about
Structure and function of the intracellular region of the plexin-b1 transmembrane receptorThe cytoplasmic domain of neuropilin-1 regulates focal adhesion turnoverLigand recognition by A-class Eph receptors: crystal structures of the EphA2 ligand-binding domain and the EphA2/ephrin-A1 complexModeling transmembrane domain dimers/trimers of plexin receptors: implications for mechanisms of signal transmission across the membraneA refined solution structure of hen lysozyme determined using residual dipolar coupling dataBinding of Rac1, Rnd1, and RhoD to a Novel Rho GTPase Interaction Motif Destabilizes Dimerization of the Plexin-B1 Effector DomainInsights into Oncogenic Mutations of Plexin-B1 Based on the Solution Structure of the Rho GTPase Binding DomainEPHA2 is associated with age-related cortical cataract in mice and humansWhen monomers are preferred: a strategy for the identification and disruption of weakly oligomerized proteinsAcceptable protein and solvent behavior in primary hydration shell simulations of hen lysozymeTrifluoroethanol and colleagues: cosolvents come of age. Recent studies with peptides and proteins.Binding and function of phosphotyrosines of the Ephrin A2 (EphA2) receptor using synthetic sterile α motif (SAM) domains.A direct coupling between global and internal motions in a single domain protein? MD investigation of extreme scenarios.Structural basis of Rnd1 binding to plexin Rho GTPase binding domains (RBDs)NMR structure of a heterodimeric SAM:SAM complex: characterization and manipulation of EphA2 binding reveal new cellular functions of SHIP2.Prediction, refinement, and persistency of transmembrane helix dimers in lipid bilayers using implicit and explicit solvent/lipid representations: microsecond molecular dynamics simulations of ErbB1/B2 and EphA1.K-Ras at Anionic Membranes: Orientation, Orientation…Orientation. Recent Simulations and Experiments.Compensatory and long-range changes in picosecond-nanosecond main-chain dynamics upon complex formation: 15N relaxation analysis of the free and bound states of the ubiquitin-like domain of human plexin-B1 and the small GTPase Rac1.Molecular simulations of a dynamic protein complex: role of salt-bridges and polar interactions in configurational transitions.Refinement of the primary hydration shell model for molecular dynamics simulations of large proteins.1H, 15N and 13C Resonance assignments and secondary structure determination reveal that the minimal Rac1 GTPase binding domain of plexin-B1 has a ubiquitin fold.Plexin structures are coming: opportunities for multilevel investigations of semaphorin guidance receptors, their cell signaling mechanisms, and functions.Dissociation of a Dynamic Protein Complex Studied by All-Atom Molecular Simulations.Backbone assignment and secondary structure of Rnd1, an unusual Rho family small GTPase.G protein beta2 subunit-derived peptides for inhibition and induction of G protein pathways. Examination of voltage-gated Ca2+ and G protein inwardly rectifying K+ channels.Molecular profiling of the "plexinome" in melanoma and pancreatic cancer.1H, 15N, 13C assignments for the activated form of the small Rho-GTPase Rac1.Combining NMR and molecular dynamics studies for insights into the allostery of small GTPase-protein interactions.Structure and dynamics analysis on plexin-B1 Rho GTPase binding domain as a monomer and dimer.Thermodynamic characterization of two homologous protein complexes: associations of the semaphorin receptor