about
The diphthamide modification pathway from Saccharomyces cerevisiae--revisitedPhosphorylation of Elp1 by Hrr25 is required for elongator-dependent tRNA modification in yeast.A versatile partner of eukaryotic protein complexes that is involved in multiple biological processes: Kti11/Dph3.Mass spectrometric analysis of the anaphase-promoting complex from yeast: identification of a subunit related to cullins.Protein interactions within Saccharomyces cerevisiae Elongator, a complex essential for Kluyveromyces lactis zymocicity.A conserved and essential basic region mediates tRNA binding to the Elp1 subunit of the Saccharomyces cerevisiae Elongator complex.The Saccharomyces cerevisiae orthologue of the human protein phosphatase 4 core regulatory subunit R2 confers resistance to the anticancer drug cisplatin.YIL113w encodes a functional dual-specificity protein phosphatase which specifically interacts with and inactivates the Slt2/Mpk1p MAP kinase in S. cerevisiae.Efficient chromosome biorientation and the tension checkpoint in Saccharomyces cerevisiae both require Bir1.The yeast elongator histone acetylase requires Sit4-dependent dephosphorylation for toxin-target capacity.Novel interactions of Saccharomyces cerevisiae type 1 protein phosphatase identified by single-step affinity purification and mass spectrometry.Ipl1p-dependent phosphorylation of Mad3p is required for the spindle checkpoint response to lack of tension at kinetochores.Evidence that the Ipl1-Sli15 (Aurora kinase-INCENP) complex promotes chromosome bi-orientation by altering kinetochore-spindle pole connectionsMannosyl-diinositolphospho-ceramide, the major yeast plasma membrane sphingolipid, governs toxicity of Kluyveromyces lactis zymocin.Elongator's toxin-target (TOT) function is nuclear localization sequence dependent and suppressed by post-translational modification.Kluyveromyces lactis zymocin mode of action is linked to RNA polymerase II function via Elongator.The complement of protein kinases of the microsporidium Encephalitozoon cuniculi in relation to those of Saccharomyces cerevisiae and Schizosaccharomyces pombeTemperature-sensitive ipl1-2/Aurora B mutation is suppressed by mutations in TOR complex 1 via the Glc7/PP1 phosphatasePhosphorylation of Sli15 by Ipl1 is important for proper CPC localization and chromosome stability in Saccharomyces cerevisiae.Kinetochore capture and bi-orientation on the mitotic spindle.Characterisation of the S-adenosylmethionine decarboxylase (SAMDC) gene of potato.Discovery, in vivo activity, and mechanism of action of a small-molecule p53 activator.A Functional Link Between Bir1 and the Saccharomyces cerevisiae Ctf19 Kinetochore Complex Revealed Through Quantitative Fitness Analysis.Use of a Yeast tRNase Killer Toxin to Diagnose Kti12 Motifs Required for tRNA Modification by Elongator.Ipl1-dependent phosphorylation of Dam1 is reduced by tension applied on kinetochores.Decoding the biosynthesis and function of diphthamide, an enigmatic modification of translation elongation factor 2 (EF2)The essential roles of cytidine diphosphate-diacylglycerol synthase in bloodstream form Trypanosoma bruceiInsights into diphthamide, key diphtheria toxin effector.Collection and characterisation of bacterial membrane proteins.A novel 'two-component' protein containing histidine kinase and response regulator domains required for sporulation in Aspergillus nidulans.Urmylation and tRNA thiolation functions of ubiquitin-like Uba4·Urm1 systems are conserved from yeast to man.The type VI secretion system deploys antifungal effectors against microbial competitorsControl of the Terminal Step of Intracellular Membrane Fusion by Protein Phosphatase 1 A regulatedMET3-GLC7 gene fusion provides evidence of a mitotic role forSaccharomyces cerevisiae protein phosphatase 1Proteins Interacting With Saccharomyces cerevisiae Type 1 Protein Phosphatase Catalytic Subunit Identified by Single-Step Affinity Purification and Mass SpectrometryScreening and characterization of microbial inhibitors against eukaryotic protein phosphatases (PP1 and PP2A)Mating-type locus control of killer toxins fromKluyveromyces lactisandPichia acaciaeMutations in SPC110, encoding the yeast spindle pole body calmodulin-binding protein, cause defects in cell integrity as well as spindle formationThe Phosphorylation State of the 110 kDa Component of the Yeast Spindle Pole Body Shows Cell Cycle Dependent RegulationKti12, a PSTK-like tRNA dependent ATPase essential for tRNA modification by Elongator.
