(Q39583866)

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:27435506%20AND%20SRC:MED&resulttype=core&format=json

19 March 2020

title

A comprehensive compilation of SUMO proteomics (English)

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:27435506%20AND%20SRC:MED&resulttype=core&format=json

19 March 2020

1

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:27435506%20AND%20SRC:MED&resulttype=core&format=json

19 March 2020

Alfred Vertegaal

series ordinal

2

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:27435506%20AND%20SRC:MED&resulttype=core&format=json

19 March 2020

author name string

Alfred C O Vertegaal

series ordinal

2

1 reference

13 September 2017

20 July 2016

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:27435506%20AND%20SRC:MED&resulttype=core&format=json

Nature Reviews Molecular Cell Biology

19 March 2020

published in

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:27435506%20AND%20SRC:MED&resulttype=core&format=json

19 March 2020

volume

17

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:27435506%20AND%20SRC:MED&resulttype=core&format=json

19 March 2020

issue

9

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:27435506%20AND%20SRC:MED&resulttype=core&format=json

19 March 2020

page(s)

581-595

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:27435506%20AND%20SRC:MED&resulttype=core&format=json

https://scigraph.springernature.com/pub.10.1038/nrm.2016.81

19 March 2020

exact match

0 references

cites work

System-wide changes to SUMO modifications in response to heat shock

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2016.81

Uncovering global SUMOylation signaling networks in a site-specific manner

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2016.81

Uncovering SUMOylation dynamics during cell-cycle progression reveals FoxM1 as a key mitotic SUMO target protein.

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2016.81

Sumoylation, a post-translational regulatory process in plants.

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2016.81

Concepts in sumoylation: a decade on

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2016.81

Sumoylation: a regulatory protein modification in health and disease

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2016.81

Ubiquitin signalling in DNA replication and repair

31 March 2020

2 references

https://api.crossref.org/works/10.1038%2FNRM.2016.81

31 March 2020

12 December 2020

Function and regulation of SUMO proteases

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2016.81

Regulation of DNA damage responses by ubiquitin and SUMO.

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2016.81

Mapping the SUMOylated landscape

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2016.81

SUMOylation-Mediated Regulation of Cell Cycle Progression and Cancer

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2016.81

A SUMOylation-dependent transcriptional subprogram is required for Myc-driven tumorigenesis

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2016.81

SUMO and ischemic tolerance

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2016.81

SUMOylation and deSUMOylation at a glance

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2016.81

Proteomic analysis of SUMO4 substrates in HEK293 cells under serum starvation-induced stress

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2016.81

Detecting endogenous SUMO targets in mammalian cells and tissues

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2016.81

In vivo identification of human small ubiquitin-like modifier polymerization sites by high accuracy mass spectrometry and an in vitro to in vivo strategy

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2016.81

Polymeric chains of SUMO-2 and SUMO-3 are conjugated to protein substrates by SAE1/SAE2 and Ubc9.

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2016.81

Nuclear and unclear functions of SUMO

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2016.81

Preferential modification of nuclear proteins by a novel ubiquitin-like molecule

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2016.81

Histone sumoylation is associated with transcriptional repression

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2016.81

Identification of SUMO-dependent chromatin-associated transcriptional repression components by a genome-wide RNAi screen.

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2016.81

Involvement of SUMO modification in MBD1- and MCAF1-mediated heterochromatin formation

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2016.81

PML is critical for ND10 formation and recruits the PML-interacting protein daxx to this nuclear structure when modified by SUMO-1

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2016.81

The mechanisms of PML-nuclear body formation

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2016.81

Role of PML and the PML-nuclear body in the control of programmed cell death

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2016.81

PML nuclear bodies: dynamic sensors of DNA damage and cellular stress

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2016.81

Principles of ubiquitin and SUMO modifications in DNA repair.

