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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
2
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pubmed:dateCreated |
2001-7-10
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pubmed:abstractText |
Glutaredoxins (GRXs) are ubiquitous GSH-dependent oxidoreductases, which catalyze the reduction of protein-glutathionyl-mixed disulfides and are considered to play an important role in the enzymatic regulation of redox-sensitive proteins. In this paper, we describe the identification and characterization of a new human homologue of the SH3BGR gene, named SH3BGRL3 (SH3 domain binding glutamic acid-rich protein like 3). SH3BGRL3 is widely expressed and codes for a highly conserved small protein, which shows a significant similarity to Glutaredoxin 1 (GRX1) of Escherichia coli and is predicted to belong to the Thioredoxin Superfamily. However, the SH3BGRL3 protein lacks both the conserved cysteine residues, which characterize the enzymatic active site of GRX. This structural feature raises the possibility that SH3BGRL3 could function as an endogenous modulator of GRX biological activity. EGFP-SH3BGRL3 fusion protein expressed in COS-7 cells localizes both to the nucleus and to the cytoplasm. The SH3BGRL3 gene was mapped to chromosome 1p34.3-35.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Bacterial Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/GLRX protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Glrx protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/Glutaredoxins,
http://linkedlifedata.com/resource/pubmed/chemical/Muscle Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Oxidoreductases,
http://linkedlifedata.com/resource/pubmed/chemical/Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/SH3BGR protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Thioredoxins
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pubmed:status |
MEDLINE
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pubmed:month |
Jul
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pubmed:issn |
0006-291X
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pubmed:author |
pubmed-author:ArrigoPP,
pubmed-author:CicconeEE,
pubmed-author:CintiRR,
pubmed-author:Di LisiRR,
pubmed-author:EgerBB,
pubmed-author:GhiottoFF,
pubmed-author:MaffeiMM,
pubmed-author:MazzoccoMM,
pubmed-author:RavazzoloRR,
pubmed-author:ScartezziniPP,
pubmed-author:VerganiGG
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pubmed:copyrightInfo |
Copyright 2001 Academic Press.
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pubmed:issnType |
Print
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pubmed:day |
13
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pubmed:volume |
285
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
540-5
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pubmed:dateRevised |
2007-11-15
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pubmed:meshHeading |
pubmed-meshheading:11444877-Amino Acid Sequence,
pubmed-meshheading:11444877-Animals,
pubmed-meshheading:11444877-Bacterial Proteins,
pubmed-meshheading:11444877-Base Sequence,
pubmed-meshheading:11444877-COS Cells,
pubmed-meshheading:11444877-Cell Line,
pubmed-meshheading:11444877-Cercopithecus aethiops,
pubmed-meshheading:11444877-Chromosome Mapping,
pubmed-meshheading:11444877-Chromosomes, Human, Pair 1,
pubmed-meshheading:11444877-Cloning, Molecular,
pubmed-meshheading:11444877-Conserved Sequence,
pubmed-meshheading:11444877-Escherichia coli,
pubmed-meshheading:11444877-Glutaredoxins,
pubmed-meshheading:11444877-Humans,
pubmed-meshheading:11444877-Jurkat Cells,
pubmed-meshheading:11444877-Mice,
pubmed-meshheading:11444877-Molecular Sequence Data,
pubmed-meshheading:11444877-Muscle Proteins,
pubmed-meshheading:11444877-Organ Specificity,
pubmed-meshheading:11444877-Oxidoreductases,
pubmed-meshheading:11444877-Proteins,
pubmed-meshheading:11444877-Reverse Transcriptase Polymerase Chain Reaction,
pubmed-meshheading:11444877-Sequence Alignment,
pubmed-meshheading:11444877-Sequence Homology, Amino Acid,
pubmed-meshheading:11444877-T-Lymphocytes,
pubmed-meshheading:11444877-Thioredoxins,
pubmed-meshheading:11444877-Transcription, Genetic,
pubmed-meshheading:11444877-Transfection,
pubmed-meshheading:11444877-Tumor Cells, Cultured
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pubmed:year |
2001
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pubmed:articleTitle |
A novel human homologue of the SH3BGR gene encodes a small protein similar to Glutaredoxin 1 of Escherichia coli.
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pubmed:affiliation |
Divisione di Neonatologia, E.O. Ospedali Galliera, Mura delle Cappuccine 14, I-16128 Genoa, Italy.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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