIP and the molecular chaperone Hsc70 form a dynamic, tethered complex | Q42833100 | ||
| Structural characterization of the substrate transfer mechanism in Hsp70/Hsp90 folding machinery mediated by Hop. | Q43984053 | ||
| Protein quality control: U-box-containing E3 ubiquitin ligases join the fold | Q44061660 | ||
| Dimerization of the human E3 ligase CHIP via a coiled-coil domain is essential for its activity. | Q47070627 | ||
| Multiple domains of the co-chaperone Hop are important for Hsp70 binding. | Q51039772 | ||
| Substrate transfer from the chaperone Hsp70 to Hsp90. | Q51290927 | ||
| Insights into the conformational dynamics of the E3 ubiquitin ligase CHIP in complex with chaperones and E2 enzymes. | Q51560326 | ||
| Structure and interactions of the helical and U-box domains of CHIP, the C terminus of HSP70 interacting protein. | Q51586726 | ||
| Mechanics of Hsp70 chaperones enables differential interaction with client proteins. | Q54369498 | ||
| Effect of nucleotide on the binding of peptides to 70-kDa heat shock protein | Q72536404 | ||
| Multistep mechanism of substrate binding determines chaperone activity of Hsp70 | Q73943514 | ||
| Molecular evolution of the HSP70 multigene family | Q27940113 | ||
| Cooperation of a ubiquitin domain protein and an E3 ubiquitin ligase during chaperone/proteasome coupling | Q28202126 | ||
| An androgen receptor NH2-terminal conserved motif interacts with the COOH terminus of the Hsp70-interacting protein (CHIP) | Q28258333 | ||
| C-terminal phosphorylation of Hsp70 and Hsp90 regulates alternate binding to co-chaperones CHIP and HOP to determine cellular protein folding/degradation balances | Q28271643 | ||
| CHIP-mediated stress recovery by sequential ubiquitination of substrates and Hsp70 | Q28303344 | ||
| Ube2w and ataxin-3 coordinately regulate the ubiquitin ligase CHIP | Q28593538 | ||
| Topology and dynamics of the 10 kDa C-terminal domain of DnaK in solution | Q28756224 | ||
| TPR proteins: the versatile helix | Q29547585 | ||
| A newly uncovered group of distantly related lysine methyltransferases preferentially interact with molecular chaperones to regulate their activity | Q30179453 | ||
| Chaperone functions of the E3 ubiquitin ligase CHIP. | Q30362083 | ||
| Engineering a ubiquitin ligase reveals conformational flexibility required for ubiquitin transfer | Q30492047 | ||
| Biological heterogeneity of the peptide-binding motif of the 70-kDa heat shock protein by surface plasmon resonance analysis | Q33290603 | ||
| Benchmarking and analysis of protein docking performance in Rosetta v3.2. | Q33988409 | ||
| Identification of residues on Hsp70 and Hsp90 ubiquitinated by the cochaperone CHIP | Q34048681 | ||
| Chaperone-dependent E3 ubiquitin ligase CHIP mediates a degradative pathway for c-ErbB2/Neu | Q34190181 | ||
| GAPDH regulates cellular heme insertion into inducible nitric oxide synthase | Q34241252 | ||
| Molecular chaperone functions in protein folding and proteostasis | Q34349321 | ||
| 3D structure of human FK506-binding protein 52: implications for the assembly of the glucocorticoid receptor/Hsp90/immunophilin heterocomplex | Q34375305 | ||
| Certain pairs of ubiquitin-conjugating enzymes (E2s) and ubiquitin-protein ligases (E3s) synthesize nondegradable forked ubiquitin chains containing all possible isopeptide linkages. | Q34617875 | ||
| Versatile TPR domains accommodate different modes of target protein recognition and function | Q35056237 | ||
| Balance between folding and degradation for Hsp90-dependent client proteins: a key role for CHIP. | Q35121021 | ||
| Global proteomic profiling of phosphopeptides using electron transfer dissociation tandem mass spectrometry. | Q35629586 | ||
| Thioredoxin-1 regulates cellular heme insertion by controlling S-nitrosation of glyceraldehyde-3-phosphate dehydrogenase | Q35956677 | ||
| Structure of an E3:E2~Ub complex reveals an allosteric mechanism shared among RING/U-box ligases. | Q36291328 | ||
| Motif-specific sampling of phosphoproteomes | Q37243739 | ||
| The molecular chaperone Hsp70 activates protein phosphatase 5 (PP5) by binding the tetratricopeptide repeat (TPR) domain | Q37536572 | ||
| Structural and functional discussion of the tetra-trico-peptide repeat, a protein interaction module | Q37992235 | ||
| The chaperone Hsp90: changing partners for demanding clients | Q38090850 | ||
