| scholarly article | Q13442814 |
| P356 | DOI | 10.1074/JBC.M115.645515 |
| P8608 | Fatcat ID | release_3bfh3cbcwnaobe2nkvkruuvlvy |
| P932 | PMC publication ID | 4571885 |
| P698 | PubMed publication ID | 26134567 |
| P50 | author | Saurav Misra | Q57421650 |
| Arnab Ghosh | Q61095291 | ||
| Yue Dai | Q89354214 | ||
| P2093 | author name string | William R Montfort | |
| Dennis J Stuehr | |||
| Elsa D Garcin | |||
| Franziska Seeger | |||
| Stanley L Hazen | |||
| Mohammad Mahfuzul Haque | |||
| Anindya Sarkar | |||
| P2860 | cites work | Quantitative analysis of HSP90-client interactions reveals principles of substrate recognition | Q24297748 |
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| Hsp90-Tau complex reveals molecular basis for specificity in chaperone action | Q24338439 | ||
| Improving the physical realism and structural accuracy of protein models by a two-step atomic-level energy minimization | Q24626539 | ||
| Atomic-level protein structure refinement using fragment-guided molecular dynamics conformation sampling | Q24627931 | ||
| Modulation of Akt kinase activity by binding to Hsp90 | Q24648565 | ||
| The Protein Model Portal | Q24654800 | ||
| The hexameric structures of human heat shock protein 90 | Q27340111 | ||
| A unique mechanism of chaperone action: heme regulation of Hap1 activity involves separate control of repression and activation. | Q37516183 | ||
| YC-1 binding to the β subunit of soluble guanylyl cyclase overcomes allosteric inhibition by the α subunit. | Q37557818 | ||
| The function of NO-sensitive guanylyl cyclase: what we can learn from genetic mouse models | Q37563705 | ||
| Single-particle EM reveals the higher-order domain architecture of soluble guanylate cyclase | Q37612777 | ||
| Nitric oxide-induced conformational changes in soluble guanylate cyclase | Q37727207 | ||
| The network interaction of the human cytosolic 90 kDa heat shock protein Hsp90: A target for cancer therapeutics. | Q37975002 | ||
| Structure and regulation of soluble guanylate cyclase | Q37992160 | ||
| The therapeutic target Hsp90 and cancer hallmarks | Q38037753 | ||
| Hsp90: structure and function | Q38041439 | ||
| Structure, function and regulation of the hsp90 machinery | Q38117496 | ||
| The universe of Hsp90. | Q38273054 | ||
| Modulation of the Hsp90 chaperone cycle by a stringent client protein | Q39016987 | ||
| RACK1 competes with HSP90 for binding to HIF-1alpha and is required for O(2)-independent and HSP90 inhibitor-induced degradation of HIF-1alpha | Q40179965 | ||
| Hypoxia-induced activation of HIF-1: role of HIF-1alpha-Hsp90 interaction | Q40920382 | ||
| Hsp90 regulates NADPH oxidase activity and is necessary for superoxide but not hydrogen peroxide production | Q41791230 | ||
| Structural analysis of the interaction between Hsp90 and the tumor suppressor protein p53. | Q41792117 | ||
| The activation mechanism of the aryl hydrocarbon receptor (AhR) by molecular chaperone HSP90. | Q41975121 | ||
| Heat shock protein 90 regulates stabilization rather than activation of soluble guanylate cyclase | Q42030989 | ||
| Heat shock protein 90 mediates the balance of nitric oxide and superoxide anion from endothelial nitric-oxide synthase | Q43559219 | ||
| Conformational dynamics of the molecular chaperone Hsp90 in complexes with a co-chaperone and anticancer drugs. | Q48542831 | ||
| Dimerization region of soluble guanylate cyclase characterized by bimolecular fluorescence complementation in vivo. | Q51795151 | ||
| Four-colour FRET reveals directionality in the Hsp90 multicomponent machinery. | Q54286902 | ||
| Phosphorylation of a heme-regulated eukaryotic initiation factor 2α kinase enhances the interaction with heat-shock protein 90 and substantially upregulates kinase activity. | Q54572043 | ||
| Mapping the 90 kDa heat shock protein binding region of the Ah receptor | Q71584120 | ||
| Role of heat shock protein 90 dissociation in mediating agonist-induced activation of the aryl hydrocarbon receptor | Q73316901 | ||
| Structural and functional analysis of the middle segment of hsp90: implications for ATP hydrolysis and client protein and cochaperone interactions | Q27640863 | ||
| NO and CO differentially activate soluble guanylyl cyclase via a heme pivot-bend mechanism | Q27641107 | ||
| PAS-mediated Dimerization of Soluble Guanylyl Cyclase Revealed by Signal Transduction Histidine Kinase Domain Crystal Structure | Q27649070 | ||
| Crystal structure of the signaling helix coiled-coil domain of the β1 subunit of the soluble guanylyl cyclase | Q27659219 | ||
| Tunnels modulate ligand flux in a heme nitric oxide/oxygen binding (H-NOX) domain | Q27675023 | ||
| The architecture of functional modules in the Hsp90 co-chaperone Sti1/Hop | Q27676637 | ||
