about
A unique set of SH3-SH3 interactions controls IB1 homodimerization.A helical structural nucleus is the primary elongating unit of insulin amyloid fibrilsThe structures of the horseradish peroxidase C-ferulic acid complex and the ternary complex with cyanide suggest how peroxidases oxidize small phenolic substratesArabidopsis thaliana peroxidase N: structure of a novel neutral peroxidaseDominant epitopes and allergic cross-reactivity: complex formation between a Fab fragment of a monoclonal murine IgG antibody and the major allergen from birch pollen Bet v 1Structure of soybean seed coat peroxidase: A plant peroxidase with unusual stability and haem-apoprotein interactionsAmylosucrase, a glucan-synthesizing enzyme from the alpha-amylase familyCrystal structures of amylosucrase from Neisseria polysaccharea in complex with D-glucose and the active site mutant Glu328Gln in complex with the natural substrate sucroseDifferential activity and structure of highly similar peroxidases. Spectroscopic, crystallographic, and enzymatic analyses of lignifying Arabidopsis thaliana peroxidase A2 and horseradish peroxidase A2Major venom allergen of yellow jackets, Ves v 5: structural characterization of a pathogenesis-related protein superfamilyStructural analysis of the two horseradish peroxidase catalytic residue variants H42E and R38S/H42E: implications for the catalytic cycleOligosaccharide and sucrose complexes of amylosucrase. Structural implications for the polymerase activityDominating IgE-binding epitope of Bet v 1, the major allergen of birch pollen, characterized by X-ray crystallography and site-directed mutagenesisChaperone binding at the ribosomal exit tunnelCrystal structure of sucrose phosphorylase from Bifidobacterium adolescentisHigh resolution crystal structures of the p120 RasGAP SH3 domainStructure of rat acidic fibroblast growth factor at 1.4 Å resolutionA tetrazolyl-substituted subtype-selective AMPA receptor agonistPartial agonism and antagonism of the ionotropic glutamate receptor iGLuR5: structures of the ligand-binding core in complex with domoic acid and 2-amino-3-[5-tert-butyl-3-(phosphonomethoxy)-4-isoxazolyl]propionic acidStructure of the first PDZ domain of human PSD-93Ionotropic glutamate-like receptor 2 binds D-serine and glycineStructural proof of a dimeric positive modulator bridging two identical AMPA receptor-binding sitesStructure of the PPX/GPPA phosphatase from Aquifex aeolicus in complex with the alarmone ppGppStructures of the ligand-binding core of iGluR2 in complex with the agonists (R)- and (S)-2-amino-3-(4-hydroxy-1,2,5-thiadiazol-3-yl)propionic acid explain their unusual equipotencyDimerization effect of sucrose octasulfate on rat FGF1Structure of a SARS coronavirus-derived peptide bound to the human major histocompatibility complex class I molecule HLA-B*1501The structure of the complex between a branched pentasaccharide and Thermobacillus xylanilyticus GH-51 arabinofuranosidase reveals xylan-binding determinants and induced fitCrystal structure of the Ig1 domain of the neural cell adhesion molecule NCAM2 displays domain swappingMolecular mechanism of agonist recognition by the ligand-binding core of the ionotropic glutamate receptor 4Full Domain Closure of the Ligand-binding Core of the Ionotropic Glutamate Receptor iGluR5 Induced by the High Affinity Agonist Dysiherbaine and the Functional Antagonist 8,9-DideoxyneodysiherbaineThe glutamate receptor GluR5 agonist (S)-2-amino-3-(3-hydroxy-7,8-dihydro-6H-cyclohepta[d]isoxazol-4-yl)propionic