Linster, Carole L
[UCL]
Van Schaftingen, Emile
[UCL]
Hanson, Andrew D
[-]
It is increasingly evident that metabolites suffer various kinds of damage, that such damage happens in all organisms and that cells have dedicated systems for damage repair and containment. First, chemical biology is demonstrating that diverse metabolites are damaged by side reactions of 'promiscuous' enzymes or by spontaneous chemical reactions, that the products are useless or toxic and that the unchecked buildup of these products can be devastating. Second, genetic and genomic evidence from prokaryotes and eukaryotes is implicating a network of new, conserved enzymes that repair damaged metabolites or somehow pre-empt damage. Metabolite (that is, small-molecule) repair is analogous to macromolecule (DNA and protein) repair and seems from comparative genomic evidence to be equally widespread. Comparative genomics also implies that metabolite repair could be the function of many conserved protein families lacking known activities. How-and how well-cells deal with metabolite damage affects fields ranging from medical genetics to metabolic engineering.
- Golubev A.G., Biochemistry (Mosc.), 61, 2018 (1996)
- Tawfik Dan S, Messy biology and the origins of evolutionary innovations, 10.1038/nchembio.441
- Van Schaftingen E., Rzem R., Veiga-da-Cunha M., l-2-Hydroxyglutaric aciduria, a disorder of metabolite repair, 10.1007/s10545-008-1042-3
- Vinci Chris R., Clarke Steven G., Homocysteine Methyltransferases Mht1 and Sam4 Prevent the Accumulation of Age-damaged (R,S)-AdoMet in the YeastSaccharomyces cerevisiae, 10.1074/jbc.m110.113076
- D'Ari Richard, Casadesús Josep, Underground metabolism, 10.1002/(sici)1521-1878(199802)20:2<181::aid-bies10>3.0.co;2-0
- O'Brien Patrick J, Herschlag Daniel, Catalytic promiscuity and the evolution of new enzymatic activities, 10.1016/s1074-5521(99)80033-7
- Andersson I., Catalysis and regulation in Rubisco, 10.1093/jxb/ern091
- Richard John P., Kinetic parameters for the elimination reaction catalyzed by triosephosphate isomerase and an estimation of the reaction's physiological significance, 10.1021/bi00232a031
- KOCHHAR Sunil, CHRISTEN Philipp, Mechanism of racemization of amino acids by aspartate aminotransferase, 10.1111/j.1432-1033.1992.tb16584.x
- Bar-Even Arren, Noor Elad, Savir Yonatan, Liebermeister Wolfram, Davidi Dan, Tawfik Dan S., Milo Ron, The Moderately Efficient Enzyme: Evolutionary and Physicochemical Trends Shaping Enzyme Parameters, 10.1021/bi2002289
- Marbaix Alexandre Y., Noël Gaëtane, Detroux Aline M., Vertommen Didier, Van Schaftingen Emile, Linster Carole L., Extremely Conserved ATP- or ADP-dependent Enzymatic System for Nicotinamide Nucleotide Repair, 10.1074/jbc.c111.310847
- Fiehn Oliver, Barupal Dinesh K., Kind Tobias, Extending Biochemical Databases by Metabolomic Surveys, 10.1074/jbc.r110.173617
- Peterhansel C., Maurino V. G., Photorespiration Redesigned, 10.1104/pp.110.165019
- Thornalley P.J., Glyoxalase I – structure, function and a critical role in the enzymatic defence against glycation, 10.1042/bst0311343
- Galperin Michael Y., Moroz Olga V., Wilson Keith S., Murzin Alexey G., House cleaning, a part of good housekeeping, 10.1111/j.1365-2958.2005.04950.x
