about
Molecular basis of tubulin transport within the cilium by IFT74 and IFT81.Crystal structure of the intraflagellar transport complex 25/27Atomic resolution structure of human -tubulin acetyltransferase bound to acetyl-CoACrystal structure of the invertebrate bifunctional purine biosynthesis enzyme PAICS at 2.8 Å resolutionReversal of RNA polymerase II ubiquitylation by the ubiquitin protease Ubp3.Architecture and function of IFT complex proteins in ciliogenesisIFT81, encoding an IFT-B core protein, as a very rare cause of a ciliopathy phenotype.Proteasome-mediated processing of Def1, a critical step in the cellular response to transcription stressDistinct ubiquitin ligases act sequentially for RNA polymerase II polyubiquitylationStructural studies of ciliary components.Complex Reconstitution from Individual Protein Modules.The Intraflagellar Transport Machinery.Intraflagellar transport protein IFT52 recruits IFT46 to the basal body and flagella.Intraflagellar transport proteins 172, 80, 57, 54, 38, and 20 form a stable tubulin-binding IFT-B2 complex.Recombinant Reconstitution and Purification of the IFT-B Core Complex from Chlamydomonas reinhardtii.Biochemical mapping of interactions within the intraflagellar transport (IFT) B core complex: IFT52 binds directly to four other IFT-B subunits.A role for checkpoint kinase-dependent Rad26 phosphorylation in transcription-coupled DNA repair in Saccharomyces cerevisiae.Crystal structures of IFT70/52 and IFT52/46 provide insight into intraflagellar transport B core complex assembly.Ca2+/Calmodulin-dependent kinase II signaling causes skeletal overgrowth and premature chondrocyte maturation.Mutations of IFT81, encoding an IFT-B core protein, as a rare cause of a ciliopathy.
P50
Q24320475-B5935D87-7FF6-4445-B545-86854C54A569Q27667586-C6417F8B-61BC-4ECE-9281-45079ABAC142Q27674573-46DAB78A-7103-4EB5-A0B0-EF7B5316044DQ27684358-778C6CAF-57AC-4A73-BAC8-42DC14423E23Q27932765-6C88B7E4-0AA0-4253-9694-0138FBB935EFQ28000079-BF9111A1-400C-4A8D-BFB1-3EC9FEEB4F16Q36209043-56DC15AD-EFFB-46F8-90C3-AC8FD7CECEA1Q37187541-57C7781A-963E-46F7-9B20-3081219F07F0Q37424165-0B228B44-C0FB-4325-A810-B966A5F21F0DQ38017496-94F8557D-C14B-482D-9404-3DA93DB4789AQ38831302-F953FAE2-2318-416F-A676-1B542A573FB7Q38879720-13BADE26-4181-40B3-8802-00CE1387D070Q38902461-E117A79F-3FF0-4E69-8ED8-E613E4720E9FQ39814785-55FEF981-90BA-498B-870B-5DBFCB42EA58Q41601126-C0814A01-E4F1-4093-BD31-9479CB8CD17DQ42276283-64D3990B-A94C-4B22-890C-B25F6AF8B4DDQ42876928-4C44B830-1893-4ED8-9F9B-CF89A6A2D89FQ42963053-7B5484AE-B70E-46F2-98D4-3F8A512FE301Q53491968-A6D7ECDE-7F6B-431D-9ACB-68BF63F5201BQ55088397-26C40843-3E44-4F96-85CB-088A85F27B5F
P50
description
onderzoeker
@nl
researcher ORCID ID = 0000-0002-3789-5077
@en
name
Michael Taschner
@ast
Michael Taschner
@en
Michael Taschner
@es
Michael Taschner
@nl
type
label
Michael Taschner
@ast
Michael Taschner
@en
Michael Taschner
@es
Michael Taschner
@nl
prefLabel
Michael Taschner
@ast
Michael Taschner
@en
Michael Taschner
@es
Michael Taschner
@nl
P106
P31
P496
0000-0002-3789-5077