about
Cryo-EM studies of the structure and dynamics of vacuolar-type ATPasesAn autoinhibited noncanonical mechanism of GTP hydrolysis by Rheb maintains mTORC1 homeostasisStructure-guided Mutation of the Conserved G3-box Glycine in Rheb Generates a Constitutively Activated Regulator of Mammalian Target of Rapamycin (mTOR)The auto-inhibitory role of the EPAC hinge helix as mapped by NMRDynamically driven ligand selectivity in cyclic nucleotide binding domains.Oncogenic and RASopathy-associated K-RAS mutations relieve membrane-dependent occlusion of the effector-binding site.The projection analysis of NMR chemical shifts reveals extended EPAC autoinhibition determinants.Probing the GTPase cycle with real-time NMR: GAP and GEF activities in cell extracts.Biochemical Classification of Disease-associated Mutants of RAS-like Protein Expressed in Many Tissues (RIT1).Molecular basis of human CD22 function and therapeutic targeting.Real-time NMR study of three small GTPases reveals that fluorescent 2'(3')-O-(N-methylanthraniloyl)-tagged nucleotides alter hydrolysis and exchange kinetics.Atomic model for the membrane-embedded VO motor of a eukaryotic V-ATPase.A comparative CEST NMR study of slow conformational dynamics of small GTPases complexed with GTP and GTP analogues.Understanding cAMP-dependent allostery by NMR spectroscopy: comparative analysis of the EPAC1 cAMP-binding domain in its apo and cAMP-bound states.Membrane-dependent modulation of the mTOR activator Rheb: NMR observations of a GTPase tethered to a lipid-bilayer nanodisc.Entropy-driven cAMP-dependent Allosteric Control of Inhibitory Interactions in Exchange Proteins Directly Activated by cAMPLabel-free assay for thermodynamic analysis of protein-ligand interactions: a multivariate strategy for allosteric ligand screeningSteric occlusion regulates proximal interactions of acyl carrier protein domain in fungal fatty acid synthase
P50
Q26741088-BC8FDD83-9A97-41C7-89B9-25E28DF97067Q27681786-21776EC4-E728-4DE5-AB42-C333C952B28CQ27682320-4F3CB340-C1BC-4992-B5CE-F1862BDC6E12Q28485307-3A8FD4E0-6159-4A7B-90C3-B7B19B770279Q34978413-EFECAB55-5859-405F-82E0-8F38424221B0Q35669207-F69B21DD-D611-4C85-9F51-C456C67A9E64Q35743330-F6C5B872-18DB-429B-81C4-75CE8BAF542DQ38458035-F0B54E0E-DC95-47F2-A879-BDE6F7A01DADQ38768357-A6EB3F42-D7BC-4835-8ED6-C452B13CF97CQ42286136-55CAAF01-452D-4CF2-A069-5F1029D8A530Q42918070-E5708848-274F-41FB-B9FD-6967FD088648Q45045809-2E80591E-ACAF-4549-8B54-2B6250F254B0Q45050798-81C1F442-D522-4369-A819-C072F59E88B7Q46921842-8DED2B8F-5710-4B56-8E09-07825EBD00DEQ48162743-D1433B2D-657A-4E61-B138-09724CE16FD8Q62273240-E96FD025-736B-432C-9FB0-74C9E358B6BBQ83120586-45B3C831-A42A-4F39-BBEC-ECFF332E7C08Q96022555-5DB96BB1-3C9B-4237-95E3-4F8B63587ECD
P50
description
onderzoeker
@nl
researcher, ORCID id # 0000-0003-0207-5877
@en
name
Mohammad T Mazhab-Jafari
@ast
Mohammad T Mazhab-Jafari
@en
Mohammad T Mazhab-Jafari
@es
Mohammad T Mazhab-Jafari
@nl
type
label
Mohammad T Mazhab-Jafari
@ast
Mohammad T Mazhab-Jafari
@en
Mohammad T Mazhab-Jafari
@es
Mohammad T Mazhab-Jafari
@nl
prefLabel
Mohammad T Mazhab-Jafari
@ast
Mohammad T Mazhab-Jafari
@en
Mohammad T Mazhab-Jafari
@es
Mohammad T Mazhab-Jafari
@nl
P106
P1153
23012450100
P31
P496
0000-0003-0207-5877