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An ubiquitin ligase recognizing a protein oxidized by iron: implications for the turnover of oxidatively damaged proteins.

An ubiquitin ligase recognizing a protein oxidized by iron: implications for the turnover of oxidatively damaged proteins. Research Abstract Details 

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  • An ubiquitin ligase recognizing a protein oxidized by iron: implications for the turnover of oxidatively damaged proteins. Abstract Text:

    kazuhiro iwaiKazuhiro Iwai,

    Protein oxidation is a natural consequence of aerobic metabolism in cells. Oxidative modification of amino acid residues of proteins causes to lose activity or function of proteins. Organisms have thus developed pathways to remove oxidized proteins by rapid protein degradation. These pathways are important components in cellular quality control mechanisms. It has been suggested that oxidized proteins are degraded by the proteasome. However, whether ubiquitylation is necessary for the degradation of oxidized proteins remains a controversial issue. We have recently identified HOIL-1 (heme-oxidized IRP2 ubiquitin ligase-1) as an E3 ligase that recognizes a protein that has been oxidized by iron. This review describes the recent progress made in understanding the ubiquitin-proteolytic pathway and the regulation of iron metabolism. The process involved in eliminating oxidized proteins and the possible roles that HOIL-1 ubiquitin ligase may play in these processes are discussed.

    An ubiquitin ligase recognizing a protein oxidized by iron: implications for the turnover of oxidatively damaged proteins. Publishing Authors By Initials

    k iwaiK Iwai,

    For similar enzymes and coenzymes: enzymes: ligases: ubiquitin-protein ligase complexes: ubiquitin-protein ligases research abstracts see: enzymes and coenzymes: enzymes: ligases: ubiquitin-protein ligase complexes: ubiquitin-protein ligases research

    PUBMED ID PMID:

    MEDLINE DATE:

    An ubiquitin ligase recognizing a protein oxidized by iron: implications for the turnover of oxidatively damaged proteins. Journal Published:

    PUBLICATION TYPE: Review

    Journal: Journal of biochemistry

    VOLUME: 134

    Page Numbers: 175-82

    Journal Abbreviation: J. Biochem.

    ISSN: 0021-924X

    DAY: 19

    MONTH: Aug

    YEAR: 2003

    An ubiquitin ligase recognizing a protein oxidized by iron: implications for the turnover of oxidatively damaged proteins. Information

    Number of References: 50

    LANGUAGE: eng

    NlmUniqueID: 376600

    An ubiquitin ligase recognizing a protein oxidized by iron: implications for the turnover of oxidatively damaged proteins. Keywords Mesh Terms:

    KEYWORDS: Ubiquitin-Protein Ligases

    MESH TERMS: metabolism

    Chemical & Substance for Abstract: An ubiquitin ligase recognizing a protein oxidized by iron: implications for the turnover of oxidatively damaged proteins. Information

    Substance Name: Ubiquitin-Protein Ligases

    Registry Number: EC 6.3.2.19

    Grant and Affiliation Information for An ubiquitin ligase recognizing a protein oxidized by iron: implications for the turnover of oxidatively damaged proteins.

    AFFILIATION: Department of Molecular Cell Biology, Graduate School of Medicine, Osaka City University, 1-4-3 Asahi-machi, Abeno-ku, Osaka 545-8585, and CREST, JST, Kawaguchi, Saitama 332-0012. kiwai@med.osaka-cu.ac.jp

    Country: Japan

    Japan Research PublicationJapan Research Publication

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    MEDLINETA: J Biochem

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