Conservation of polar residues as hot spots at protein interfaces.
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Perturbation of the Dimer Interface of Triosephosphate Isomerase and its Effect on Trypanosoma cruziMolecular determinants for antibody binding on group 1 house dust mite allergens.Human cancer protein-protein interaction network: a structural perspectiveJoint evolutionary trees: a large-scale method to predict protein interfaces based on sequence samplingDrug targets for cell cycle dysregulators in leukemogenesis: in silico docking studiesProgress and challenges in predicting protein interfacesStructural mapping of protein interactions reveals differences in evolutionary pressures correlated to mRNA level and protein abundanceA simple physical model for binding energy hot spots in protein-protein complexesDevelopment of unified statistical potentials describing protein-protein interactions.ECMIS: computational approach for the identification of hotspots at protein-protein interfaces.Algorithmic approaches to protein-protein interaction site prediction.Screening for clusters of charge in human virus proteomesPrediction of binding hot spot residues by using structural and evolutionary parameters.A novel method for protein-protein interaction site prediction using phylogenetic substitution models.Identification of hot-spot residues in protein-protein interactions by computational docking.A new, structurally nonredundant, diverse data set of protein-protein interfaces and its implicationsMultiple diverse ligands binding at a single protein site: a matter of pre-existing populations.Docking protein domains in contact space.Identification of hot regions in protein-protein interactions by sequential pattern mining.Prediction of protein-protein binding site by using core interface residue and support vector machineSitesIdentify: a protein functional site prediction tool.Tradeoff between stability and multispecificity in the design of promiscuous proteins.Conserved residue clusters at protein-protein interfaces and their use in binding site identification.Alanine-shaving mutagenesis to determine key interfacial residues governing the assembly of a nano-cage maxi-ferritinRigorous assessment and integration of the sequence and structure based features to predict hot spots.Hotspot-centric de novo design of protein binders.From laptop to benchtop to bedside: structure-based drug design on protein targets.How similar are protein folding and protein binding nuclei? Examination of vibrational motions of energy hot spots and conserved residuesReduced polymorphism in domains involved in protein-protein interactions.Structural and functional characterization of mature forms of metalloprotease E495 from Arctic sea-ice bacterium Pseudoalteromonas sp. SM495.Prediction and redesign of protein-protein interactionsIdentification of protein oligomerization states by analysis of interface conservation.Protein binding site prediction using an empirical scoring functionHot spots in a network of functional sites.Protein-protein interactions: structurally conserved residues distinguish between binding sites and exposed protein surfacesIdentification of an anchor residue for CheA-CheY interactions in the chemotaxis system of Escherichia coli.ATPase subdomain IA is a mediator of interdomain allostery in Hsp70 molecular chaperones.The effect of macromolecular crowding on the electrostatic component of barnase-barstar binding: a computational, implicit solvent-based study.Identification of protein-ligand binding sites by the level-set variational implicit-solvent approachAn in vitro and in vivo disconnect uncovered through high-throughput identification of botulinum neurotoxin A antagonists.
P2860
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P2860
Conservation of polar residues as hot spots at protein interfaces.
description
2000 nî lūn-bûn
@nan
2000年の論文
@ja
2000年学术文章
@wuu
2000年学术文章
@zh-cn
2000年学术文章
@zh-hans
2000年学术文章
@zh-my
2000年学术文章
@zh-sg
2000年學術文章
@yue
2000年學術文章
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2000年學術文章
@zh-hant
name
Conservation of polar residues as hot spots at protein interfaces.
@en
Conservation of polar residues as hot spots at protein interfaces.
@nl
type
label
Conservation of polar residues as hot spots at protein interfaces.
@en
Conservation of polar residues as hot spots at protein interfaces.
@nl
prefLabel
Conservation of polar residues as hot spots at protein interfaces.
@en
Conservation of polar residues as hot spots at protein interfaces.
@nl
P2093
P1433
P1476
Conservation of polar residues as hot spots at protein interfaces.
@en
P2093
P304
P356
10.1002/(SICI)1097-0134(20000601)39:4<331::AID-PROT60>3.3.CO;2-1
P407
P50
P577
2000-06-01T00:00:00Z