- Moroz Olga V., Murzin Alexey G., Makarova Kira S., Koonin Eugene V., Wilson Keith S., Galperin Michael Y., Dimeric dUTPases, HisE, and MazG belong to a New Superfamily of all-α NTP Pyrophosphohydrolases with Potential “House-cleaning” Functions, 10.1016/j.jmb.2005.01.030
- Bessman Maurice J., Frick David N., O'Handley Suzanne F., The MutT Proteins or “Nudix” Hydrolases, a Family of Versatile, Widely Distributed, “Housecleaning” Enzymes, 10.1074/jbc.271.41.25059
- Aussel Laurent, Zhao Weidong, Hébrard Magali, Guilhon Aude-Agnès, Viala Julie P. M., Henri Sandrine, Chasson Lionel, Gorvel Jean-Pierre, Barras Frédéric, Méresse Stéphane, Salmonella detoxifying enzymes are sufficient to cope with the host oxidative burst : Oxidative stress adaptation by Salmonella, 10.1111/j.1365-2958.2011.07611.x
- Jenkins Amy L., Zhang Yang, Ealick Steven E., Begley Tadhg P., Mutagenesis studies on TenA: A thiamin salvage enzyme from Bacillus subtilis, 10.1016/j.bioorg.2007.10.005
- Linster Carole L., Noël Gaëtane, Stroobant Vincent, Vertommen Didier, Vincent Marie-Françoise, Bommer Guido T., Veiga-da-Cunha Maria, Van Schaftingen Emile, Ethylmalonyl-CoA Decarboxylase, a New Enzyme Involved in Metabolite Proofreading, 10.1074/jbc.m111.281527
- Rafter G.W., J. Biol. Chem., 208, 799 (1954)
- Oppenheimer Norman J., Kaplan Nathan O., Glyceraldehyde-3-phosphate dehydrogenase catalyzed hydration of the 5-6 double bond of reduced β-nicotinamide adenine dinucleotide (βNADH). Formation of β-6-hydroxy-1,4,5,6-tetrahydronicotinamide adenine dinucleotide, 10.1021/bi00720a002
- Yoshida Akira, Dave Vibha, Inhibition of NADP-dependent dehydrogenases by modified products of NADPH, 10.1016/0003-9861(75)90344-6
- Acheson Scott A., Kirkman Henry N., Wolfenden Richard, Equilibrium of 5,6-hydration of NADH and mechanism of ATP-dependent dehydration, 10.1021/bi00419a030
- Aravind L., Guilt by Association: Contextual Information in Genome Analysis, 10.1101/gr.10.8.1074
- Stover Patrick, Schirch Verne, The metabolic role of leucovorin, 10.1016/0968-0004(93)90162-g
- Baggott Joseph E., Hydrolysis of 5,10-Methenyltetrahydrofolate to 5-Formyltetrahydrofolate at pH 2.5 to 4.5, 10.1021/bi001362m
- Jeanguenin Linda, Lara-Núñez Aurora, Pribat Anne, Mageroy Melissa Hamner, Gregory Jesse F., Rice Kelly C., de Crécy-Lagard Valérie, Hanson Andrew D., Moonlighting Glutamate Formiminotransferases Can Functionally Replace 5-Formyltetrahydrofolate Cycloligase, 10.1074/jbc.m110.190504
- Hoffman Jerald L., Chromatographic analysis of the chiral and covalent instability of S-adenosyl-L-methionine, 10.1021/bi00363a041
- Vinci Chris R., Clarke Steven G., Recognition of Age-damaged (R,S)-Adenosyl-L-methionine by Two Methyltransferases in the YeastSaccharomyces cerevisiae, 10.1074/jbc.m610029200
- Rzem R., Vincent M.-F., Van Schaftingen E., Veiga-da-Cunha M., l-2-Hydroxyglutaric aciduria, a defect of metabolite repair, 10.1007/s10545-007-0487-0
- Wright S. Kirk, Viola Ronald E., Alteration of the Specificity of Malate Dehydrogenase by Chemical Modulation of an Active Site Arginine, 10.1074/jbc.m100892200
- Rzem R., Van Schaftingen E., Veiga-da-Cunha M., The gene mutated in l-2-hydroxyglutaric aciduria encodes l-2-hydroxyglutarate dehydrogenase, 10.1016/j.biochi.2005.06.005
- Kalliri E., Mulrooney S. B., Hausinger R. P., Identification of Escherichia coli YgaF as an L-2-Hydroxyglutarate Oxidase, 10.1128/jb.01977-07
