about
Site-specific identification of SUMO-2 targets in cells reveals an inverted SUMOylation motif and a hydrophobic cluster SUMOylation motifUncovering global SUMOylation signaling networks in a site-specific mannerSystem-wide identification of wild-type SUMO-2 conjugation sites.Label-Free Identification and Quantification of SUMO Target Proteins.A high-yield double-purification proteomics strategy for the identification of SUMO sites.c-Myc is targeted to the proteasome for degradation in a SUMOylation-dependent manner, regulated by PIAS1, SENP7 and RNF4System-wide Analysis of SUMOylation Dynamics in Response to Replication Stress Reveals Novel Small Ubiquitin-like Modified Target Proteins and Acceptor Lysines Relevant for Genome Stability.Site-specific mapping of the human SUMO proteome reveals co-modification with phosphorylation.A comprehensive compilation of SUMO proteomics.SUMO-2 Orchestrates Chromatin Modifiers in Response to DNA Damage.Ubiquitin-specific Protease 11 (USP11) Deubiquitinates Hybrid Small Ubiquitin-like Modifier (SUMO)-Ubiquitin Chains to Counteract RING Finger Protein 4 (RNF4).SUMO in the DNA damage response.Uncovering SUMOylation dynamics during cell-cycle progression reveals FoxM1 as a key mitotic SUMO target protein.Site-specific characterization of endogenous SUMOylation across species and organs.Systems-wide Analysis of Serine ADP-Ribosylation Reveals Widespread Occurrence and Site-Specific Overlap with PhosphorylationSUMOylation promotes protective responses to DNA-protein crosslinksAn Advanced Strategy for Comprehensive Profiling of ADP-ribosylation Sites Using Mass Spectrometry-based ProteomicsMulti-site SUMOylation restrains DNA polymerase η interactions with DNA damage sites
P50
Q24297572-F10E1DEA-CCD7-402C-A567-A1B57710D8F1Q34041994-E77158E4-3921-4538-BC14-8D0C6F4326D9Q35814214-6702B1C0-8D0B-4D8D-92D0-B8FF2ACFFDBDQ38746141-99A21BF8-4EE6-4C6C-88F4-62D799E2342EQ38750217-7C9454F6-6E6F-4A2F-A9ED-9B95EE2B0F83Q38884352-00B68128-8172-4AEF-9C19-AABB84E6DCB3Q38901752-21DDF244-6CB8-4176-9387-CC6EE69599A4Q39005647-E6BB1FEB-2286-4729-9D9F-D6A76059B304Q39583866-C0923831-2895-471D-B570-D356C52CB49AQ41836116-F0AE5256-9583-4290-9201-73207FF91B32Q42076334-65E10697-569F-48F2-A7CA-7D341BE65EBCQ43228311-E4D7F20E-55A9-4AFC-827A-0172339C6C75Q53064370-DEDF8754-7DFF-4B6D-B72A-3A3014579168Q55320105-93161112-0859-4B72-9DAD-31BECB101920Q58833071-78FF605A-7F43-4F26-ACA4-3CA3B65A611AQ64026834-67BA9D56-A096-4742-AC13-B25D41395038Q91859979-D1174018-B3A7-4E10-929B-D164E0FFBB5CQ94461375-82186038-917F-40EB-BDAB-57D952F3C695
P50
description
hulumtues
@sq
researcher
@en
wetenschapper
@nl
հետազոտող
@hy
name
Ivo A Hendriks
@ast
Ivo A Hendriks
@en
Ivo A Hendriks
@es
Ivo A Hendriks
@nl
Ivo A Hendriks
@sl
type
label
Ivo A Hendriks
@ast
Ivo A Hendriks
@en
Ivo A Hendriks
@es
Ivo A Hendriks
@nl
Ivo A Hendriks
@sl
prefLabel
Ivo A Hendriks
@ast
Ivo A Hendriks
@en
Ivo A Hendriks
@es
Ivo A Hendriks
@nl
Ivo A Hendriks
@sl
P106
P21
P31
P496
0000-0002-1439-3701