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2016.81

Modification of the human thymine-DNA glycosylase by ubiquitin-like proteins facilitates enzymatic turnover

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2016.81

Control of spontaneous and damage-induced mutagenesis by SUMO and ubiquitin conjugation

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2016.81

RAD6-dependent DNA repair is linked to modification of PCNA by ubiquitin and SUMO.

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2016.81

The SUMO modification pathway is involved in the BRCA1 response to genotoxic stress.

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2016.81

Mammalian SUMO E3-ligases PIAS1 and PIAS4 promote responses to DNA double-strand breaks

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2016.81

SUMO-targeted ubiquitin E3 ligase RNF4 is required for the response of human cells to DNA damage

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2016.81

RNF4, a SUMO-targeted ubiquitin E3 ligase, promotes DNA double-strand break repair

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2016.81

RNF4 is required for DNA double-strand break repair in vivo

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2016.81

SUMO modification regulates BLM and RAD51 interaction at damaged replication forks

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2016.81

SUMO modification of the ubiquitin-conjugating enzyme E2-25K

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2016.81

Functionality of human thymine DNA glycosylase requires SUMO-regulated changes in protein conformation

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2016.81

Specification of SUMO1- and SUMO2-interacting motifs

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2016.81

Poly-small ubiquitin-like modifier (PolySUMO)-binding proteins identified through a string search

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2016.81

Identification of a SUMO-binding motif that recognizes SUMO-modified proteins

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2016.81

Multivalent interactions of the SUMO-interaction motifs in RING finger protein 4 determine the specificity for chains of the SUMO

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2016.81

A role for non-covalent SUMO interaction motifs in Pc2/CBX4 E3 activity

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2016.81

SUMO-targeted ubiquitin ligases in genome stability.

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2016.81

A SIM-ultaneous role for SUMO and ubiquitin

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2016.81

Quality control of a transcriptional regulator by SUMO-targeted degradation

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2016.81

Nuclear organization in genome stability: SUMO connections

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2016.81

Conserved function of RNF4 family proteins in eukaryotes: targeting a ubiquitin ligase to SUMOylated proteins

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2016.81

RNF4 is a poly-SUMO-specific E3 ubiquitin ligase required for arsenic-induced PML degradation

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2016.81

Arsenic trioxide stimulates SUMO-2/3 modification leading to RNF4-dependent proteolytic targeting of PML.

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2016.81

Arsenic-induced SUMO-dependent recruitment of RNF4 into PML nuclear bodies

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2016.81

Arsenic degrades PML or PML-RARalpha through a SUMO-triggered RNF4/ubiquitin-mediated pathway

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2016.81

Fission yeast Rnf4 homologs are required for DNA repair.

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2016.81

RNF4-dependent hybrid SUMO-ubiquitin chains are signals for RAP80 and thereby mediate the recruitment of BRCA1 to sites of DNA damage.

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2016.81

A role for SUMO in nucleotide excision repair

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2016.81

Protein group modification and synergy in the SUMO pathway as exemplified in DNA repair

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2016.81

The SUMO system: a master organizer of nuclear protein assemblies.

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2016.81

Oxidative stress-induced assembly of PML nuclear bodies controls sumoylation of partner proteins

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2016.81

SUMOylation and PARylation cooperate to recruit and stabilize SLX4 at DNA damage sites.

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2016.81

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2016.81

Proteomics to study genes and genomes

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2016.81

Proteomic analysis of post-translational modifications

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2016.81

Andromeda: a peptide search engine integrated into the MaxQuant environment

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2016.81

MaxQuant enables high peptide identification rates, individualized p.p.b.-range mass accuracies and proteome-wide protein quantification

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2016.81

Status of large-scale analysis of post-translational modifications by mass spectrometry

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2016.81

Decoding signalling networks by mass spectrometry-based proteomics

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2016.81

Lysine acetylation targets protein complexes and co-regulates major cellular functions

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2016.81

A tissue-specific atlas of mouse protein phosphorylation and expression

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2016.81

Global, in vivo, and site-specific phosphorylation dynamics in signaling networks

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2016.81

Immunoaffinity enrichment and mass spectrometry analysis of protein methylation

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2016.81

Global identification of modular cullin-RING ligase substrates

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2016.81

A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2016.81

Systematic and quantitative assessment of the ubiquitin-modified proteome

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2016.81

Proteome-wide identification of SUMO2 modification sites

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2016.81

System-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.

