about
Proteins and Their Interacting Partners: An Introduction to Protein-Ligand Binding Site Prediction MethodsFunFOLDQA: a quality assessment tool for protein-ligand binding site residue predictionsAssessing the quality of modelled 3D protein structures using the ModFOLD server.The enzymatic nature of an anonymous protein sequence cannot reliably be inferred from superfamily level structural information aloneIntFOLD: an integrated server for modelling protein structures and functions from amino acid sequences.TAPO: A combined method for the identification of tandem repeats in protein structures.Toolbox for Protein Structure Prediction.Rapid model quality assessment for protein structure predictions using the comparison of multiple models without structural alignments.In silico Identification and Characterization of Protein-Ligand Binding Sites.The IntFOLD server: an integrated web resource for protein fold recognition, 3D model quality assessment, intrinsic disorder prediction, domain prediction and ligand binding site prediction.The FunFOLD2 server for the prediction of protein-ligand interactions.FunFOLD: an improved automated method for the prediction of ligand binding residues using 3D models of proteins.DisProt 7.0: a major update of the database of disordered proteins.An assessment of the amount of untapped fold level novelty in under-sampled areas of the tree of lifeNeurotoxicity of a Biopesticide Analog on Zebrafish Larvae at Nanomolar Concentrations.The ModFOLD4 server for the quality assessment of 3D protein modelsAutomated tertiary structure prediction with accurate local model quality assessment using the IntFOLD-TS method.The binding site distance test score: a robust method for the assessment of predicted protein binding sites.The stability of Fbw7α in M-phase requires its phosphorylation by PKC.Usage of a dataset of NMR resolved protein structures to test aggregation versus solubility prediction algorithms.Improvement of 3D protein models using multiple templates guided by single-template model quality assessment.Accurate template-based modeling in CASP12 using the IntFOLD4-TS, ModFOLD6, and ReFOLD methods.DisProt 7.0: a major update of the database of disordered proteins
P50
Q26773424-D45C9356-2B72-4EA8-9963-B98C0C92FF30Q28729081-DC4ED472-E98A-48C7-B9AC-B5809332C1F7Q30359521-0953C8F9-1682-4173-9EF9-2CD75A2A9D15Q30370436-C8D21A29-3D3C-4FD3-BC12-3D4BBD89FC61Q30373190-6C516E6C-3F5F-4581-AC06-8319FB4B11E3Q30378558-4A778AEC-1704-44CD-AB38-EE5307013298Q30380863-CE487496-43EA-4C9E-95F8-62AACF5211D9Q30382356-EEEEBC79-2B50-4AB6-AB7E-5E42310C9137Q30387083-DAB3952F-D2A9-44C6-9598-FAABFF7CA2B1Q30401404-3B136E10-A8F2-4E4B-8A12-2E53560F726EQ30431835-8F1F8E03-B6BE-4289-8EE7-599CA54478CCQ33901432-8FC47D8A-14D8-40FD-B12C-DA101CFF6CBDQ34546157-0CE08021-B0C5-4D60-9FEE-90956503E7DEQ35798553-FDD10A32-D8C0-42D4-ACCE-234B28B0B4F8Q36229913-168C3095-EADD-4F86-9DCC-870039B45042Q36954050-8A79E941-6F77-4F77-AB40-769565D73465Q39682349-7B6E3ED5-274C-483C-AE35-4FE71BF7E9D2Q39835004-A57B99A0-4C57-4034-852E-68AABCCDEA62Q41545354-39D353EE-1F8A-4B9B-9AC3-CE0E4902D9F4Q47774509-77C5FCDA-B992-4278-803D-B1356FE4C145Q47989298-1C27E5F2-1496-4FCF-9F47-549A81FD1F3DQ48022610-4F075F2F-98A3-4A42-91E0-D915AF5979C0Q57204000-F9F86D18-E93C-4A73-B773-61663AE0847E
P50
description
researcher
@en
wetenschapper
@nl
հետազոտող
@hy
name
Daniel Barry Roche
@ast
Daniel Barry Roche
@en
Daniel Barry Roche
@es
Daniel Barry Roche
@nl
type
label
Daniel Barry Roche
@ast
Daniel Barry Roche
@en
Daniel Barry Roche
@es
Daniel Barry Roche
@nl
prefLabel
Daniel Barry Roche
@ast
Daniel Barry Roche
@en
Daniel Barry Roche
@es
Daniel Barry Roche
@nl
P106
P1153
35765749600
P21
P31
P496
0000-0002-9204-1840