Ribosomal protein S3 is stabilized by sumoylation (Q24339379)

Ribosomal protein S3

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SUMO1 activating enzyme subunit 1

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Small ubiquitin like modifier 1

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Ubiquitin conjugating enzyme E2 I

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protein sumoylation

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author name string

Chang-Young Jang

1

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Hyun-Seock Shin

2

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Hag Dong Kim

3

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Jung Woo Kim

4

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Soo-Young Choi

5

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Joon Kim

6

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language of work or name

English

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publication date

28 October 2011

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24 September 2011

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Europe PubMed Central

PubMed publication ID

21968017

https://www.ebi.ac.uk/europepmc/webservices/rest/search?resulttype=core&format=json&query=SRC:MED AND EXT_ID:21968017

full work available at URL

13 December 2024

https://api.elsevier.com/content/article/PII:S0006291X11017037?httpAccept=text/xml

1 reference

10.1016/J.BBRC.2011.09.099

DOI

https://api.crossref.org/works/10.1016/J.BBRC.2011.09.099

https://api.elsevier.com/content/article/PII:S0006291X11017037?httpAccept=text/plain

13 December 2024

1 reference

10.1016/J.BBRC.2011.09.099

DOI

https://api.crossref.org/works/10.1016/J.BBRC.2011.09.099

Biochemical and Biophysical Research Communications

13 December 2024

published in

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volume

414

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issue

3

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page(s)

523-7

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Constitutive expression of human ribosomal protein L7 arrests the cell cycle in G1 and induces apoptosis in Jurkat T-lymphoma cells

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Modification in reverse: the SUMO proteases

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SUMO-1 modification of Mdm2 prevents its self-ubiquitination and increases Mdm2 ability to ubiquitinate p53.

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An E3-like factor that promotes SUMO conjugation to the yeast septins

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SP-RING for SUMO: new functions bloom for a ubiquitin-like protein

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SUMO-1 modification of IkappaBalpha inhibits NF-kappaB activation

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A new protease required for cell-cycle progression in yeast

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Regulation of gene-activation pathways by PIAS proteins in the immune system

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Involvement of ribosomal proteins in regulating cell growth and apoptosis: translational modulation or recruitment for extraribosomal activity?

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

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SUMO-1 conjugation to topoisomerase I: A possible repair response to topoisomerase-mediated DNA damage

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Interaction between human tRNA synthetases involves repeated sequence elements

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The ubiquitin-like proteins SMT3 and SUMO-1 are conjugated by the UBC9 E2 enzyme

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Implication of mammalian ribosomal protein S3 in the processing of DNA damage

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Characterization and Mechanism of Action of DrosophilaRibosomal Protein S3 DNA Glycosylase Activity for the Removal of Oxidatively Damaged DNA Bases

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

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c-Jun and p53 Activity Is Modulated by SUMO-1 Modification

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Differential regulation of sentrinized proteins by a novel sentrin-specific protease

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Conversion of the bifunctional 8-oxoguanine/beta-delta apurinic/apyrimidinic DNA repair activities of Drosophila ribosomal protein S3 into the human S3 monofunctional beta-elimination catalyst through a single amino acid change

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Altered cellular responses by varying expression of a ribosomal protein gene: sequential coordination of enhancement and suppression of ribosomal protein S3a gene expression induces apoptosis

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The ubiquitin-like protein Smt3p is activated for conjugation to other proteins by an Aos1p/Uba2p heterodimer

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SUMO-1 modification activates the transcriptional response of p53

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Activation of p53 by conjugation to the ubiquitin-like protein SUMO-1.

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Protein modification by SUMO

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