| Molecular chaperones as enzymes that catalytically unfold misfolded polypeptides. | Q38107685 | ||
| Structure, function and regulation of the hsp90 machinery | Q38117496 | ||
| New insights into ubiquitin E3 ligase mechanism | Q38201970 | ||
| Different combinations of the heat-shock cognate protein 70 (hsc70) C-terminal functional groups are utilized to interact with distinct tetratricopeptide repeat-containing proteins | Q38296271 | ||
| Enhanced HSP70 lysine methylation promotes proliferation of cancer cells through activation of Aurora kinase B. | Q39275975 | ||
| CHIP facilitates ubiquitination of inducible nitric oxide synthase and promotes its proteasomal degradation | Q39861615 | ||
| Molecular basis for TPR domain-mediated regulation of protein phosphatase 5. | Q40919534 | ||
| P433 | issue | 3 | |
| P407 | language of work or name | English | Q1860 |
| P921 | main subject | molecular chaperones | Q422496 |
| protein ubiquitination | Q3547638 | ||
| P304 | page(s) | 472-482 | |
| P577 | publication date | 2015-02-12 | |
| P1433 | published in | Structure | Q15709970 |
| P1476 | title | A bipartite interaction between Hsp70 and CHIP regulates ubiquitination of chaperoned client proteins | |
| P478 | volume | 23 |
| Q37689581 | 1H, 15N and 13C resonance assignments for free and IEEVD peptide-bound forms of the tetratricopeptide repeat domain from the human E3 ubiquitin ligase CHIP. |
| Q28771725 | ARD1-mediated Hsp70 acetylation balances stress-induced protein refolding and degradation |
| Q47952887 | BAG3-mediated proteostasis at a glance |
| Q37563337 | C-terminus of HSC70-Interacting Protein (CHIP) Inhibits Adipocyte Differentiation via Ubiquitin- and Proteasome-Mediated Degradation of PPARγ. |
| Q100750093 | CHIP phosphorylation by protein kinase G enhances protein quality control and attenuates cardiac ischemic injury |
| Q36128041 | Centipede venoms as a source of drug leads. |
| Q47222331 | Chaperone-Mediated Regulation of Choline Acetyltransferase Protein Stability and Activity by HSC/HSP70, HSP90, and p97/VCP. |
| Q47115164 | Combined x-ray crystallography and computational modeling approach to investigate the Hsp90 C-terminal peptide binding to FKBP51. |
| Q93372373 | Dynamic Phosphorylation of the C Terminus of Hsp70 Regulates the Mitochondrial Import of SOD2 and Redox Balance |
| Q89978558 | HSP70 Multi-Functionality in Cancer |
| Q28771720 | HSP70 regulates the function of mitotic centrosomes |
| Q92593512 | Hsp70 and DNAJA2 limit CFTR levels through degradation |
| Q93249519 | Human Stress-inducible Hsp70 Has a High Propensity to Form ATP-dependent Antiparallel Dimers That Are Differentially Regulated by Cochaperone Binding |
| Q39346211 | Multiple functions of the E3 ubiquitin ligase CHIP in immunity |
| Q47673940 | Natural (and Unnatural) Small Molecules as Pharmacological Chaperones and Inhibitors in Cancer. |
| Q41098204 | Novel Entropically Driven Conformation-specific Interactions with Tomm34 Protein Modulate Hsp70 Protein Folding and ATPase Activities |
| Q47104372 | Novel galeterone analogs act independently of AR and AR-V7 for the activation of the unfolded protein response and induction of apoptosis in the CWR22Rv1 prostate cancer cell model. |
| Q37465994 | PARP1 regulates the protein stability and proapoptotic function of HIPK2. |
| Q94686440 | Pharmacological inhibition of PRMT7 links arginine monomethylation to the cellular stress response |
| Q30674391 | Protein-Protein Interactions Modulate the Docking-Dependent E3-Ubiquitin Ligase Activity of Carboxy-Terminus of Hsc70-Interacting Protein (CHIP) |
| Q41884789 | Specific Binding of Tetratricopeptide Repeat Proteins to Heat Shock Protein 70 (Hsp70) and Heat Shock Protein 90 (Hsp90) Is Regulated by Affinity and Phosphorylation |
| Q38994404 | The Evolutionarily Conserved E3 Ubiquitin Ligase AtCHIP Contributes to Plant Immunity |
| Q64057115 | The cochaperone CHIP marks Hsp70- and Hsp90-bound substrates for degradation through a very flexible mechanism |
| Q39144895 | The remarkable multivalency of the Hsp70 chaperones |
| Q37214887 | UBQLN2 Mediates Autophagy-Independent Protein Aggregate Clearance by the Proteasome |
| Q58766271 | UBXN2A enhances CHIP-mediated proteasomal degradation of oncoprotein mortalin-2 in cancer cells |
| Q50698146 | [Mechanism of heat shock protein 90 for regulating 26S proteasome in hyperthermia]. |
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