PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 20146531-9 2010 Formation of a complex with intact Hsp70 and Hsp90 or their respective C-terminal octapeptides induced folding of the TPR domain to a defined, highly stabilized structure with protected amide hydrogens. Hydrogen 192-201 heat shock protein 90 alpha family class A member 1 Homo sapiens 45-50 16165354-1 2005 The 7-carbamate groups of geldanamycin and its 17-(2-dimethylaminoethyl)amino-17-demethoxy derivative (17-DMAG) bind the N-terminal domain of Hsp90 by establishing a network of hydrogen bonds which involve four buried water molecules. Hydrogen 177-185 heat shock protein 90 alpha family class A member 1 Homo sapiens 142-147 16565516-3 2006 Titration of p23 with Hsp90 results in the selective broadening of certain cross-peaks in the 15N-1H heteronuclear single quantum correlation (HSQC) spectrum. Hydrogen 98-100 heat shock protein 90 alpha family class A member 1 Homo sapiens 22-27 20373211-3 2010 In order to identify essential chemical functional features for Hsp90 inhibition, a pharmacophore model consisting of one hydrogen bond donor, two hydrogen bond acceptor lipid and one hydrophobic feature has been developed using Hypogen (Catalyst 2.0 software) on a total set of 103 inhibitors consisting of 16 and 87 compounds in the training and the test set, respectively. Hydrogen 122-130 heat shock protein 90 alpha family class A member 1 Homo sapiens 64-69 17764690-3 2007 Hydrogen-exchange mass spectrometry was used to study the structural and conformational changes undergone by full-length human Hsp90beta in solution upon binding of the kinase-specific co-chaperone Cdc37 and two Hsp90 ATPase inhibitors: Radicicol and the first-generation anticancer drug DMAG. Hydrogen 0-8 heat shock protein 90 alpha family class A member 1 Homo sapiens 127-132 17764690-4 2007 Changes in hydrogen exchange pattern in the complexes in regions of Hsp90 remote to the ligand-binding site were observed indicating long-range effects. Hydrogen 11-19 heat shock protein 90 alpha family class A member 1 Homo sapiens 68-73 15713410-4 2005 The pyrazole ring forms hydrogen bonds to the backbone carbonyl of Gly97, the hydroxyl group of Thr184 and to a water molecule, which is present in all of the published HSP90 structures. Hydrogen 24-32 heat shock protein 90 alpha family class A member 1 Homo sapiens 169-174 34770993-6 2021 Together, GAS are new Hsp90 inhibitors by binding to Hsp90 (hydrogen bond and hydrophobic interaction). Hydrogen 60-68 heat shock protein 90 alpha family class A member 1 Homo sapiens 22-27 34770993-6 2021 Together, GAS are new Hsp90 inhibitors by binding to Hsp90 (hydrogen bond and hydrophobic interaction). Hydrogen 60-68 heat shock protein 90 alpha family class A member 1 Homo sapiens 53-58 34286666-11 2021 HighlightsHsp90 inhibitors that entered different phases of clinical trials were subjected to Zinc15 based structure query to afford potential enzyme inhibitors 19 and 20.Quantum chemical calculations confirmed docking results and verified pivotal role of a conserved residues (Asn51, Leu103, Phe138 and Tyr139) in making effective hydrogen bonds.MD simulations of top-ranked docked derivatives revealed the achievement of stable binding modes with less conformational variation of 20 than 19 in the active site of Hsp90-alpha NTD.H-bond, hydrophobic contacts and salt bridge interactions were determinant forces in binding interactions of in silico hits.Resorcinol and isoxazole were important structural motifs of in silico hits in binding to the active site of Hsp90-alpha NTD.Communicated by Ramaswamy H. Sarma. Hydrogen 332-340 heat shock protein 90 alpha family class A member 1 Homo sapiens 515-526 35429283-5 2022 Molecular modeling studies also confirmed possible mode of interaction between 6u and the binding sites of HSP90 by hydrogen bond and hydrophobic interactions. Hydrogen 116-124 heat shock protein 90 alpha family class A member 1 Homo sapiens 107-112 31141217-4 2019 The two inhibitor-bound structures reveal that Ser52, a nonconserved residue in the ATP binding pocket in Hsp90alpha, provides additional stability to PU-11-trans through a water-mediated hydrogen-bonding network. Hydrogen 188-196 heat shock protein 90 alpha family class A member 1 Homo sapiens 106-116 32812680-2 2020 A large-scale analysis of Hsp90alpha:inhibitor structures shows that inhibitor hydrogen-bonding to a conserved aspartate (D93 in Hsp90alpha) stands out as most universal among Hsp90 inhibitors. Hydrogen 79-87 heat shock protein 90 alpha family class A member 1 Homo sapiens 26-36 32812680-2 2020 A large-scale analysis of Hsp90alpha:inhibitor structures shows that inhibitor hydrogen-bonding to a conserved aspartate (D93 in Hsp90alpha) stands out as most universal among Hsp90 inhibitors. Hydrogen 79-87 heat shock protein 90 alpha family class A member 1 Homo sapiens 129-139 32812680-2 2020 A large-scale analysis of Hsp90alpha:inhibitor structures shows that inhibitor hydrogen-bonding to a conserved aspartate (D93 in Hsp90alpha) stands out as most universal among Hsp90 