about
Arginine methylation regulates DNA polymerase betaModification of the human thymine-DNA glycosylase by ubiquitin-like proteins facilitates enzymatic turnoverT:G mismatch-specific thymine-DNA glycosylase (TDG) as a coregulator of transcription interacts with SRC1 family members through a novel tyrosine repeat motif.DNA glycosylases: in DNA repair and beyondBase excision by thymine DNA glycosylase mediates DNA-directed cytotoxicity of 5-fluorouracilNEJ1 controls non-homologous end joining in Saccharomyces cerevisiae.Conserved interactions of the splicing factor Ntr1/Spp382 with proteins involved in DNA double-strand break repair and telomere metabolism.SMC1 coordinates DNA double-strand break repair pathways.Saccharomyces cerevisiae LIF1: a function involved in DNA double-strand break repair related to mammalian XRCC4.T:G mismatch-specific thymine-DNA glycosylase potentiates transcription of estrogen-regulated genes through direct interaction with estrogen receptor alphaImmunohistochemical analysis reveals high frequency of PMS2 defects in colorectal cancerEmbryonic lethal phenotype reveals a function of TDG in maintaining epigenetic stabilityVersatile recombinant SUMOylation system for the production of SUMO-modified proteinModulation of age- and cancer-associated DNA methylation change in the healthy colon by aspirin and lifestyle.Spontaneous DNA damage, genome instability, and cancer--when DNA replication escapes control.ELF exposure system for live cell imaging.DNA fragmentation in human fibroblasts under extremely low frequency electromagnetic field exposure.The versatile thymine DNA-glycosylase: a comparative characterization of the human, Drosophila and fission yeast orthologs.Gadd45a promotes DNA demethylation through TDG.Translesion DNA synthesis: little fingers teach tolerance.Cell cycle regulation as a mechanism for functional separation of the apparently redundant uracil DNA glycosylases TDG and UNG2.Rad52-independent accumulation of joint circular minichromosomes during S phase in Saccharomyces cerevisiaeMeiotic recombination: sealing the partnership at the junction.7,8-Dihydro-8-oxoadenine, a highly mutagenic adduct, is repaired by Escherichia coli and human mismatch-specific uracil/thymine-DNA glycosylases.Oestrogen receptor β regulates epigenetic patterns at specific genomic loci through interaction with thymine DNA glycosylase.Biochemical reconstitution of TET1-TDG-BER-dependent active DNA demethylation reveals a highly coordinated mechanismThe enigmatic thymine DNA glycosylase.3CAPS - a structural AP-site analogue as a tool to investigate DNA base excision repair.Resources for methylome analysis suitable for gene knockout studies of potential epigenome modifiersDNA Repair in mammalian cells: Mismatched repair: variations on a theme.Reversible Top1 cleavage complexes are stabilized strand-specifically at the ribosomal replication fork barrier and contribute to ribosomal DNA stabilityFunctionality of human thymine DNA glycosylase requires SUMO-regulated changes in protein conformation.Active DNA demethylation by DNA repair: Facts and uncertainties.Extremely low-frequency magnetic fields and risk of childhood leukemia: A risk assessment by the ARIMMORA consortium.Acetylation regulates the DNA end-trimming activity of DNA polymerase beta.Identification of hMutLbeta, a heterodimer of hMLH1 and hPMS1.Recognition of DNA alterations by the mismatch repair systemDNA ligase 4 stabilizes the ribosomal DNA array upon fork collapse at the replication fork barrier.Tet oxidizes thymine to 5-hydroxymethyluracil in mouse embryonic stem cell DNA.Sumoylation of poly(ADP-ribose) polymerase 1 inhibits its acetylation and restrains transcriptional coactivator function.
P50
Q24314833-10C14FC1-E142-45AD-ABC2-87E692C49483Q24534803-526CAB44-5677-4556-A169-CA76A815FD1CQ24817047-DA0B846F-A5AC-4048-A5E5-D75E3BE230B1Q26830166-32E0626C-69B5-455E-B40E-EEEDCF4F42BBQ27863401-16AB9DE7-5C4A-4911-BD33-AF38561D8974Q27930222-2F40EC3F-5B11-4D7A-8FE1-D62F0660EE38Q27930755-67B96FC2-0025-4CDA-99E2-DAC2712D1EDFQ27931613-B2FA3FC6-A8C4-4CB7-BD61-DDA3AC22B429Q27938296-1473AC31-046D-447D-A763-F49C09C68D31Q28188710-F0603CFA-E86C-4D0C-A7B7-0B2BA0BD22A9Q28249924-F85ECADE-ACBE-43BE-9A0E-7EF50ABBA2EBQ28508931-69A5CA11-4C72-403F-AB71-54435FB8BD6BQ28540592-9FD21809-3686-49C7-84D0-E4040C4DF050Q33958348-41532A13-8953-492B-8208-B330EC25D3FDQ34175345-AD2C3DF9-C5FA-4B85-93D2-065A37ED0887Q34466461-99308E87-F499-4B8F-AD3E-B81178E4BF2DQ34613583-A3193A23-C88D-461B-B79F-890A54426896Q34980538-8F3DEBEB-46E0-4968-8210-59BD578A7711Q35562151-2D7CE8E4-5B2B-4943-886A-58EAD79AA37BQ35798500-08D1E5E0-DB7A-404C-ABC0-253E5B42675FQ35893888-1A032BAE-EFBF-4036-BFA5-0B7B74371375Q35920107-2D67A597-2F3E-45F7-BF07-E6638E7886A0Q35959032-978FA8A4-E53A-47F3-B1EC-280A5F0DD7B9Q36559222-C67178DF-F1C2-4168-A181-9E095232E148Q36588163-FE7DBD4A-2970-47FB-867B-0CDE9B1DEA8BQ36651017-07FB454D-B6AC-4107-986F-BB39DABFA82DQ36658394-CC90CDD9-E7B1-4933-ADFC-72ED70F8E6B0Q36701059-FB5F0196-FD10-4FD7-A758-DBBAAEB939F3Q36742802-46E9F91E-EBA0-49AB-A2B0-4B03B7A11828Q37372520-08BB46A5-43A5-4305-B1BB-EF0C07D5FC8EQ37734415-2CBAA12F-7D8A-49F3-B198-0ED7617ADB09Q38328146-752FCB23-7086-4E5E-8FFE-FA29F34C3E3CQ38849765-E934F620-D90C-421F-A4AD-E1AC6D4A2591Q38893180-9A96FE79-7B88-4818-AE97-D03A5EE55D8DQ40687477-B33B19E4-2303-4AD8-9390-251BA4BCE402Q40920177-BA7D4D7D-3FAC-4695-81F7-E58E05E62853Q41886077-5FB0BF66-B9B6-4BC4-B34C-59EF1D1544E0Q43028286-205DC1E0-1AE9-44FB-BA1A-E2353F9C0EB8Q45128222-BB5B781C-3016-43D7-95DD-67901B8889DDQ45923700-6F225325-5684-4C7D-9143-8C5DB9B5271E
P50
description
onderzoeker
@nl
researcher ORCID ID = 0000-0003-1843-6147
@en
name
Primo Schär
@ast
Primo Schär
@en
Primo Schär
@nl
type
label
Primo Schär
@ast
Primo Schär
@en
Primo Schär
@nl
prefLabel
Primo Schär
@ast
Primo Schär
@en
Primo Schär
@nl
P1053
G-5967-2012
P106
P21
P31
P3829
P496
0000-0003-1843-6147