about
The modified base J is the target for a novel DNA-binding protein in kinetoplastid protozoansA UV-induced genetic network links the RSC complex to nucleotide excision repair and shows dose-dependent rewiring.An N-terminal acidic region of Sgs1 interacts with Rpa70 and recruits Rad53 kinase to stalled forks.A key role for Chd1 in histone H3 dynamics at the 3' ends of long genes in yeastDirect screening for chromatin status on DNA barcodes in yeast delineates the regulome of H3K79 methylation by Dot1A barcode screen for epigenetic regulators reveals a role for the NuB4/HAT-B histone acetyltransferase complex in histone turnoverRecombination-induced tag exchange to track old and new proteins.Patterns and mechanisms of ancestral histone protein inheritance in budding yeast.Localized H3K36 methylation states define histone H4K16 acetylation during transcriptional elongation in Drosophila.Dot1 histone methyltransferases share a distributive mechanism but have highly diverged catalytic properties.Spatiotemporal analysis of organelle and macromolecular complex inheritanceChemical biology approaches to probe the proteome.A modified epigenetics toolbox to study histone modifications on the nucleosome core.The emerging roles of DOT1L in leukemia and normal development.Progressive methylation of ageing histones by Dot1 functions as a timer.A network model of the molecular organization of chromatin in Drosophila.Recombination-induced tag exchange (RITE) cassette series to monitor protein dynamics in Saccharomyces cerevisiae.Flexibility in crosstalk between H2B ubiquitination and H3 methylation in vivoDot1 binding induces chromatin rearrangements by histone methylation-dependent and -independent mechanisms.Heterologous expression reveals distinct enzymatic activities of two DOT1 histone methyltransferases of Trypanosoma brucei.N-terminal acetylation and replicative age affect proteasome localization and cell fitness during aging.Mutational analysis of the Sir3 BAH domain reveals multiple points of interaction with nucleosomes.Yeast PP4 interacts with ATR homolog Ddc2-Mec1 and regulates checkpoint signaling.Nonprocessive methylation by Dot1 leads to functional redundancy of histone H3K79 methylation states.Drug toxicity profiling of a Saccharomyces cerevisiae deubiquitinase deletion panel shows that acetaminophen mimics tyrosine.CD8– dendritic cells preferentially cross-presentSaccharomyces cerevisiae antigensNews about old histones: A role for histone age in controlling the epigenomeThe modified DNA base beta-D-glucosylhydroxymethyluracil confers resistance to micrococcal nuclease and is incompletely recovered by 32P-postlabelingCrosstalk between aging and the epigenomeDecoding the chromatin proteome of a single genomic locus by DNA sequencingA novel germline variant in the DOT1L gene co-segregating in a Dutch family with a history of melanomaInhibition of transcription leads to rewiring of locus-specific chromatin proteomesEpi-ID: Systematic and Direct Screening for Chromatin Regulators in Yeast by Barcode-ChIP-SeqApplication of Recombination -Induced Tag Exchange (RITE) to study histone dynamics in human cellsDot1 promotes H2B ubiquitination by a methyltransferase-independent mechanismCD4+ T cell help creates memory CD8+ T cells with innate and help-independent recall capacitiesConserved crosstalk between histone deacetylation and H3K79 methylation generates DOT1L-dose dependency in HDAC1-deficient thymic lymphomaA genetic interaction map centered on cohesin reveals auxiliary factors in sister chromatid cohesion
P50
Q22066054-C4B5B02F-1E8A-4F8E-9F54-5F05F39FC236Q27930598-249B6F5C-E8F7-4E33-B49D-B4A043287C2FQ27933571-BFEEAD7C-FDA5-4B0D-847D-EC9040C37F8DQ28481279-C336FC3C-8891-4034-9B5C-A9BCD03BB805Q28818751-B2D305E3-0189-4D43-B3D0-F64BB0162D0CQ31036616-EB0DDBF6-8E56-4D29-BAB3-2DAB27BA2527Q33591551-A78E59BA-D43C-4B32-9AB9-261DD90DBC90Q33930554-6DE5B670-ED99-4C00-8B3A-0406EEB3B7AAQ36274737-66BD8530-4FA5-4CC5-A88C-967C309D595DQ36293950-2B061BBC-1D42-43B7-9DE5-10F781A8DB54Q36512250-77219FAF-14ED-4203-BAF9-F8DAD2CD6D16Q37313174-E4998188-7634-4E6C-97F7-BDEDD83A9183Q37829707-AE3A8A29-E266-4B7C-86CA-3157035E9C35Q38214063-AFA94D0A-D5A3-47BC-8D70-54D7631680FAQ38296266-DDFECCEC-077B-4054-871D-2B1C0D2961D9Q39188957-48A9C007-D15B-4871-8E49-A0F22DEBE1C2Q41940776-C413E4D3-755C-456E-B765-B12ACC102435Q42551223-C7E3626D-8DA6-46FB-9001-08264E8BBDB7Q42602158-B834C15F-9E4E-4463-8E8B-3B7D44736967Q42805713-0992FCA2-D276-4F9C-8FA5-16E9B59930F2Q43088198-5BF62A44-81C8-4585-A588-8BB1A317CE5FQ43127474-D7E83121-2D6B-4B4C-9BA7-59F44C51F152Q44916228-6598923D-6572-4E18-A1EA-707B800EAEB6Q46567995-5E3A830C-D3DB-47CD-BF66-11907BE69EEAQ47273765-FFD828A3-DD1B-4D24-A679-DEB905DDF308Q60251156-70845D44-CD0F-47B1-BB00-CE34569389EAQ60644732-0121BAE3-A879-44B0-A576-9A2B9DE354B1Q74506688-73D3A35F-3EEE-48D3-A283-7477EFE5D768Q83443554-49FAAE48-8EE1-4A74-9ED4-A14EBC1035E9Q90036650-9AB68D39-54D6-4704-9BA5-847C8E5DA556Q90121660-C6671BFE-3912-4736-AE8F-175C71148BB4Q90437137-182B8098-22A2-4843-8E4F-B7BC1A6F342EQ90645719-64805412-53D6-4AD9-9471-BEDC462139AAQ90758704-E7B66409-8413-4DF7-88CD-68626526B091Q91375252-DD419716-4B80-4193-9531-ED5C5EFBCD37Q91666115-4B160E72-D676-4EE2-94CD-54DDCCCCC294Q91871911-B02BD786-BC9C-4787-B8B8-626875C0E078Q91997228-54913B08-2138-4513-8E67-F4801295FD08
P50
description
hulumtues
@sq
researcher
@en
wetenschapper
@nl
հետազոտող
@hy
name
Fred van Leeuwen
@ast
Fred van Leeuwen
@en
Fred van Leeuwen
@es
Fred van Leeuwen
@nl
Fred van Leeuwen
@sl
type
label
Fred van Leeuwen
@ast
Fred van Leeuwen
@en
Fred van Leeuwen
@es
Fred van Leeuwen
@nl
Fred van Leeuwen
@sl
prefLabel
Fred van Leeuwen
@ast
Fred van Leeuwen
@en
Fred van Leeuwen
@es
Fred van Leeuwen
@nl
Fred van Leeuwen
@sl
P1053
A-7698-2010
P106
P21
P31
P3829
P496
0000-0002-7267-7251