Investigation of flap flexibility of β-secretase using molecular dynamic simulations.
about
Enzyme Tunnels and Gates As Relevant Targets in Drug Design.Unveiling a novel transient druggable pocket in BACE-1 through molecular simulations: Conformational analysis and binding mode of multisite inhibitors.Understanding the structural basis of substrate recognition by Plasmodium falciparum plasmepsin V to aid in the design of potent inhibitors.Differential flap dynamics in l,d-transpeptidase2 from mycobacterium tuberculosis revealed by molecular dynamics.Population density analysis for determining the protonation state of the catalytic dyad in BACE1-tertiary carbinamine-based inhibitor complex.Sequence, Structural Analysis and Metrics to Define the Unique Dynamic Features of the Flap Regions Among Aspartic Proteases.A comparative molecular dynamics study on BACE1 and BACE2 flap flexibility.
P2860
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P2860
Investigation of flap flexibility of β-secretase using molecular dynamic simulations.
description
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2015年の論文
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2015年学术文章
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Investigation of flap flexibility of β-secretase using molecular dynamic simulations.
@en
Investigation of flap flexibility of β-secretase using molecular dynamic simulations.
@nl
type
label
Investigation of flap flexibility of β-secretase using molecular dynamic simulations.
@en
Investigation of flap flexibility of β-secretase using molecular dynamic simulations.
@nl
prefLabel
Investigation of flap flexibility of β-secretase using molecular dynamic simulations.
@en
Investigation of flap flexibility of β-secretase using molecular dynamic simulations.
@nl
P2860
P1476
Investigation of flap flexibility of β-secretase using molecular dynamic simulations.
@en
P2093
Hezekiel M Kumalo
Soumendranath Bhakat
P2860
P304
P356
10.1080/07391102.2015.1064831
P577
2015-07-28T00:00:00Z