Binding of a reduced peptide inhibitor to the aspartic proteinase from Rhizopus chinensis: implications for a mechanism of action
about
Molecular surface recognition: determination of geometric fit between proteins and their ligands by correlation techniquesComputational Insights into Substrate and Site Specificities, Catalytic Mechanism, and Protonation States of the Catalytic Asp Dyad of β -SecretaseCrystal structure of cardosin A, a glycosylated and Arg-Gly-Asp-containing aspartic proteinase from the flowers of Cynara cardunculus LAtomic resolution analysis of the catalytic site of an aspartic proteinase and an unexpected mode of binding by short peptidesDirect observation by X-ray analysis of the tetrahedral “intermediate” of aspartic proteinasesInsights from Atomic-Resolution X-Ray Structures of Chemically Synthesized HIV-1 Protease in Complex with InhibitorsThe Catalytic Mechanism of an Aspartic Proteinase Explored with Neutron and X-ray DiffractionCrystallographic Insights into the Autocatalytic Assembly Mechanism of a Bacteriophage Tail SpikeProtein conformational dynamics in the mechanism of HIV-1 protease catalysisCamel and bovine chymosin: the relationship between their structures and cheese-making propertiesX-ray crystallographic structure of a complex between a synthetic protease of human immunodeficiency virus 1 and a substrate-based hydroxyethylamine inhibitorCrystal structure of a putative aspartic proteinase domain of theMycobacterium tuberculosiscell surface antigen PE_PGRS16The structure of endothiapepsin complexed with a Phe-Tyr reduced-bond inhibitor at 1.35 Å resolutionHigh-resolution X-ray diffraction study of the complex between endothiapepsin and an oligopeptide inhibitor: the analysis of the inhibitor binding and description of the rigid body shift in the enzymeX-ray-crystallographic studies of complexes of pepstatin A and a statine-containing human renin inhibitor with endothiapepsinIn vitro inhibition of HIV-1 proteinase by ceruleninInhibition of human immunodeficiency virus 1 protease in vitro: rational design of substrate analogue inhibitorsAnalysis of crystal structures of aspartic proteinases: on the role of amino acid residues adjacent to the catalytic site of pepsin-like enzymesConformational Dynamics and Binding Free Energies of Inhibitors of BACE-1: From the Perspective of Protonation EquilibriaPenicillopepsin-JT2, a recombinant enzyme from Penicillium janthinellum and the contribution of a hydrogen bond in subsite S3 to k(cat).Structural studies of vacuolar plasmepsinsValidating the vitality strategy for fighting drug resistance.Engineering the substrate specificity of rhizopuspepsin: the role of Asp 77 of fungal aspartic proteinases in facilitating the cleavage of oligopeptide substrates with lysine in P1Preliminary neutron and ultrahigh-resolution X-ray diffraction studies of the aspartic proteinase endothiapepsin cocrystallized with a gem-diol inhibitor.Catalytic contribution of flap-substrate hydrogen bonds in "HIV-1 protease" explored by chemical synthesis.Analysis of the structure of chemically synthesized HIV-1 protease complexed with a hexapeptide inhibitor. Part I: Crystallographic refinement of 2 A data.Comparative modeling of proteins in the design of novel renin inhibitors.The function of cathepsins B, D, and X in atherosclerosis.HIV-1 protease as a potential target for anti-AIDS therapy.A role for the aspartyl protease from the human immunodeficiency virus type 1 (HIV-1) in the orchestration of virus assembly.Looking at the proteases from a simple perspective.Computational insights into the development of novel therapeutic strategies for Alzheimer's disease.Dynamic and Electrostatic Effects on the Reaction Catalyzed by HIV-1 Protease.Molecular dynamics studies on both bound and unbound renin protease.Fullerene-based inhibitors of HIV-1 protease.A structural comparison of 21 inhibitor complexes of the aspartic proteinase from Endothia parasitica.Active site specificity of plasmepsin IIStoneHinge: hinge prediction by network analysis of individual protein structures.Assigning the protonation states of the key aspartates in β-Secretase using QM/MM X-ray structure refinementMolecular-dynamics investigation of molecular flexibility in ligand binding.
P2860
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P2860
Binding of a reduced peptide inhibitor to the aspartic proteinase from Rhizopus chinensis: implications for a mechanism of action
description
1987 nî lūn-bûn
@nan
1987 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած
@hyw
1987 թվականի հոտեմբերին հրատարակված գիտական հոդված
@hy
1987年の論文
@ja
1987年論文
@yue
1987年論文
@zh-hant
1987年論文
@zh-hk
1987年論文
@zh-mo
1987年論文
@zh-tw
1987年论文
@wuu
name
Binding of a reduced peptide i ...... ions for a mechanism of action
@ast
Binding of a reduced peptide i ...... ions for a mechanism of action
@en
Binding of a reduced peptide i ...... ions for a mechanism of action
@nl
type
label
Binding of a reduced peptide i ...... ions for a mechanism of action
@ast
Binding of a reduced peptide i ...... ions for a mechanism of action
@en
Binding of a reduced peptide i ...... ions for a mechanism of action
@nl
prefLabel
Binding of a reduced peptide i ...... ions for a mechanism of action
@ast
Binding of a reduced peptide i ...... ions for a mechanism of action
@en
Binding of a reduced peptide i ...... ions for a mechanism of action
@nl
P2093
P2860
P356
P1476
Binding of a reduced peptide i ...... ions for a mechanism of action
@en
P2093
P2860
P304
P356
10.1073/PNAS.84.20.7009
P407
P577
1987-10-01T00:00:00Z