- Topcu M., L-2-Hydroxyglutaric aciduria: identification of a mutant gene C14orf160, localized on chromosome 14q22.1, 10.1093/hmg/ddh300
- Kranendijk Martijn, Struys Eduard A., Salomons Gajja S., Van der Knaap Marjo S., Jakobs Cornelis, Progress in understanding 2-hydroxyglutaric acidurias, 10.1007/s10545-012-9462-5
- Zhao G, Winkler M E, A novel alpha-ketoglutarate reductase activity of the serA-encoded 3-phosphoglycerate dehydrogenase of Escherichia coli K-12 and its possible implications for human 2-hydroxyglutaric aciduria., 10.1128/jb.178.1.232-239.1996
- ACHOURI Younes, NOËL Gaëtane, VERTOMMEN Didier, RIDER Mark H., VEIGA-DA-CUNHA Maria, van SCHAFTINGEN Emile, Identification of a dehydrogenase acting on D-2-hydroxyglutarate, 10.1042/bj20031933
- Kaufman E.E., J. Biol. Chem., 263, 16872 (1988)
- Dang Lenny, White David W., Gross Stefan, Bennett Bryson D., Bittinger Mark A., Driggers Edward M., Fantin Valeria R., Jang Hyun Gyung, Jin Shengfang, Keenan Marie C., Marks Kevin M., Prins Robert M., Ward Patrick S., Yen Katharine E., Liau Linda M., Rabinowitz Joshua D., Cantley Lewis C., Thompson Craig B., Vander Heiden Matthew G., Su Shinsan M., Cancer-associated IDH1 mutations produce 2-hydroxyglutarate, 10.1038/nature08617
- Kranendijk M., Struys E. A., van Schaftingen E., Gibson K. M., Kanhai W. A., van der Knaap M. S., Amiel J., Buist N. R., Das A. M., de Klerk J. B., Feigenbaum A. S., Grange D. K., Hofstede F. C., Holme E., Kirk E. P., Korman S. H., Morava E., Morris A., Smeitink J., Sukhai R. N., Vallance H., Jakobs C., Salomons G. S., IDH2 Mutations in Patients with D-2-Hydroxyglutaric Aciduria, 10.1126/science.1192632
- Struys Eduard A., Salomons Gajja S., Achouri Younes, Van Schaftingen Emile, Grosso Salvatore, Craigen William J., Verhoeven Nanda M., Jakobs Cornelis, Mutations in the d-2-Hydroxyglutarate Dehydrogenase Gene Cause d-2-Hydroxyglutaric Aciduria, 10.1086/427890
- Waite M., J. Biol. Chem., 237, 2750 (1962)
- FUJII Tadashi, MUKAIHARA Manabu, AGEMATU Hitosi, TSUNEKAWA Hiroshi, Biotransformation ofL-Lysine toL-Pipecolic Acid Catalyzed byL-Lysine 6-Aminotransferase and Pyrroline-5-carboxylate Reductase, 10.1271/bbb.66.622
- Mills Philippa B, Struys Eduard, Jakobs Cornelis, Plecko Barbara, Baxter Peter, Baumgartner Matthias, Willemsen Michèl A A P, Omran Heymut, Tacke Uta, Uhlenberg Birgit, Weschke Bernhard, Clayton Peter T, Mutations in antiquitin in individuals with pyridoxine-dependent seizures, 10.1038/nm1366
- Struys Eduard A., Jakobs Cornelis, Metabolism of lysine in α-aminoadipic semialdehyde dehydrogenase-deficient fibroblasts: Evidence for an alternative pathway of pipecolic acid formation, 10.1016/j.febslet.2009.11.055
- Goyer Aymeric, Johnson Tanya L., Olsen Laura J., Collakova Eva, Shachar-Hill Yair, Rhodes David, Hanson Andrew D., Characterization and Metabolic Function of a Peroxisomal Sarcosine and Pipecolate Oxidase fromArabidopsis, 10.1074/jbc.m400071200
- Hagedorn Curt H., Phang James M., Transfer of reducing equivalents into mitochondria by the interconversions of proline and Δ1-pyrroline-5-carboxylate, 10.1016/0003-9861(83)90010-3
- Rayapati P. J., Stewart C. R., Hack E., Pyrroline-5-Carboxylate Reductase Is in Pea (Pisum sativum L.) Leaf Chloroplasts, 10.1104/pp.91.2.581
- Ning Baitang, Elbein Alan D., Cloning, expression and characterization of the pig liver GDP-mannose pyrophosphorylase : Evidence that GDP-mannose and GDP-Glc pyrophosphorylases are different proteins, 10.1046/j.1432-1033.2000.01781.x