acid and the 8-methyl analogue: synthesis, molecular pharmacology, and biostructural characterizationDistinct structural features of cyclothiazide are responsible for effects on peak current amplitude and desensitization kinetics at iGluR2Neuroplastin-55 binds to and signals through the fibroblast growth factor receptorThe apo structure of sucrose hydrolase from Xanthomonas campestris pv. campestris shows an open active-site grooveStructural model and trans-interaction of the entire ectodomain of the olfactory cell adhesion moleculeCrystal Structure of Lymnaea stagnalis AChBP Complexed with the Potent nAChR Antagonist DHβE Suggests a Unique Mode of AntagonismThermodynamics and structural analysis of positive allosteric modulation of the ionotropic glutamate receptor GluA2Binding site and interlobe interactions of the ionotropic glutamate receptor GluK3 ligand binding domain revealed by high resolution crystal structure in complex with (S)-glutamateIntersubunit Bridge Formation Governs Agonist Efficacy at Nicotinic Acetylcholine 4 2 Receptors: UNIQUE ROLE OF HALOGEN BONDING REVEALEDA high-affinity, dimeric inhibitor of PSD-95 bivalently interacts with PDZ1-2 and protects against ischemic brain damage
P50
Q24541394-CD5E9712-C2AC-4EE7-AF6C-9C6924EFD8E2Q27334707-212AFA9F-53AF-4854-9D9A-605E4C4BFE2AQ27620499-FB1EACE6-5992-43C7-9DE9-31D4EF98B6ECQ27621736-5CEB54F9-6612-4405-A3F6-9A594AFDD014Q27625005-3780A697-8A45-4BD1-B992-4B876AE7EFC5Q27630799-A31193C7-F363-40A6-B06A-DDA78B39A79EQ27631232-924CBC0E-2180-4284-B6C9-BF0C123A22D0Q27633428-EB74953A-54FD-479C-B4DF-F372A9F2F005Q27634774-E96FCA4A-A82C-46F1-BE3B-BCD5F159B919Q27636869-34E5C9F5-803A-410E-82FD-A2CB3D3DCEDCQ27639708-54F0EA49-9048-4B79-AF3C-DC2028913EF4Q27639735-1FF7B51A-F953-4CD8-B803-1892662996C4Q27641972-B5093797-3DDF-49E6-B1F5-B6787164A0A3Q27642699-4E87C332-4775-4415-8635-970CE785AE79Q27643064-E94D4C7B-F073-4891-A6ED-039206A97583Q27643405-C2C9D3F8-3DD8-4247-864B-A98D5561CAA5Q27643740-D25D2DCD-D9F9-41B0-AEB8-D4A4CDF40DC1Q27644586-7B9034B3-07CE-432C-B461-5A0C34496325Q27646152-52636354-8E48-4F35-A5F0-4EE645EA89ABQ27646716-29282C58-347E-40B8-B2C5-94AC01E0CB54Q27647469-26CAD9B7-9537-4032-AC33-6805BBFFEC17Q27649098-ED446D9B-42BB-479A-9B4A-39498FEF160DQ27649393-D57F6943-341F-4634-A3B5-213A0A136EA9Q27649834-3E07DA93-E806-41A0-BDC4-78B195F0F117Q27650780-A2A7D641-40ED-4C06-8264-AE5A40AAD3CDQ27650782-03E42435-2AB9-4ED7-97D3-26E7BFA403EEQ27650888-283084F6-4BFE-4734-B757-E1FD1869B243Q27651640-36E105A9-1669-4CE8-AE21-113ED76BE3BCQ27652965-E6044207-9C13-48B0-811A-E857E17E4A5FQ27654204-3D8728C2-CA7D-453B-A29D-7FD2E140BCF3Q27656350-454DB509-1F6A-4A67-A98E-B025FCBD867FQ27656358-74926F8F-973B-4426-B0DF-13D85F28D109Q27658401-905855D1-183A-4CC3-B4B8-FD10DD5508A8Q27658475-1D544A67-38BF-422F-BD24-886FDD76DAF9Q27666681-9342B87E-4060-4C2F-A231-AF9C5D967980Q27671732-6F3261C2-48D3-4974-B558-EAA6BC352164Q27673244-E8574010-0C37-4558-A14E-8F3F92977906Q27673692-F5D33FBB-8140-4F7E-BB61-17956B6303C0Q27676179-37E725A9-390A-4148-96F4-FE8541D4C196Q27677328-FFAD17E3-2DEB-4959-B6E0-3427C4CC729C
P50
description
hulumtues
@sq
onderzoeker
@nl
researcher
@en
հետազոտող
@hy
name
Michael Gajhede
@ast
Michael Gajhede
@en
Michael Gajhede
@es
Michael Gajhede
@fr
Michael Gajhede
@sl
type
label
Michael Gajhede
@ast
Michael Gajhede
@en
Michael Gajhede
@es
Michael Gajhede
@fr
Michael Gajhede
@sl
prefLabel
Michael Gajhede
@ast
Michael Gajhede
@en
Michael Gajhede
@es
Michael Gajhede
@fr
Michael Gajhede
@sl
P106
P21
P31
P496
0000-0001-9864-2287
P569
2000-01-01T00:00:00Z