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2016.81

SUMO-2 Orchestrates Chromatin Modifiers in Response to DNA Damage.

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2016.81

Mapping of SUMO sites and analysis of SUMOylation changes induced by external stimuli

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2016.81

Large-scale analysis of lysine SUMOylation by SUMO remnant immunoaffinity profiling.

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2016.81

System-wide identification of wild-type SUMO-2 conjugation sites

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2016.81

Molecular characterization of the SUMO-1 modification of RanGAP1 and its role in nuclear envelope association

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2016.81

A new vertebrate SUMO enzyme family reveals insights into SUMO-chain assembly

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2016.81

Structural basis for catalytic activation by the human ZNF451 SUMO E3 ligase

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2016.81

The ubiquitin-proteasome system is a key component of the SUMO-2/3 cycle

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2016.81

Heat shock induces a massive but differential inactivation of SUMO-specific proteases

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2016.81

A cellular system that degrades misfolded proteins and protects against neurodegeneration

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2016.81

Proteome-wide analysis of SUMO2 targets in response to pathological DNA replication stress in human cells

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2016.81

Proteotoxic stress reprograms the chromatin landscape of SUMO modification.

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2016.81

Sumoylation of heterogeneous nuclear ribonucleoproteins, zinc finger proteins, and nuclear pore complex proteins: a proteomic analysis

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2016.81

SUMO modification of heterogeneous nuclear ribonucleoproteins

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2016.81

DNA damage-induced heterogeneous nuclear ribonucleoprotein K sumoylation regulates p53 transcriptional activation

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2016.81

SUMOylation of hnRNP-K is required for p53-mediated cell-cycle arrest in response to DNA damage

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2016.81

Formation and Nuclear Export of Preribosomes Are Functionally Linked to the Small-Ubiquitin-Related Modifier Pathway

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2016.81

The SUMO system controls nucleolar partitioning of a novel mammalian ribosome biogenesis complex

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2016.81

A proteomic screen for nucleolar SUMO targets shows SUMOylation modulates the function of Nop5/Nop58.

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2016.81

Nuclear export and cytoplasmic maturation of ribosomal subunits

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2016.81

Association of the human SUMO-1 protease SENP2 with the nuclear pore

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2016.81

A nuclear envelope protein linking nuclear pore basket assembly, SUMO protease regulation, and mRNA surveillance

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2016.81

SUMO-1 modification of histone deacetylase 1 (HDAC1) modulates its biological activities

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2016.81

SUMO promotes HDAC-mediated transcriptional repression.

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2016.81

The SUMO E3 ligase RanBP2 promotes modification of the HDAC4 deacetylase

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2016.81

SUMOylation negatively modulates target gene occupancy of the KDM5B, a histone lysine demethylase

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2016.81

SUMO-targeted ubiquitin ligases.

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2016.81

SUMOylation of Psmd1 controls Adrm1 interaction with the proteasome

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2016.81

The SUMO pathway is essential for nuclear integrity and chromosome segregation in mice

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2016.81

SUMOylation inhibits FOXM1 activity and delays mitotic transition.

