The DNA Damage Response: Making It Safe to Play with Knives

Molecular Cell, Journal Year: 2010, Volume and Issue: 40(2), P. 179 - 204

Published: Oct. 1, 2010

Language: Английский

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Targeting hypoxia in cancer therapy

Nature reviews. Cancer, Journal Year: 2011, Volume and Issue: 11(6), P. 393 - 410

Published: May 24, 2011

Language: Английский

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Glutathione catalysis and the reaction mechanisms of glutathione-dependent enzymes

Biochimica et Biophysica Acta (BBA) - General Subjects, Journal Year: 2012, Volume and Issue: 1830(5), P. 3217 - 3266

Published: Oct. 2, 2012

Glutathione-dependent catalysis is a metabolic adaptation to chemical challenges encountered by all life forms. In the course of evolution, nature optimized numerous mechanisms use glutathione as most versatile nucleophile for conversion plethora sulfur-, oxygen- or carbon-containing electrophilic substances.This comprehensive review summarizes fundamental principles and compares structures glutathione-dependent enzymes, including reductase, glutaredoxins, peroxidases, peroxiredoxins, glyoxalases 1 2, transferases MAPEG. Moreover, open mechanistic questions, evolutionary aspects physiological relevance are discussed each enzyme family.It surprising how little known about many often reaction geometries acid-base catalysts neglected, puzzles remain unsolved despite almost century research. On one hand, several families with non-related protein folds recognize moiety their substrates. other thioredoxin fold used catalysis. Ancient well recent structural changes this did not only significantly alter mechanism, but also resulted in completely different functions.Glutathione-dependent enzymes excellent study objects structure-function relationships molecular evolution. Notably, times systems biology, outcome models on metabolism redox regulation more than questionable long properties neither studied nor understood. Furthermore, presented could have implications drug development. This article part Special Issue entitled Cellular functions glutathione.

Language: Английский

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Thiyl Radicals in Organic Synthesis

Chemical Reviews, Journal Year: 2014, Volume and Issue: 114(5), P. 2587 - 2693

Published: Jan. 2, 2014

ADVERTISEMENT RETURN TO ISSUEReviewNEXTThiyl Radicals in Organic SynthesisFabrice Dénès*†, Mark Pichowicz‡, Guillaume Povie‡, and Philippe Renaud‡View Author Information† Laboratoire CEISAM UMR CNRS 6230 - UFR des Sciences et Techniques, Université de Nantes, 2 rue la Houssinière, BP 92208 44322 Nantes Cedex 3, France‡ Department of Chemistry Biochemistry, University Berne, Freiestrasse CH-3012 Bern, Switzerland*E-mail: [email protected]Cite this: Chem. Rev. 2014, 114, 5, 2587–2693Publication Date (Web):January 2, 2014Publication History Received13 August 2013Published online2 January 2014Published inissue 12 March 2014https://pubs.acs.org/doi/10.1021/cr400441mhttps://doi.org/10.1021/cr400441mreview-articleACS PublicationsCopyright © 2014 American Chemical SocietyRequest reuse permissionsArticle Views35344Altmetric-Citations758LEARN ABOUT THESE METRICSArticle Views are the COUNTER-compliant sum full text article downloads since November 2008 (both PDF HTML) across all institutions individuals. These metrics regularly updated to reflect usage leading up last few days.Citations number other articles citing this article, calculated by Crossref daily. Find more information about citation counts.The Altmetric Attention Score is a quantitative measure attention that research has received online. Clicking on donut icon will load page at altmetric.com with additional details score social media presence for given article. how calculated. Share Add toView InAdd Full Text ReferenceAdd Description ExportRISCitationCitation abstractCitation referencesMore Options onFacebookTwitterWechatLinked InRedditEmail Other access optionsGet e-Alertsclose SUBJECTS:Addition reactions,Cyclization,Hydrocarbons,Hydrogen abstraction,Thiols Get e-Alerts

Language: Английский

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SAMHD1 restricts the replication of human immunodeficiency virus type 1 by depleting the intracellular pool of deoxynucleoside triphosphates

Nature Immunology, Journal Year: 2012, Volume and Issue: 13(3), P. 223 - 228

Published: Feb. 12, 2012

Language: Английский

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Regulation of mammalian nucleotide metabolism and biosynthesis

Nucleic Acids Research, Journal Year: 2015, Volume and Issue: 43(4), P. 2466 - 2485

Published: Jan. 27, 2015

Nucleotides are required for a wide variety of biological processes and constantly synthesized de novo in all cells. When cells proliferate, increased nucleotide synthesis is necessary DNA replication RNA production to support protein at different stages the cell cycle, during which these events regulated multiple levels. Therefore precursor nucleotides also strongly Nucleotide an energy intensive process that uses metabolic pathways across compartments several sources carbon nitrogen. The transcription level by set master factors but enzyme allosteric regulation feedback inhibition. Here we review cellular demands biosynthesis, their mechanisms cycle. use stable isotope tracers delineating biosynthetic routes intersecting how quantitatively controlled under conditions highlighted. Moreover, importance viability discussed this may lead potential new approaches drug development diseases such as cancer.

Language: Английский

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Focus on mammalian thioredoxin reductases — Important selenoproteins with versatile functions

Biochimica et Biophysica Acta (BBA) - General Subjects, Journal Year: 2009, Volume and Issue: 1790(6), P. 495 - 526

Published: Feb. 18, 2009

Language: Английский

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Thioredoxin and thioredoxin reductase: Current research with special reference to human disease

Biochemical and Biophysical Research Communications, Journal Year: 2010, Volume and Issue: 396(1), P. 120 - 124

Published: May 1, 2010

Language: Английский

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The Radical SAM Superfamily

Critical Reviews in Biochemistry and Molecular Biology, Journal Year: 2008, Volume and Issue: 43(1), P. 63 - 88

Published: Jan. 1, 2008

The radical S-adenosylmethionine (SAM) superfamily currently comprises more than 2800 proteins with the amino acid sequence motif CxxxCxxC unaccompanied by a fourth conserved cysteine. charcteristic three-cysteine nucleates [4Fe–4S] cluster, which binds SAM as ligand to unique Fe not ligated cysteine residue. members participate in 40 distinct biochemical transformations, and most have been biochemically characterized. A handful of this purified at least partially Significant mechanistic structural information is available for lysine 2,3-aminomutase, pyruvate formate-lyase, coproporphyrinogen III oxidase, MoaA required molybdopterin biosynthesis. Biochemical spore photoproduct lyase, anaerobic ribonucleotide reductase activation subunit, lipoyl synthase, MiaB involved methylthiolation isopentenyladenine-37 tRNA. enzymes characterized date common cleavage [4Fe–4S]1 + –SAM complex [4Fe–4S]2 +–Met 5′ -deoxyadenosyl radical, abstracts hydrogen atom from substrate initiate mechanism.

Language: Английский

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Glutaredoxin systems

Biochimica et Biophysica Acta (BBA) - General Subjects, Journal Year: 2008, Volume and Issue: 1780(11), P. 1304 - 1317

Published: June 19, 2008

Language: Английский

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