P50
Q27011240-7D17A7EF-E302-4C7F-9918-6A1396FFDC6FQ27930355-6EB3C3B5-B483-447D-A8C1-482927982A8EQ27931438-FAEE697B-73A7-41FE-9FB6-B3DCD2A38E1FQ27931885-3392D166-6623-4816-9B76-EF2ADD07BF33Q27932912-00EAAC76-847D-4EFC-B5A0-557C8A9F59AFQ27933238-57A2B941-E1EC-44BB-98AA-4DE60481674BQ27934196-1A40D1B8-AD9A-4C88-945B-9201C7DAE62FQ27936407-769708C5-E7E3-477B-80D2-E02C9B0D1DFEQ27937233-EA028B31-BB4D-4C5F-B82C-26CB2393E92CQ27937480-2C1F078A-CACD-498C-A9CF-2889EF3962A0Q27937983-D4963C85-54AE-4A00-B724-23A75D28BE61Q27939198-F146E51D-A2E4-4BFC-962D-0A0BCAAC080DQ29619579-F1748430-6D82-4F54-8A31-E271C1D31B4BQ30320232-7E97E02E-A1BC-4CCC-9AEB-649B14E738E6Q30320615-F715BA81-FFD5-4E28-A150-894F2186291DQ30320879-5195EA28-1C01-4202-A803-FB81F9E3C08DQ33296914-795DFB8B-FB37-4AED-9217-9B5E72743C16Q34652362-5478B611-676C-40C4-9A89-556329518255Q35099863-B383C282-A0E7-4A4D-B746-68458B968E3FQ36337950-388AB4D5-5EED-44F6-BC21-9990E452B06FQ36725474-8956ABD4-D0E3-448B-947D-2435F739FBBCQ37343700-B63E8AD2-A748-42A5-93CF-BD27F6E26671Q38654369-8B014967-EABD-42F0-8817-20937DFDB4E9Q41669285-8D6D4CBF-7AE5-458F-A97C-4B66B7BA521EQ41837810-A3AC3E0D-1BB4-493A-AC28-F3D6E0A95C1CQ41998714-09D75C4D-DBE5-47B2-B463-FCA073D5DA4EQ42052783-1CD46CDE-700A-4177-BFDB-528CF9A40BF3Q43095337-B1E16956-3A6B-4380-B8D6-C6D5A92549AFQ44663709-2E36191C-60AA-4D05-957B-32BA290C8ED0Q46480035-BC94F3F0-C633-41E6-B077-0863F8CEC961Q54286226-8A0D38D5-95FA-47F2-830E-3A9FD2C99908Q57840409-D43E2E4C-C5B1-4636-B21D-3913AA02F5C3Q58197789-C3D73A3D-96E3-4EC1-BB10-1F0295BE9123Q58197792-15FDC7A9-98D3-4005-90BD-0C017029E8FAQ60154719-0C2CAE57-2B77-4100-AB99-434AE03AF617Q60154720-88C4E5E4-5F16-4B56-A1D9-1E9CE6825E51Q60154722-A1BB27D5-827F-493A-A668-6C2EF5F8A86AQ60154726-E6D7D470-706A-40E1-810A-AA4D07123B1EQ60154733-C9BC2FF2-7F6D-4CBA-8E7D-74E77C9E8882Q63953814-43ED8D72-4716-4F40-8A23-BB77BB49D9B7
P50
description
onderzoeker
@nl
researcher
@en
հետազոտող
@hy
name
Michael J Stark
@nl
Michael J Stark
@sl
Michael J. Stark
@en
Michael J. Stark
@es
type
label
Michael J Stark
@nl
Michael J Stark
@sl
Michael J. Stark
@en
Michael J. Stark
@es
prefLabel
Michael J Stark
@nl
Michael J Stark
@sl
Michael J. Stark
@en
Michael J. Stark
@es
P106
P1153
35075009300
P31
P496
0000-0001-9086-191X