inhibitors. Hydrogen 79-87 heat shock protein 90 alpha family class A member 1 Homo sapiens 26-31 32812680-8 2020 While aspartate and asparagine sidechains can both act as hydrogen bond acceptors, we show that a steric clash prevents the Hsp90 Asp93 Asn sidechain from adopting the necessary rotamer, whereas this steric restriction is absent in Topoisomerasese II. Hydrogen 58-66 heat shock protein 90 alpha family class A member 1 Homo sapiens 124-129 31725288-6 2019 Together, 41 is a novel Hsp90-Cdc37 disruptor by binding to Cdc37 (hydrogen bond and/or covalent bond). Hydrogen 67-75 heat shock protein 90 alpha family class A member 1 Homo sapiens 24-29 31518867-5 2019 Molecular docking studies suggest that the binding process of these compounds with heat shock protein 90 (Hsp90), BHb and HHb is a spontaneous molecular interaction process, in which van der Waals forces and hydrogen bonds play major roles, and pi-pi interaction also has influence on binding process. Hydrogen 208-216 heat shock protein 90 alpha family class A member 1 Homo sapiens 83-104 31518867-5 2019 Molecular docking studies suggest that the binding process of these compounds with heat shock protein 90 (Hsp90), BHb and HHb is a spontaneous molecular interaction process, in which van der Waals forces and hydrogen bonds play major roles, and pi-pi interaction also has influence on binding process. Hydrogen 208-216 heat shock protein 90 alpha family class A member 1 Homo sapiens 106-111 35056725-1 2022 In the context of our SAR study concerning 6BrCaQ analogues as C-terminal Hsp90 inhibitors, we designed and synthesized a novel series of 3-(heteroaryl)quinolin-2(1H), of types 3, 4, and 5, as a novel class of analogues. Hydrogen 163-165 heat shock protein 90 alpha family class A member 1 Homo sapiens 74-79 32527460-10 2020 Molecular docking studies suggested mode of interaction to HSP90 via hydrogen bonding. Hydrogen 69-77 heat shock protein 90 alpha family class A member 1 Homo sapiens 59-64 31560152-6 2020 The results indicate that 20 residues in group A of the hierarchical tree are responsible for major contributions, and van der Waals interactions as well as hydrogen bonding interactions between important residues in HSP90 and key regions of inhibitors are the main force for promoting inhibitor bindings. Hydrogen 157-165 heat shock protein 90 alpha family class A member 1 Homo sapiens 217-222 31493740-4 2019 In the present in silico investigation, a structure-based pharmacophore model was generated with hydrogen bond donor, hydrogen bond acceptor and hydrophobic features complementary to crucial residues Ala55, Lys58, Asp93, Ile96, Met98 and Thr184 directed at inhibiting the ATP-binding activity of Hsp90. Hydrogen 97-105 heat shock protein 90 alpha family class A member 1 Homo sapiens 296-301 28426997-5 2017 Further molecular dynamics simulation indicated that the hydrophobic interactions as well as the hydrogen bonds contributed to the high affinity of 9p to Hsp90. Hydrogen 97-105 heat shock protein 90 alpha family class A member 1 Homo sapiens 154-159 30869872-0 2019 The Hsp90 Chaperone: 1H and 19F Dynamic Nuclear Magnetic Resonance Spectroscopy Reveals a Perfect Enzyme. Hydrogen 21-23 heat shock protein 90 alpha family class A member 1 Homo sapiens 4-9 30869872-3 2019 We used 19F and 1H dynamic nuclear magnetic resonance (NMR) spectroscopy to study the opening and closing kinetics of Hsp90 and to determine the kcat for ATP hydrolysis. Hydrogen 16-18 heat shock protein 90 alpha family class A member 1 Homo sapiens 118-123 30827868-5 2019 The molecular modeling of 57 demonstrated that 57 bound well to the C-terminal ATP-binding pocket in the open conformation of the hHSP90 homodimer with hydrogen bonding and pi-cation interactions. Hydrogen 152-160 heat shock protein 90 alpha family class A member 1 Homo sapiens 130-136 29564982-11 2018 The molecular docking analysis of compound m45 with the N-terminal domain binding site of the HSP90 show hydroxyl group on phenyl ring is necessary to form hydrogen bonding with hydrophilic residues in binding site and a conserved water molecule. Hydrogen 156-164 heat shock protein 90 alpha family class A member 1 Homo sapiens 94-99 26100249-4 2015 Molecular docking simulation analysis revealed that curcumin fit well in the binding pocket of Hsp90, with hydrogen bonds, hydrophobic interactions and conjugation to maintain adhesion. Hydrogen 107-115 heat shock protein 90 alpha family class A member 1 Homo sapiens 95-100 26056257-6 2015 Molecular dynamics simulations and hydrogen/deuterium exchange of Hsp90-dependent Src kinase variants further reveal increased transitions between inactive and active states and exposure of specific kinase regions. Hydrogen 35-43 heat shock protein 90 alpha family class A member 1 Homo sapiens 66-71 24726919-7 2014 Moreover, native-state hydrogen exchange indicates that Hsp90 can also interact with partially folded states only transiently populated from within a thermodynamically stable, native-state ensemble. Hydrogen 23-31 heat shock protein 90 alpha family class A member 1 Homo sapiens 56-61