about
The RNA-binding region of human TRBP interacts with microRNA precursors through two independent domainsBiochemical and structural characterization of an intramolecular interaction in FOXO3a and its binding with p53Crystal structure of type I ryanodine receptor amino-terminal -trefoil domain reveals a disease-associated mutation"hot spot"loopCharacterization of a conserved "threonine clasp" in CAP-Gly domains: role of a functionally critical OH/pi interaction in protein recognition.Observation of CH⋅⋅⋅π Interactions between Methyl and Carbonyl Groups in Proteins.The acute myeloid leukemia fusion protein AML1-ETO targets E proteins via a paired amphipathic helix-like TBP-associated factor homology domainParallel screening and optimization of protein constructs for structural studiesDissecting the roles of TRBP and PACT in double-stranded RNA recognition and processing of noncoding RNAs.S6K2-mediated regulation of TRBP as a determinant of miRNA expression in human primary lymphatic endothelial cells.Argonaute Utilization for miRNA Silencing Is Determined by Phosphorylation-Dependent Recruitment of LIM-Domain-Containing Proteins.Stereospecific isotopic labeling of methyl groups for NMR spectroscopic studies of high-molecular-weight proteins.Structural basis of CBP/p300 recruitment in leukemia induction by E2A-PBX1.Characterization of the intrinsic and TSC2-GAP-regulated GTPase activity of Rheb by real-time NMR.Conserved asymmetry underpins homodimerization of Dicer-associated double-stranded RNA-binding proteins.Backbone 1H, 13C, and 15N resonance assignments for a 29 kD monomeric variant of Pseudomonas aeruginosa dimethylarginine dimethylaminohydrolase.iHADAMAC: a complementary tool for sequential resonance assignment of globular and highly disordered proteins.Backbone resonance assignments of the micro-RNA precursor binding region of human TRBP.Characterization and Manipulation of the Pseudomonas aeruginosa Dimethylarginine Dimethylaminohydrolase Monomer–Dimer EquilibriumThe LxxLL motif: a multifunctional binding sequence in transcriptional regulationSite-selective C-C modification of proteins at neutral pH using organocatalyst-mediated cross aldol ligationsBinding of a peptide from a Streptococcus dysgalactiae MSCRAMM to the N-terminal F1 module pair of human fibronectin involves both modulesA simple biosynthetic method for stereospecific resonance assignment of prochiral methyl groups in proteinsSelective isotopic unlabeling of proteins using metabolic precursors: application to NMR assignment of intrinsically disordered proteinsA systematic mutagenesis-driven strategy for site-resolved NMR studies of supramolecular assembliesDirect detection of CH/pi interactions in proteinsScrambling free combinatorial labeling of alanine-β, isoleucine-δ1, leucine-proS and valine-proS methyl groups for the detection of long range NOEsA HIF-LIMD1 negative feedback mechanism mitigates the pro-tumorigenic effects of hypoxia
P50
Q24320118-92356489-A3D2-44D6-A5CC-217B527A241BQ27652325-E1BF33C9-2A12-4358-A3F8-CF9E18874CC5Q27656078-1690400F-F4A3-46F1-9799-FD0907137C99Q30372818-3B352E6C-D065-40DE-911A-E13499954E88Q30402426-6CE29C36-F10D-4A92-9F24-40714C10BB09Q34771988-4EA9916A-2C87-41BC-8D06-7EA616365BE1Q37255422-63D27531-2AB0-4D82-8319-29808050020DQ38335714-1CA02B3B-C2D2-4538-BCE6-1566A678F439Q38758450-F0BF279A-FFE2-4AA9-A285-3A821D938755Q40145349-AF424723-6D15-441C-BF65-D21EE6F21373Q43161110-DF51DC9E-56DD-43FF-8093-B5CB8E576815Q43448957-F7403B8E-3A30-4D43-848A-4881C2D19A86Q46142408-9E4DBA47-CA4C-4641-96F2-31462531A09CQ47106289-0D95E3F1-448D-4EC0-88B3-80FB573753D0Q47300965-DE0C113A-38FB-4758-81D7-0ABC91D633A2Q51487830-259B8064-3BB8-4591-ADC1-361D3053FCE8Q54492101-6EF20A3E-6DB5-4E65-9D2A-FE6B4B0B0E42Q58449601-95538CA5-5229-4ED7-96F4-A0C8BB424284Q58484404-809DB5DF-FEA4-4F6D-AA59-50B9C5EF2465Q61847158-FCE1D100-96E8-49D4-856E-2F00EBBDCDF1Q73935973-7FE589C1-3F77-4C5C-89E5-9D3634FAF9CAQ83347076-C51047E9-FBEB-40D1-8591-3992D2A95884Q83622809-2AB1CEC8-3F56-4121-BC78-4EA9CA6099C3Q84230311-B709E9A6-2C12-4277-85A2-C99944AEFC78Q84272323-79505E85-38FD-42E1-B8CF-931BFB8E0B2FQ86069491-AE5E9BC6-F59A-414F-ACE1-1827A5A28B0DQ89181309-573D8493-66EC-4441-B8FE-C65F4CA3F09F
P50
description
onderzoeker
@nl
researcher ORCID ID = 0000-0003-2057-8291
@en
name
Michael J Plevin
@ast
Michael J Plevin
@en
Michael J Plevin
@es
Michael J Plevin
@nl
type
label
Michael J Plevin
@ast
Michael J Plevin
@en
Michael J Plevin
@es
Michael J Plevin
@nl
prefLabel
Michael J Plevin
@ast
Michael J Plevin
@en
Michael J Plevin
@es
Michael J Plevin
@nl
P108
P106
P31
P496
0000-0003-2057-8291