- Adler Lital N., Gomez Tara A., Clarke Steven G., Linster Carole L., A Novel GDP-d-glucose Phosphorylase Involved in Quality Control of the Nucleoside Diphosphate Sugar Pool inCaenorhabditis elegansand Mammals, 10.1074/jbc.m111.238774
- Linster Carole L., Gomez Tara A., Christensen Kathryn C., Adler Lital N., Young Brian D., Brenner Charles, Clarke Steven G., ArabidopsisVTC2Encodes a GDP-l-Galactose Phosphorylase, the Last Unknown Enzyme in the Smirnoff-Wheeler Pathway to Ascorbic Acid in Plants, 10.1074/jbc.m702094200
- Lambrecht Jennifer A., Flynn Jeffrey M., Downs Diana M., Conserved YjgF Protein Family Deaminates Reactive Enamine/Imine Intermediates of Pyridoxal 5′-Phosphate (PLP)-dependent Enzyme Reactions, 10.1074/jbc.m111.304477
- Choe Eunok, Huang Rongmin, Min David B., Chemical Reactions and Stability of Riboflavin in Foods, 10.1111/j.1365-2621.2005.tb09055.x
- Grininger Martin, Zeth Kornelius, Oesterhelt Dieter, Dodecins: A Family of Lumichrome Binding Proteins, 10.1016/j.jmb.2005.12.072
- Grininger Martin, Staudt Heike, Johansson Patrik, Wachtveitl Josef, Oesterhelt Dieter, Dodecin Is the Key Player in Flavin Homeostasis of Archaea, 10.1074/jbc.m808063200
- Burow Meike, Markert Jana, Gershenzon Jonathan, Wittstock Ute, Comparative biochemical characterization of nitrile-forming proteins from plants and insects that alter myrosinase-catalysed hydrolysis of glucosinolates : Nitrile-forming proteins from plants and insects, 10.1111/j.1742-4658.2006.05252.x
- Keeley Jon E., Rundel Philip W., Evolution of CAM and C4Carbon‐Concentrating Mechanisms, 10.1086/374192
- Helling R. B., Janes B. K., Kimball H., Tran T., Bundesmann M., Check P., Phelan D., Miller C., Toxic Waste Disposal in Escherichia coli, 10.1128/jb.184.13.3699-3703.2002
- Nichols Robert J., Sen Saunak, Choo Yoe Jin, Beltrao Pedro, Zietek Matylda, Chaba Rachna, Lee Sueyoung, Kazmierczak Krystyna M., Lee Karis J., Wong Angela, Shales Michael, Lovett Susan, Winkler Malcolm E., Krogan Nevan J., Typas Athanasios, Gross Carol A., Phenotypic Landscape of a Bacterial Cell, 10.1016/j.cell.2010.11.052
- Baba Tomoya, Ara Takeshi, Hasegawa Miki, Takai Yuki, Okumura Yoshiko, Baba Miki, Datsenko Kirill A, Tomita Masaru, Wanner Barry L, Mori Hirotada, Construction of Escherichia coli K-12 in-frame, single-gene knockout mutants: the Keio collection, 10.1038/msb4100050
- Goyer Aymeric, Collakova Eva, de la Garza Rocío Díaz, Quinlivan Eoin P., Williamson Jerry, Gregory Jesse F., Shachar-Hill Yair, Hanson Andrew D., 5-Formyltetrahydrofolate Is an Inhibitory but Well Tolerated Metabolite inArabidopsisLeaves, 10.1074/jbc.m503106200
- Thiele Ines, Palsson Bernhard Ø, A protocol for generating a high-quality genome-scale metabolic reconstruction, 10.1038/nprot.2009.203
- Seaver S. M. D., Henry C. S., Hanson A. D., Frontiers in metabolic reconstruction and modeling of plant genomes, 10.1093/jxb/err371
- Waller J. C., Alvarez S., Naponelli V., Lara-Nunez A., Blaby I. K., Da Silva V., Ziemak M. J., Vickers T. J., Beverley S. M., Edison A. S., Rocca J. R., Gregory J. F., de Crecy-Lagard V., Hanson A. D., A role for tetrahydrofolates in the metabolism of iron-sulfur clusters in all domains of life, 10.1073/pnas.0911586107