plexin-B1 RhoGTPase binding domain with Rnd1 and active Rac1.Tripping a switch: PDZRhoGEF rgRGS-bound Galpha13.Integrated computational approach to the analysis of NMR relaxation in proteins: application to ps-ns main chain 15N-1H and global dynamics of the Rho GTPase binding domain of plexin-B1.Analysis of 15N-1H NMR relaxation in proteins by a combined experimental and molecular dynamics simulation approach: picosecond-nanosecond dynamics of the Rho GTPase binding domain of plexin-B1 in the dimeric state indicates allosteric pathways.Importance of the CMAP correction to the CHARMM22 protein force field: dynamics of hen lysozyme.Hydrogen exchange in native and denatured states of hen egg-white lysozyme.Structural and dynamical properties of a denatured protein. Heteronuclear 3D NMR experiments and theoretical simulations of lysozyme in 8 M urea.Global disruption of the WASP autoinhibited structure on Cdc42 binding. Ligand displacement as a novel method for monitoring amide hydrogen exchange.Equilibrium unfolding studies of horse muscle acylphosphatase.Acceleration of the folding of hen lysozyme by trifluoroethanolConformational Properties of Four Peptides Spanning the Sequence of Hen Lysozyme
P50
Q24309186-4086412E-2CBF-46D5-A5BA-5DC9F2B182A6Q24324024-E1BAB8D3-3DDC-41F4-8028-4301C8D4AFDAQ24338237-388E802B-02E4-4EF9-BD06-58F654F42125Q27310828-B70774FD-13CE-42D2-BEB6-8232F35B9219Q27630831-F50ABDF4-0481-4109-BB0E-9177CBA2F661Q27648718-EDAC447E-1B48-4D80-9628-2AEE3188155BQ27649860-ABC1E413-1E2B-408A-9230-F35B20A3AE3FQ28475827-BC43001A-7753-41D0-93D1-C9B6391BF66AQ30349959-8D3F0162-F906-4DFC-9B63-5AF94D66083FQ33270625-09C08EBB-D004-42D9-A2B5-E2974DF08DAAQ33671691-D227F609-6210-41C2-AC60-24CEBD4D8DA2Q33888617-7FD81238-376E-4F1E-845F-C216BC065151Q35079361-4795CB2F-D1B7-45C6-9C26-AE0CC6D685F2Q35110931-09083E87-1698-443C-9E45-2FAD88A00F30Q36451527-3E1C2646-9CF3-49E5-B144-474C46992068Q36569264-875AE995-7547-4767-B5F4-87359A5A838DQ36678708-CC7BF3D4-3AD8-42B3-B7E0-07D87368030BQ37154008-359907AF-1401-4B7D-9C08-BF2F3DA45EA8Q37337992-2A636DB0-FF3D-4CA8-A2EC-33BBBD66BB99Q37384449-84DECD3A-0AF1-4FBA-91A5-1A916A00D24CQ37434673-62EB3E53-0769-4ED1-9FFE-20B482E16ED6Q38022543-53058BB6-15EF-405F-8451-E9DB6B2238ECQ38742285-0C64FDE9-FA57-4E0D-99F7-3DCE05E5A6D7Q39614422-2A8BED03-A7C1-4352-B2F4-225216947691Q40436463-410AEECC-8E06-4F26-916A-CD540EF5C761Q41692560-5E73BBA8-1DB5-461D-9CBA-08112D37B515Q41884961-7D0BBEA2-C30E-4CF6-9E7F-26C273C87C5FQ42159319-BEA48E53-0DBC-4F8F-B06F-83E90BDDECE7Q42277883-0C0701DD-33EF-47A0-AF2D-6462D4C8181EQ42606532-B906D44F-ADB5-4780-B0B4-3A0709B72AD7Q42665712-AA799E44-F49B-4785-8BC2-5DA5F50B87D2Q42719047-9FF447E9-FC12-45A6-B6E4-F3F620D1ED66Q43041951-B5F47874-FB0C-4A45-8DC0-6B51A01D158BQ43203629-102A4A8E-091B-4B0F-8537-E3314F845464Q44184711-86783586-7FF4-4D68-A798-8E792923F6ABQ46667139-647837A3-179A-45CB-843D-4464FF32146BQ52544597-ABF537ED-350A-45D9-BA72-A9893AA2DFDDQ53129332-E55A2FD9-247D-4700-9FC4-2D274C7AFE48Q54806606-95F79922-AD56-411C-8896-D299EAF0F80FQ54806609-CA140628-44A2-40D8-95C9-09CCC6DCDC97
P50
description
hulumtues
@sq
researcher
@en
wetenschapper
@nl
հետազոտող
@hy
name
Matthias Buck
@ast
Matthias Buck
@en
Matthias Buck
@es
Matthias Buck
@nl
Matthias Buck
@sl
type
label
Matthias Buck
@ast
Matthias Buck
@en
Matthias Buck
@es
Matthias Buck
@nl
Matthias Buck
@sl
prefLabel
Matthias Buck
@ast
Matthias Buck
@en
Matthias Buck
@es
Matthias Buck
@nl
Matthias Buck
@sl
P1053
B-2106-2017
P106
P21
P31
P3829
P496
0000-0002-2958-0403