Literature DB >> 11978480

Carbonyl modified proteins in cellular regulation, aging, and disease.

Rodney L Levine1.   

Abstract

The oxidative modification of proteins by reactive species is implicated in the etiology or progression of a panoply of disorders and diseases. The level of these modified molecules can be quantitated by measurement of the protein carbonyl content, which has been shown to increase in a variety of diseases and processes, notably during aging. For the most part, oxidatively modified proteins are not repaired and must be removed by proteolytic degradation, a process which normally proceeds very efficiently, from microorganisms to mammals. In eukaryotes, removal is usually carried out by the proteosome, which selectively degrades oxidatively modified proteins, whether they be damaged by reactive oxygen species or specifically oxidized by cellular regulatory processes. The molecular deficiencies that cause accumulation of oxidatively modified proteins are not identified, but regardless of cause, the accumulation is likely to disrupt normal cellular function.

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Year:  2002        PMID: 11978480     DOI: 10.1016/s0891-5849(02)00765-7

Source DB:  PubMed          Journal:  Free Radic Biol Med        ISSN: 0891-5849            Impact factor:   7.376


  160 in total

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2.  Elevated levels of protein carbonyls in sera of chronic fatigue syndrome patients.

Authors:  Iva V Smirnova; Martin L Pall
Journal:  Mol Cell Biochem       Date:  2003-06       Impact factor: 3.396

Review 3.  Measuring reactive species and oxidative damage in vivo and in cell culture: how should you do it and what do the results mean?

Authors:  Barry Halliwell; Matthew Whiteman
Journal:  Br J Pharmacol       Date:  2004-05       Impact factor: 8.739

Review 4.  Mechanisms of resistance to oxidative and nitrosative stress: implications for fungal survival in mammalian hosts.

Authors:  Tricia A Missall; Jennifer K Lodge; Joan E McEwen
Journal:  Eukaryot Cell       Date:  2004-08

Review 5.  Redox modification of cell signaling in the cardiovascular system.

Authors:  Dan Shao; Shin-ichi Oka; Christopher D Brady; Judith Haendeler; Philip Eaton; Junichi Sadoshima
Journal:  J Mol Cell Cardiol       Date:  2011-09-17       Impact factor: 5.000

6.  The reactivity of human serum albumin toward trans-4-hydroxy-2-nonenal.

Authors:  Qingyuan Liu; David C Simpson; Scott Gronert
Journal:  J Mass Spectrom       Date:  2012-04       Impact factor: 1.982

7.  Accumulation of oxidized proteins in Herpesvirus infected cells.

Authors:  Shomita S Mathew; Patrick W Bryant; April D Burch
Journal:  Free Radic Biol Med       Date:  2010-05-02       Impact factor: 7.376

8.  Fatty acid amide hydrolase is a key regulator of endocannabinoid-induced myocardial tissue injury.

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Journal:  Free Radic Biol Med       Date:  2010-11-09       Impact factor: 7.376

9.  Protective potential of Opuntia microdasys flower decoction on fructose-alloxan-induced diabetic rats on kidney and pancreas: chemical and immunohistochemical analyses.

Authors:  Hassiba Chahdoura; Aida Khlifi; Jihéne Ben Lamine; Borhane Eddine Cherif Ziani; Khawla Adouni; Safia El Bok; Zohra Haouas; Fadoua Neffati; Abdelfattah Zakhama; Guido Flamini; Lotfi Achour
Journal:  Environ Sci Pollut Res Int       Date:  2018-10-01       Impact factor: 4.223

10.  Mechanism of protein decarbonylation.

Authors:  Chi-Ming Wong; Lucia Marcocci; Dividutta Das; Xinhong Wang; Haibei Luo; Makhosazane Zungu-Edmondson; Yuichiro J Suzuki
Journal:  Free Radic Biol Med       Date:  2013-09-14       Impact factor: 7.376

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