| Crystal structure of the Alpha subunit PAS domain from soluble guanylyl cyclase | Q27679506 | ||
| HADDOCK: a protein-protein docking approach based on biochemical or biophysical information | Q27860814 | ||
| Features and development of Coot | Q27861079 | ||
| Definition of a minimal domain of the dioxin receptor that is associated with Hsp90 and maintains wild type ligand binding affinity and specificity | Q28289572 | ||
| Interaction between the 90-kDa heat shock protein and soluble guanylyl cyclase: physiological significance and mapping of the domains mediating binding | Q28572045 | ||
| HADDOCK versus HADDOCK: new features and performance of HADDOCK2.0 on the CAPRI targets | Q29615981 | ||
| Crystal structure of an Hsp90-nucleotide-p23/Sba1 closed chaperone complex | Q29617515 | ||
| The HADDOCK web server for data-driven biomolecular docking | Q29617755 | ||
| Endothelium-derived relaxing factor produced and released from artery and vein is nitric oxide | Q29619956 | ||
| Allosteric regulation of the Hsp90 dynamics and stability by client recruiter cochaperones: protein structure network modeling | Q30358343 | ||
| The I-TASSER Suite: protein structure and function prediction. | Q30370293 | ||
| How well can the accuracy of comparative protein structure models be predicted? | Q30372425 | ||
| Higher-order interactions bridge the nitric oxide receptor and catalytic domains of soluble guanylate cyclase. | Q30539237 | ||
| Nitric oxide and heat shock protein 90 activate soluble guanylate cyclase by driving rapid change in its subunit interactions and heme content. | Q34075870 | ||
| Structure-activity relationships in purine-based inhibitor binding to HSP90 isoforms | Q34329097 | ||
| Structure of an Hsp90-Cdc37-Cdk4 complex. | Q34562863 | ||
| Structural Analysis of E. coli hsp90 reveals dramatic nucleotide-dependent conformational rearrangements | Q34575808 | ||
| HSP90 empowers evolution of resistance to hormonal therapy in human breast cancer models | Q34793260 | ||
| Hsp90 interacts with inducible NO synthase client protein in its heme-free state and then drives heme insertion by an ATP-dependent process | Q35003199 | ||
| Client-loading conformation of the Hsp90 molecular chaperone revealed in the cryo-EM structure of the human Hsp90:Hop complex | Q35129923 | ||
| Ligand displaces heat shock protein 90 from overlapping binding sites within the aryl hydrocarbon receptor ligand-binding domain | Q35266378 | ||
| Post-translational modifications of Hsp90 and their contributions to chaperone regulation | Q35581165 | ||
| Modulation of heme/substrate binding cleft of neuronal nitric-oxide synthase (nNOS) regulates binding of Hsp90 and Hsp70 proteins and nNOS ubiquitination | Q35668831 | ||
| Cross-monomer substrate contacts reposition the Hsp90 N-terminal domain and prime the chaperone activity | Q35764464 | ||
| Soluble guanylyl cyclase requires heat shock protein 90 for heme insertion during maturation of the NO-active enzyme | Q36167665 | ||
| Heme as key regulator of major mammalian cellular functions: molecular, cellular, and pharmacological aspects. | Q36411963 | ||
| Uncovering a region of heat shock protein 90 important for client binding in E. coli and chaperone function in yeast. | Q36604957 | ||
| Molecular model of a soluble guanylyl cyclase fragment determined by small-angle X-ray scattering and chemical cross-linking | Q36713981 | ||
| Diversity and conservation of interactions for binding heme in b-type heme proteins. | Q36834143 | ||
| P433 | issue | 35 | |
| P407 | language of work or name | English | Q1860 |
| P304 | page(s) | 21615-21628 | |
| P577 | publication date | 2015-07-01 | |
| P1433 | published in | Journal of Biological Chemistry | Q867727 |
| P1476 | title | Heat Shock Protein 90 Associates with the Per-Arnt-Sim Domain of Heme-free Soluble Guanylate Cyclase: IMplications for Enzyme Maturation | |
| P478 | volume | 290 |
| Q51107142 | D-Glyceraldehyde-3-Phosphate Dehydrogenase Structure and Function. |
| Q48191556 | Hsp90 chaperones hemoglobin maturation in erythroid and nonerythroid cells |
| Q88500342 | Physiological activation and deactivation of soluble guanylate cyclase |
| Q38777323 | Regulation of sGC via hsp90, Cellular Heme, sGC Agonists, and NO: New Pathways and Clinical Perspectives |
| Q58075704 | Sources of Vascular Nitric Oxide and Reactive Oxygen Species and Their Regulation |
| Q38894826 | Structure and Activation of Soluble Guanylyl Cyclase, the Nitric Oxide Sensor |
| Q55436230 | Structure/function of the soluble guanylyl cyclase catalytic domain. |
| Q51216676 | The diverse roles of Hsp90 and where to find them. |
| Q56534524 | Thioredoxin shapes the sensory response to produced nitric oxide |
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