PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 34185514-6 2021 Moreover, pH-dependent protonation exerts a significant effect on the hydrogen bonding interactions of CS9, C6U, and 6WE to BACE1, which correspondingly alters the binding abilities of the three inhibitors to BACE1. Hydrogen 70-78 beta-secretase 1 Homo sapiens 124-129 34185514-6 2021 Moreover, pH-dependent protonation exerts a significant effect on the hydrogen bonding interactions of CS9, C6U, and 6WE to BACE1, which correspondingly alters the binding abilities of the three inhibitors to BACE1. Hydrogen 70-78 beta-secretase 1 Homo sapiens 209-214 33352819-0 2020 Evaluation of High-Temperature Hydrogen Sensors Based on BaCe0.6Zr0.3Y0.1O3-alpha and Sr(Ce0.9Zr0.1)0.95Yb0.05O3-alpha Perovskites for Industrial Applications. Hydrogen 31-39 beta-secretase 1 Homo sapiens 57-61 33352819-5 2020 In the present work, amperometric hydrogen sensors were constructed and evaluated using two solid-state electrolytes, BaCe0.6Zr0.3Y0.1O3-alpha and Sr(Ce0.9Zr0.1)0.95Yb0.05O3-alpha. Hydrogen 34-42 beta-secretase 1 Homo sapiens 118-122 29444415-8 2018 It interacted with important amino acid residues in BACE1, such as ASN37, GLN73, and TRP76, through hydrogen bonding. Hydrogen 100-108 beta-secretase 1 Homo sapiens 52-57 31654211-8 2019 The hydrogen-bond interactions, hydrophobic contacts, and pi-pi stacking interactions of BTT with flap residues (Val67-Asp77) of BACE1 confine the movement of the flap and help to achieve closed (non-active) conformation. Hydrogen 4-12 beta-secretase 1 Homo sapiens 129-134 29310523-8 2019 Hydrogen bond occupancy of NS7 and NS9 generated from MD trajectories showed good interaction with the flap residues Gln73, Thr72 of BACE-1 and Arg141, Thr138 residues of GSK-3beta. Hydrogen 0-8 beta-secretase 1 Homo sapiens 133-139 31865778-6 2020 present within to an aromatic nucleus and the structural features such as hydrophobic, ring aromatic and hydrogen bond acceptor/donor are responsible for the enhancement of the BACE1 enzyme inhibitory activity. Hydrogen 105-113 beta-secretase 1 Homo sapiens 177-182 29966870-3 2018 Profiling of donepezil, a potent acetylcholinesterase (hAChE) inhibitor, into BACE-1 inhibition was achieved through introduction of backbone amide linkers to the designed compounds which are capable of hydrogen-bonding with BACE-1 catalytic site. Hydrogen 203-211 beta-secretase 1 Homo sapiens 78-84 29910719-4 2018 The molecular docking results show that AZD3293 binds within the active region of BACE1 by forming hydrogen bonds against Asp32 and Lys107 with distances 2.95 and 2.68 A, respectively. Hydrogen 99-107 beta-secretase 1 Homo sapiens 82-87 28081663-6 2018 This study focuses on analyses of 153 BACE1-ligand complexes for the direct contacts (hydrogen bonds and weak interactions) observed between protein and ligand and indirect contacts (water-mediated hydrogen bonds), observed in BACE1-ligand complex crystal structures. Hydrogen 86-94 beta-secretase 1 Homo sapiens 38-43 28081663-6 2018 This study focuses on analyses of 153 BACE1-ligand complexes for the direct contacts (hydrogen bonds and weak interactions) observed between protein and ligand and indirect contacts (water-mediated hydrogen bonds), observed in BACE1-ligand complex crystal structures. Hydrogen 198-206 beta-secretase 1 Homo sapiens 38-43 28081663-6 2018 This study focuses on analyses of 153 BACE1-ligand complexes for the direct contacts (hydrogen bonds and weak interactions) observed between protein and ligand and indirect contacts (water-mediated hydrogen bonds), observed in BACE1-ligand complex crystal structures. Hydrogen 198-206 beta-secretase 1 Homo sapiens 227-232 21942621-4 2011 In contrast, the network of hydrogen bonds in the active site is more stable in the complex of BACE with the gem-diol intermediate than the other two states of the substrate. Hydrogen 28-36 beta-secretase 1 Homo sapiens 95-99 28413992-4 2017 RESULTS: It was found that hydrogen bond interactions play a significant role in the accurate positioning of ligands within the "active site" of BACE1 to permit docking. Hydrogen 27-35 beta-secretase 1 Homo sapiens 145-150 28869548-5 2017 Docking analysis results for complexes with BACE1 indicated that SER10 and THR232 residues of BACE1 hydrogen bonded with two oxygen atoms of tangeretin, while three additional BACE1 residues (ALA157, VAL336 and THR232) interacted with three oxygen atoms of nobiletin. Hydrogen 100-108 beta-secretase 1 Homo sapiens 44-49 