- Galperin Michael Y., Koonin Eugene V., From complete genome sequence to ‘complete’ understanding?, 10.1016/j.tibtech.2010.05.006
- Gerdes Svetlana, El Yacoubi Basma, Bailly Marc, Blaby Ian K, Blaby-Haas Crysten E, Jeanguenin Linda, Lara-Núñez Aurora, Pribat Anne, Waller Jeffrey C, Wilke Andreas, Overbeek Ross, Hanson Andrew D, de Crécy-Lagard Valérie, Synergistic use of plant-prokaryote comparative genomics for functional annotations, 10.1186/1471-2164-12-s1-s2
- Chowdhury Rasheduzzaman, Yeoh Kar Kheng, Tian Ya-Min, Hillringhaus Lars, Bagg Eleanor A, Rose Nathan R, Leung Ivanhoe K H, Li Xuan S, Woon Esther C Y, Yang Ming, McDonough Michael A, King Oliver N, Clifton Ian J, Klose Robert J, Claridge Timothy D W, Ratcliffe Peter J, Schofield Christopher J, Kawamura Akane, The oncometabolite 2-hydroxyglutarate inhibits histone lysine demethylases, 10.1038/embor.2011.43
- Copley S.D., J. Cosmol., 10, 3345 (2010)
- Kruschwitz H.L., J. Biol. Chem., 269, 28757 (1994)
- Andreou Alexandra, Brodhun Florian, Feussner Ivo, Biosynthesis of oxylipins in non-mammals, 10.1016/j.plipres.2009.02.002
- Gould S. J., Lewontin R. C., The Spandrels of San Marco and the Panglossian Paradigm: A Critique of the Adaptationist Programme, 10.1098/rspb.1979.0086
- Izumi Y., Acta, 326, 485 (1973)
- Pierson D E, Campbell A, Cloning and nucleotide sequence of bisC, the structural gene for biotin sulfoxide reductase in Escherichia coli., 10.1128/jb.172.4.2194-2198.1990
- Bertoldi Mariarita, Voltattorni Carla Borri, Dopa decarboxylase exhibits low pH half-transaminase and high pH oxidative deaminase activities toward serotonin (5-hydroxytryptamine), 10.1110/ps.46601
- di Salvo Martino L., Safo Martin K., Musayev Faik N., Bossa Francesco, Schirch Verne, Structure and mechanism of Escherichia coli pyridoxine 5′-phosphate oxidase, 10.1016/s1570-9639(03)00060-8
- Fukui S., J. Biol. Chem., 240, 1315 (1965)
- Gangolf Marjorie, Wins Pierre, Thiry Marc, El Moualij Benaïssa, Bettendorff Lucien, Thiamine Triphosphate Synthesis in Rat Brain Occurs in Mitochondria and Is Coupled to the Respiratory Chain, 10.1074/jbc.m109.054379
- Lakaye Bernard, Makarchikov Alexander F., Antunes Adelio Fernandes, Zorzi Willy, Coumans Bernard, De Pauw Edwin, Wins Pierre, Grisar Thierry, Bettendorff Lucien, Molecular Characterization of a Specific Thiamine Triphosphatase Widely Expressed in Mammalian Tissues, 10.1074/jbc.m111241200
- Cooper Arthur J.L., The role of glutamine transaminase K (GTK) in sulfur and α-keto acid metabolism in the brain, and in the possible bioactivation of neurotoxicants, 10.1016/j.neuint.2003.12.002
- Kabil Omer, Banerjee Ruma, Redox Biochemistry of Hydrogen Sulfide, 10.1074/jbc.r110.128363
- Sikora M., Jakubowski H., Homocysteine editing and growth inhibition in Escherichia coli, 10.1099/mic.0.026609-0
- Lee Byung Cheon, Gladyshev Vadim N., The biological significance of methionine sulfoxide stereochemistry, 10.1016/j.freeradbiomed.2010.11.008
- Drozak Jakub, Veiga-da-Cunha Maria, Vertommen Didier, Stroobant Vincent, Van Schaftingen Emile, Molecular Identification of Carnosine Synthase as ATP-grasp Domain-containing Protein 1 (ATPGD1), 10.1074/jbc.m109.095505
- Kozmin Stanislav G., Leroy Prune, Pavlov Youri I., Schaaper Roel M., YcbX and yiiM, two novel determinants for resistance of Escherichia coli to N-hydroxylated base analogues, 10.1111/j.1365-2958.2008.06128.x
