Literature DB >> 9130258

Posttranslational arginylation of brain proteins.

M E Hallak1, G Bongiovanni.   

Abstract

The knowledge of brain protein metabolism is important in understanding nervous system brain function. Protein synthesis rates are high in young brain, decline rapidly at adult stages, and thereafter continue falling slowly with age. The breakdown of protein appears to follow a similar rate (1). Protein synthesis and degradation however, are only the two extremes of a complex phenomena which includes a variety of other protein modifications. Proteolytic cleavage is the most common covalent modification of proteins; probably all proteins that have been isolated were modified by proteolysis, since only few are found with the starting amino acid (methionine) attached. This suggests that most proteins were subject to one or more co- and/or posttranslational modifications (2). One of these posttranslational modifications is the arginylation of proteins, described 30 years ago, which now is being recognized as a widespread modification of proteins. In this review, the current status of posttranslational arginylation of brain proteins is discussed.

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Year:  1997        PMID: 9130258     DOI: 10.1023/a:1027315912242

Source DB:  PubMed          Journal:  Neurochem Res        ISSN: 0364-3190            Impact factor:   3.996


  32 in total

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Journal:  Proc Natl Acad Sci U S A       Date:  1996-03-05       Impact factor: 11.205

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Journal:  Eur J Biochem       Date:  1994-05-01

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Journal:  Biochem J       Date:  1990-04-15       Impact factor: 3.857

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Journal:  Neurochem Res       Date:  1993-11       Impact factor: 3.996

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  5 in total

1.  Post-translational arginylation of proteins in cultured cells.

Authors:  S Fissolo; G Bongiovanni; M B Decca; M E Hallak
Journal:  Neurochem Res       Date:  2000-01       Impact factor: 3.996

2.  Calreticulin and Arginylated Calreticulin Have Different Susceptibilities to Proteasomal Degradation.

Authors:  Victor E Goitea; Marta E Hallak
Journal:  J Biol Chem       Date:  2015-05-12       Impact factor: 5.157

3.  Arginylation-dependent neural crest cell migration is essential for mouse development.

Authors:  Satoshi Kurosaka; N Adrian Leu; Fangliang Zhang; Ralph Bunte; Sougata Saha; Junling Wang; Caiying Guo; Wei He; Anna Kashina
Journal:  PLoS Genet       Date:  2010-03-12       Impact factor: 5.917

4.  Arginyltransferase regulates alpha cardiac actin function, myofibril formation and contractility during heart development.

Authors:  Reena Rai; Catherine C L Wong; Tao Xu; N Adrian Leu; Dawei W Dong; Caiying Guo; K John McLaughlin; John R Yates; Anna Kashina
Journal:  Development       Date:  2008-10-23       Impact factor: 6.868

5.  Global analysis of posttranslational protein arginylation.

Authors:  Catherine C L Wong; Tao Xu; Reena Rai; Aaron O Bailey; John R Yates; Yuri I Wolf; Henry Zebroski; Anna Kashina
Journal:  PLoS Biol       Date:  2007-10       Impact factor: 8.029

  5 in total

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