about
An antibody that prevents the hemagglutinin low pH fusogenic transitionDesign and Characterization of Modular Scaffolds for Tubulin AssemblyThe determinants that govern microtubule assembly from the atomic structure of GTP-tubulinThe structure of apo-kinesin bound to tubulin links the nucleotide cycle to movementStructures of a diverse set of colchicine binding site inhibitors in complex with tubulin provide a rationale for drug discoveryX-ray structures of a hydrolytic antibody and of complexes elucidate catalytic pathway from substrate binding and transition state stabilization through water attack and product releaseKinesin, 30 years later: Recent insights from structural studiesN-terminal stathmin-like peptides bind tubulin and impede microtubule assemblyMechanism of microtubule stabilization by taccalonolide AJ.Insight into microtubule disassembly by kinesin-13s from the structure of Kif2C bound to tubulin.New Insights into the Coupling between Microtubule Depolymerization and ATP Hydrolysis by Kinesin-13 Protein Kif2C.Mechanism of inactivation of a catalytic antibody by p-nitrophenyl esters.Microtubule-destabilizing agents: structural and mechanistic insights from the interaction of colchicine and vinblastine with tubulin.The structural switch of nucleotide-free kinesin.Similarities of hydrolytic antibodies revealed by their X-ray structures: a review.Kif2C minimal functional domain has unusual nucleotide binding properties that are adapted to microtubule depolymerization.Studying drug-tubulin interactions by X-ray crystallography.A neutralizing antibody Fab-influenza haemagglutinin complex with an unprecedented 2:1 stoichiometry: characterization and crystallization.Structure of influenza virus haemagglutinin complexed with a neutralizing antibody.Insight into tubulin regulation from a complex with colchicine and a stathmin-like domain.Elucidating Tau function and dysfunction in the era of cryo-EM.Crystallization and preliminary X-ray diffraction studies of complexes between an influenza hemagglutinin and Fab fragments of two different monoclonal antibodiesInsight into the GTPase activity of tubulin from complexes with stathmin-like domains[The regulation of tubulin by vinblastine]Insight into microtubule nucleation from tubulin-capping proteins
P50
Q27638286-3E130D84-826F-40C8-9C49-4E9A3A642B9BQ27670721-56987A4B-12BD-4F5B-BBBD-CCDCBC9D6876Q27670993-FCC9F959-3A6C-425F-821B-47E159B23577Q27696177-F1312BF0-3C89-4B70-B10C-0D779ED1CE23Q27702294-84A9EA19-7D8F-476E-84B1-502D0BA05942Q27740546-5096439B-0560-427C-B8F0-776F9B160FA4Q28081794-9F554160-461D-48AC-990E-6868292B2E6CQ28279828-C7FF4180-B864-4ED2-82BC-DA67FADCFA9DQ33786408-F19F00C9-4FB5-486B-8931-84B3DB789ED6Q33890109-BFBB79A7-C2AA-4C8C-B8B2-7B2C1C35F83DQ35883888-940C0DB5-B0AA-4AA5-8048-796D7D42003CQ36868903-ECAC0769-F7E0-4A1C-A54E-B70788EA2D2AQ38096825-1E6CA6B0-E6C7-419A-9B32-A97B40881E42Q38962633-5F596658-B1D1-4A0E-815D-569248341E1AQ41710648-0C153374-0FD1-4761-B67F-4D5AB01ED689Q42141431-08A36FEF-32E5-48AF-8FF7-2A2E6DA8B6FCQ42639927-AD02A468-25E5-48DD-BB7C-BCD9FA20CD04Q44223873-E3756874-A874-453D-9429-E512DEA9D1DDQ45788230-9D522990-1EA9-4069-8C57-CAD80F6DCF4DQ47967639-32429EE5-3659-4FFC-810E-708946176E60Q64914771-B7A57FD2-C5C0-4C0D-86C4-5C6A86E5491FQ70830914-CAF71C23-C08F-42CE-814E-A889CE1BCABDQ80823671-B715DCBF-4DE2-46E6-B320-18E8F233E2C9Q81295142-82BA2D20-0BFA-480B-88F8-D49D295BA253Q91622746-493BF480-8D01-4B26-8E8B-25DA6A3B470A
P50
description
researcher
@en
name
Benoît Gigant
@en
Gigant B
@nl
type
label
Benoît Gigant
@en
Gigant B
@nl
altLabel
Gigant B
@en
prefLabel
Benoît Gigant
@en
Gigant B
@nl
P106
P31
P496
0000-0002-5946-6759