- Kotthaus Jürke, Wahl Bettina, Havemeyer Antje, Kotthaus Joscha, Schade Dennis, Garbe-Schönberg Dieter, Mendel Ralf, Bittner Florian, Clement Bernd, Reduction ofNω-hydroxy-L-arginine by the mitochondrial amidoxime reducing component (mARC), 10.1042/bj20100960
- Tagliabracci Vincent S., Heiss Christian, Karthik Chandra, Contreras Christopher J., Glushka John, Ishihara Mayumi, Azadi Parastoo, Hurley Thomas D., DePaoli-Roach Anna A., Roach Peter J., Phosphate Incorporation during Glycogen Synthesis and Lafora Disease, 10.1016/j.cmet.2011.01.017
- Cai Hui, Strouse Jane, Dumlao Darren, Jung Michael E., Clarke Steven, Distinct Reactions Catalyzed by Bacterial and Yeasttrans-Aconitate Methyltransferases†, 10.1021/bi0022902
- Cai Hui, Clarke Steven, A Novel Methyltransferase Catalyzes the Methyl Esterification oftrans-Aconitate inEscherichia coli, 10.1074/jbc.274.19.13470
- Cai Hui, Dumlao Darren, Katz Jonathan E., Clarke Steven, Identification of the Gene and Characterization of the Activity of thetrans-Aconitate Methyltransferase fromSaccharomyces cerevisiae†, 10.1021/bi011380j
- Andralojc Paul John, Madgwick Pippa J., Tao Yong, Keys Alfred, Ward Jane L., Beale Michael H., Loveland Jane E., Jackson Phil J., Willis Antony C., Gutteridge Steven, Parry Martin A.J., 2-Carboxy-D-arabinitol 1-phosphate (CA1P) phosphatase: evidence for a wider role in plant Rubisco regulation, 10.1042/bj20111443
- Aon J. C., Caimi R. J., Taylor A. H., Lu Q., Oluboyede F., Dally J., Kessler M. D., Kerrigan J. J., Lewis T. S., Wysocki L. A., Patel P. S., Suppressing Posttranslational Gluconoylation of Heterologous Proteins by Metabolic Engineering of Escherichia coli, 10.1128/aem.01790-07
- Saito Natsumi, Robert Martin, Kochi Hayataro, Matsuo Goh, Kakazu Yuji, Soga Tomoyoshi, Tomita Masaru, Metabolite Profiling Reveals YihU as a Novel Hydroxybutyrate Dehydrogenase for Alternative Succinic Semialdehyde Metabolism inEscherichia coli, 10.1074/jbc.m109.002089
- Fuhrer T., Chen L., Sauer U., Vitkup D., Computational Prediction and Experimental Verification of the Gene Encoding the NAD+/NADP+-Dependent Succinate Semialdehyde Dehydrogenase in Escherichia coli, 10.1128/jb.01027-07
- Kim K.-S., Pelton J. G., Inwood W. B., Andersen U., Kustu S., Wemmer D. E., The Rut Pathway for Pyrimidine Degradation: Novel Chemistry and Toxicity Problems, 10.1128/jb.00201-10
- Matsunaga Toshiyuki, Shintani Shinichi, Hara Akira, Multiplicity of Mammalian Reductases for Xenobiotic Carbonyl Compounds, 10.2133/dmpk.21.1
- Stefani M., Taddei N., Ramponi G., Insights into acylphosphatase structure and catalytic mechanism : , 10.1007/pl00000585
- Harms N, Ras J, Reijnders W N, van Spanning R J, Stouthamer A H, S-formylglutathione hydrolase of Paracoccus denitrificans is homologous to human esterase D: a universal pathway for formaldehyde detoxification?, 10.1128/jb.178.21.6296-6299.1996
- KATO Nobuo, YAMAGAMI Tomohide, SHIMAO Masayuki, SAKAZAWA Chikahiro, Formaldehyde dismutase, a novel NAD-binding oxidoreductase from Pseudomonas putida F61, 10.1111/j.1432-1033.1986.tb09548.x
- Murdanoto A.P., Appl. Environ. Microbiol., 63, 1715 (1997)
Bibliographic reference |
Linster, Carole L ; Van Schaftingen, Emile ; Hanson, Andrew D. Metabolite damage and its repair or pre-emption.. In: Nature Chemical Biology, Vol. 9, no.2, p. 72-80 (2013) |
Permanent URL |
http://hdl.handle.net/2078.1/123557 |