28869548-5 2017 Docking analysis results for complexes with BACE1 indicated that SER10 and THR232 residues of BACE1 hydrogen bonded with two oxygen atoms of tangeretin, while three additional BACE1 residues (ALA157, VAL336 and THR232) interacted with three oxygen atoms of nobiletin. Hydrogen 100-108 beta-secretase 1 Homo sapiens 94-99 28869548-5 2017 Docking analysis results for complexes with BACE1 indicated that SER10 and THR232 residues of BACE1 hydrogen bonded with two oxygen atoms of tangeretin, while three additional BACE1 residues (ALA157, VAL336 and THR232) interacted with three oxygen atoms of nobiletin. Hydrogen 100-108 beta-secretase 1 Homo sapiens 94-99 28728105-8 2017 Molecular docking revealed that the nitrogen atom of imidazopyridines and the oxygen atom of the phenoxypropyl linker were involved in hydrogen bound interactions with Asp228 and Asp32 of BACE1 active site, respectively. Hydrogen 135-143 beta-secretase 1 Homo sapiens 188-193 28728106-3 2017 And the introduce of connecting amide bonds, enables the target molecules provide sufficient hydrogen bond donors and acceptors to interact with the catalytic site of BACE-1. Hydrogen 93-101 beta-secretase 1 Homo sapiens 167-173 27639619-4 2016 The results show that selective BACE1 inhibition may be due to the formation of strong electrostatic interactions with Asp32 and Asp228 and a large number of hydrogen bonds, pi-pi and Van der Waals interactions with the amino acid residues located inside the catalytic cavity, which has different volume and shape compared to BACE2 and CTSD. Hydrogen 158-166 beta-secretase 1 Homo sapiens 32-37 27697060-7 2016 Both, hydrogen bond and hydrophobic interactions were found to be involved in the proper positioning of these diabetic drugs within the catalytic site (CAS) of AChE and BACE enzymes to permit docking. Hydrogen 6-14 beta-secretase 1 Homo sapiens 169-173 25863345-7 2015 Binding of APP to the BACE1 cavity shifts the equilibrium towards a stable complex stabilized by strong electrostatic surface complementarity along with several van der Waals and hydrogen bonding interactions. Hydrogen 179-187 beta-secretase 1 Homo sapiens 22-27 20620068-5 2010 The most effective BACE 1 inhibitor 9f (27.85+/-2.46 micromol/L) was selected for further receptor-binding studies, the result of which indicated that an essential hydrogen bonds was formed between the urea group of 9f and the catalytic aspartate Asp228. Hydrogen 164-172 beta-secretase 1 Homo sapiens 19-25 21183353-4 2011 The most potent inhibitor, tert-alcohol containing (R)-12 (IC(50)=0.19muM) was co-crystallized in the active site of the BACE-1 protease, furnishing a novel binding mode in which the N-terminal amine makes a hydrogen bond to one of the catalytic aspartic acids. Hydrogen 208-216 beta-secretase 1 Homo sapiens 121-127 20806954-9 2010 The hydrogen bonds formed between the INH peptide, residues Tyr1, Tyr3, and Leu7 with the BACE1 residues Leu267, Cys269, Trp270, Asp311, and Asp 317 can strengthen the binding of the BACE1-INH complex. Hydrogen 4-12 beta-secretase 1 Homo sapiens 90-95 20806954-9 2010 The hydrogen bonds formed between the INH peptide, residues Tyr1, Tyr3, and Leu7 with the BACE1 residues Leu267, Cys269, Trp270, Asp311, and Asp 317 can strengthen the binding of the BACE1-INH complex. Hydrogen 4-12 beta-secretase 1 Homo sapiens 183-188 18249539-4 2008 Herein, we replaced acidic moieties at the P(4) position with other hydrogen bond acceptor groups, and these inhibitors exhibited improved BACE1 inhibitory activities in cultured cells. Hydrogen 68-76 beta-secretase 1 Homo sapiens 139-144 15845357-9 2005 Although the overall structures of the three enzymes are quite similar to each other, some subtle difference around their active sites that distinguishes cathepsin-E from cathepsin-D and BACE1 has been revealed through an analysis of hydrogen bond network and microenvironment. Hydrogen 234-242 beta-secretase 1 Homo sapiens 187-192 19284778-3 2009 For one such hit class, defined by a central aminobenzylpiperidine (ABP) moiety, X-ray crystal structures of BACE mutant-disulfide conjugates revealed that the fragment bound by engaging both catalytic aspartates with hydrogen bonds. Hydrogen 218-226 beta-secretase 1 Homo sapiens 109-113 17685503-2 2007 X-ray crystallography revealed that the exocyclic amino group participated in a hydrogen bonding array with the two catalytic aspartic acids of BACE-1 (Asp(32), Asp(228)). Hydrogen 80-88 beta-secretase 1 Homo sapiens 144-150