about
Sampling and scoring: a marriage made in heavenCAPRI: a Critical Assessment of PRedicted InteractionsThe binding domain structure of retinoblastoma-binding proteinsProtein docking by the underestimation of free energy funnels in the space of encounter complexesEvidence of conformational selection driving the formation of ligand binding sites in protein-protein interfacesNovel druggable hot spots in avian influenza neuraminidase H5N1 revealed by computational solvent mapping of a reduced and representative receptor ensemble.A benchmark testing ground for integrating homology modeling and protein docking.Minimal ensembles of side chain conformers for modeling protein-protein interactionsEmpirical potentials and functions for protein folding and binding.Exploring the binding sites of the haloalkane dehalogenase DhlA from Xanthobacter autotrophicus GJ10.Fragment-based identification of druggable 'hot spots' of proteins using Fourier domain correlation techniques.Discrimination of near-native structures in protein-protein docking by testing the stability of local minima.Where does amantadine bind to the influenza virus M2 proton channel?Robust identification of binding hot spots using continuum electrostatics: application to hen egg-white lysozyme.A membrane model for cytosolic calcium oscillations. A study using Xenopus oocytesFree energy landscapes of encounter complexes in protein-protein associationDynamical view of the positions of key side chains in protein-protein recognitionOptimal clustering for detecting near-native conformations in protein docking.Protein-protein association kinetics and protein docking.FTFlex: accounting for binding site flexibility to improve fragment-based identification of druggable hot spots.Stimulators of translation identified during a small molecule screening campaignNew Frontiers in DruggabilityLessons from Hot Spot Analysis for Fragment-Based Drug Discovery.Toward computational determination of peptide-receptor structure.Empirical free energy calculation: comparison to calorimetric data.Analysis of protein binding sites by computational solvent mapping.The FTMap family of web servers for determining and characterizing ligand-binding hot spots of proteins.Focused grid-based resampling for protein docking and mapping.DARS (Decoys As the Reference State) potentials for protein-protein docking.Protein-protein docking by fast generalized Fourier transforms on 5D rotational manifolds.SDU: A Semidefinite Programming-Based Underestimation Method for Stochastic Global Optimization in Protein Docking.Convergence and combination of methods in protein-protein docking.Binding hot spots and amantadine orientation in the influenza a virus M2 proton channelA New Approach to Rigid Body Minimization with Application to Molecular Docking.The ClusPro web server for protein-protein docking.New additions to the ClusPro server motivated by CAPRI.Flexible Refinement of Protein-Ligand Docking on Manifolds.Accounting for pairwise distance restraints in FFT-based protein-protein docking.Protein-protein docking with reduced potentials by exploiting multi-dimensional energy funnels.A Subspace Semi-Definite programming-based Underestimation (SSDU) method for stochastic global optimization in protein docking.
P50
Q27010280-323DDA8B-3567-41E7-B515-99280D8C07D3Q28208450-778B452F-5BA4-4915-8AE3-32A6EE211EE4Q28263012-5A2FAD7F-E9CA-4C32-B0E5-731D50658FCBQ28473662-83D89817-9AB0-40CC-9019-3A60B64CFDC1Q28543479-FA255588-FA72-47D3-9110-50FA4015EB8FQ30367220-F1FBE98E-68FC-40BE-AB2D-6BD308A49C15Q30388027-83977F91-6998-4DE2-A6FB-8775F328708DQ30409794-DEC2A1FF-DE40-4FA1-A6DF-4EA98FCF9568Q30426883-6E4D93AB-1DFD-4197-8BFD-E386639F22CEQ31119468-6AAF0C00-DF83-4954-A3C3-14FF4EE19582Q33403707-0C229006-A401-4CC3-9D43-F5A223FADF46Q33662936-5836379D-6F3F-4AB5-A686-462F79B70525Q34057747-82B1E8F2-64F3-4540-9126-6EA7343BC20AQ34076535-0E9BD3CD-D557-439A-959F-27FDB6C4B52CQ34091502-337392C5-2470-4187-85F1-92BA1271DAFEQ34169869-FB809E6B-2825-4122-A3C4-CB995A00F888Q34174903-C36713D5-046E-4D3D-9601-EE91A6287C55Q34350884-C74AC5A5-3888-44BB-8098-BC33259F561AQ34525863-A56CC8BB-D8C5-4D66-871E-69EB2B48D956Q34615879-4254FC09-50FD-4F93-AF93-E83132E3AEB1Q35090040-9B25CE10-9837-41A4-BB46-C417C17E5298Q35730955-D3320FAA-5E27-462E-87D8-667973FF6C4AQ36269125-24CC9A14-098E-4EFE-8C8A-532AB8558E0BQ36277738-22556C8B-73DB-4B29-908D-F7F58FC5A904Q36280587-12CBC61C-B4FC-450A-8EA7-1D637DC7C10AQ36478348-EF37C01E-AEEE-4714-910F-D9F7CAD42D44Q36604792-CED4DCB6-1505-4CB4-ACFE-1B8C6A67B3B3Q36746240-B35833BE-ABC8-456E-BBC9-6297D5B08874Q36938608-B2E728D0-F62F-43E0-A778-FCB644BE426BQ37142683-C4AFA677-F00F-45A5-8EED-3C1CDF58BA46Q37347238-2FB4EFCE-9F10-4A83-A6BB-6667BFCB1F88Q37392115-722F8163-AAB1-428A-A2EC-7AD2CEEE5207Q37418850-338F0C74-C42C-4ECD-B68B-E8AD37617ADFQ38845434-F3047C22-7DBD-471B-9C2E-043FCF878132Q39024817-013F260E-D90A-4D6B-A097-9A955B2FF814Q39114594-653CE480-69C9-46C1-BB89-86C8CFD76495Q39559973-5E91394C-BA46-4031-977F-3BA9EB9AB7FFQ39644733-6601A601-4034-430F-BCB7-9489CBF2CB92Q39749623-539C41CD-7F6B-4F6A-B823-A31BE9618C9DQ39851287-73E1216C-D642-47E1-9EC4-1007A85E9550
P50
description
researcher
@en
wetenschapper
@nl
հետազոտող
@hy
name
Sandor Vajda
@ast
Sandor Vajda
@en
Sandor Vajda
@es
Sandor Vajda
@nl
Sandor Vajda
@sl
type
label
Sandor Vajda
@ast
Sandor Vajda
@en
Sandor Vajda
@es
Sandor Vajda
@nl
Sandor Vajda
@sl
prefLabel
Sandor Vajda
@ast
Sandor Vajda
@en
Sandor Vajda
@es
Sandor Vajda
@nl
Sandor Vajda
@sl
P106
P31
P496
0000-0003-1540-8220