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2016.81

SUMO-2/3 modification and binding regulate the association of CENP-E with kinetochores and progression through mitosis

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2016.81

DNA repair factor XPC is modified by SUMO-1 and ubiquitin following UV irradiation

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2016.81

Sumoylation of MDC1 is important for proper DNA damage response

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2016.81

c-Myc is targeted to the proteasome for degradation in a SUMOylation-dependent manner, regulated by PIAS1, SENP7 and RNF4

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2016.81

SUMOylation of Myc-family proteins

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2016.81

Comprehensive identification of SUMO2/3 targets and their dynamics during mitosis

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2016.81

Identification of SUMO-2/3-modified proteins associated with mitotic chromosomes

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2016.81

Regulation of SUMO2 target proteins by the proteasome in human cells exposed to replication stress

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2016.81

SUMO-1 conjugation in vivo requires both a consensus modification motif and nuclear targeting

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2016.81

Structural basis for E2-mediated SUMO conjugation revealed by a complex between ubiquitin-conjugating enzyme Ubc9 and RanGAP1

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2016.81

Site-specific identification of SUMO-2 targets in cells reveals an inverted SUMOylation motif and a hydrophobic cluster SUMOylation motif

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2016.81

An extended consensus motif enhances the specificity of substrate modification by SUMO

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2016.81

PDSM, a motif for phosphorylation-dependent SUMO modification

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2016.81

Oncogenic Ras abrogates MEK SUMOylation that suppresses the ERK pathway and cell transformation

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2016.81

p300 Transcriptional Repression Is Mediated by SUMO Modification

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2016.81

An acetylation switch regulates SUMO-dependent protein interaction networks.

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2016.81

Proteomic analyses reveal divergent ubiquitylation site patterns in murine tissues

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2016.81

Mass Spectrometric Analysis of Lysine Ubiquitylation Reveals Promiscuity at Site Level

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2016.81

Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2016.81

Mislocalized activation of oncogenic RTKs switches downstream signaling outcomes

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2016.81

31 March 2020

Ubiquitin modifications

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2016.81

Expanding the ubiquitin code through post-translational modification

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2016.81

Defining roles of PARKIN and ubiquitin phosphorylation by PINK1 in mitochondrial quality control using a ubiquitin replacement strategy.

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2016.81

PINK1 phosphorylates ubiquitin to activate Parkin E3 ubiquitin ligase activity

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2016.81

SUMO chains: polymeric signals

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2016.81

Identification of the enzyme required for activation of the small ubiquitin-like protein SUMO-1

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2016.81

Expression and regulation of the mammalian SUMO-1 E1 enzyme

31 March 2020

2 references

https://api.crossref.org/works/10.1038%2FNRM.2016.81

31 March 2020

12 December 2020

SUMO: a history of modification

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2016.81

Protein modification by SUMO

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2016.81

Insights into E3 ligase activity revealed by a SUMO-RanGAP1-Ubc9-Nup358 complex

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2016.81

The small ubiquitin-like modifier-1 (SUMO-1) consensus sequence mediates Ubc9 binding and is essential for SUMO-1 modification

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2016.81

A new protease required for cell-cycle progression in yeast

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2016.81

Modification in reverse: the SUMO proteases

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2016.81

The SUMO-specific protease SENP5 is required for cell division

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2016.81

SUMO-specific protease 1 is essential for stabilization of HIF1alpha during hypoxia

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2016.81

Distinct and overlapping sets of SUMO-1 and SUMO-2 target proteins revealed by quantitative proteomics

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2016.81

Proteomics analysis of nucleolar SUMO-1 target proteins upon proteasome inhibition.

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2016.81

Purification and identification of endogenous polySUMO conjugates

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2016.81

Comparative proteomic analysis identifies a role for SUMO in protein quality control

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2016.81

Proteomic analysis of ubiquitin-like posttranslational modifications induced by the adenovirus E4-ORF3 protein

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2016.81

Functional Proteomics Study Reveals SUMOylation of TFII-I is Involved in Liver Cancer Cell Proliferation.

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2016.81

Role of SUMO-1-modified PML in nuclear body formation

31 March 2020

1 reference

PubMed

12 December 2020

Viral immediate-early proteins abrogate the modification by SUMO-1 of PML and Sp100 proteins, correlating with nuclear body disruption

1 reference

PubMed

12 December 2020

Identifiers

DOI

10.1038/NRM.2016.81

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:27435506%20AND%20SRC:MED&resulttype=core&format=json

19 March 2020

1 reference