IRECS: a new algorithm for the selection of most probable ensembles of side-chain conformations in protein models.
about
A smoothed backbone-dependent rotamer library for proteins derived from adaptive kernel density estimates and regressionsMolecular basis of telaprevir resistance due to V36 and T54 mutations in the NS3-4A protease of the hepatitis C virusA multiscale approach to characterize the early aggregation steps of the amyloid-forming peptide GNNQQNY from the yeast prion sup-35Incorporating post-translational modifications and unnatural amino acids into high-throughput modeling of protein structures.Assessment of protein side-chain conformation prediction methods in different residue environments.Prediction of side chain orientations in proteins by statistical machine learning methods.Explicit orientation dependence in empirical potentials and its significance to side-chain modelingTemplate-based protein modeling: recent methodological advances.Beyond rotamers: a generative, probabilistic model of side chains in proteins.RASP: rapid modeling of protein side chain conformations.Binary image representation of a ligand binding site: its application to efficient sampling of a conformational ensembleCurrent progress in Structure-Based Rational Drug Design marks a new mindset in drug discoveryPeptidomimetic escape mechanisms arise via genetic diversity in the ligand-binding site of the hepatitis C virus NS3/4A serine protease.Ketoamide resistance and hepatitis C virus fitness in val55 variants of the NS3 serine protease.Multiple sclerosis: Molecular mimicry of an antimyelin HLA class I restricted T-cell receptor.OPUS-Rota: a fast and accurate method for side-chain modeling.Side chain substitution benchmark for peptide/MHC interaction.BiPPred: Combined sequence- and structure-based prediction of peptide binding to the Hsp70 chaperone BiP.GalaxyDock2: protein-ligand docking using beta-complex and global optimization.Bap (Sil1) regulates the molecular chaperone BiP by coupling release of nucleotide and substrate.Amino acid substitutions within HLA-B*27-restricted T cell epitopes prevent recognition by hepatitis delta virus-specific CD8+ T cells.
P2860
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P2860
IRECS: a new algorithm for the selection of most probable ensembles of side-chain conformations in protein models.
description
2007 nî lūn-bûn
@nan
2007 թուականի Յունիսին հրատարակուած գիտական յօդուած
@hyw
2007 թվականի հունիսին հրատարակված գիտական հոդված
@hy
2007年の論文
@ja
2007年論文
@yue
2007年論文
@zh-hant
2007年論文
@zh-hk
2007年論文
@zh-mo
2007年論文
@zh-tw
2007年论文
@wuu
name
IRECS: a new algorithm for the ...... nformations in protein models.
@ast
IRECS: a new algorithm for the ...... nformations in protein models.
@en
IRECS: a new algorithm for the ...... nformations in protein models.
@nl
type
label
IRECS: a new algorithm for the ...... nformations in protein models.
@ast
IRECS: a new algorithm for the ...... nformations in protein models.
@en
IRECS: a new algorithm for the ...... nformations in protein models.
@nl
prefLabel
IRECS: a new algorithm for the ...... nformations in protein models.
@ast
IRECS: a new algorithm for the ...... nformations in protein models.
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IRECS: a new algorithm for the ...... nformations in protein models.
@nl
P2860
P356
P1433
P1476
IRECS: a new algorithm for the ...... nformations in protein models.
@en
P2093
Christoph Hartmann
P2860
P304
P356
10.1110/PS.062658307
P577
2007-06-13T00:00:00Z