Title: Redox modulation of glucose‐6‐P dehydrogenase in <i>Anacystis nidulans</i> and its ‘uncoupling’ by phage infection
Abstract: FEBS LettersVolume 126, Issue 1 p. 85-88 Full-length articleFree Access Redox modulation of glucose-6-P dehydrogenase in Anacystis nidulans and its ‘uncoupling’ by phage infection Csaba Cséke, Csaba Cséke Institute of Plant Physiology, Biological Research Center, Hungarian Academy of Sciences, POB 521, 6701 Szeged, HungarySearch for more papers by this authorÁrpád Balogh, Árpád Balogh Institute of Plant Physiology, Biological Research Center, Hungarian Academy of Sciences, POB 521, 6701 Szeged, HungarySearch for more papers by this authorGábor L. Farkas, Gábor L. Farkas Institute of Plant Physiology, Biological Research Center, Hungarian Academy of Sciences, POB 521, 6701 Szeged, HungarySearch for more papers by this author Csaba Cséke, Csaba Cséke Institute of Plant Physiology, Biological Research Center, Hungarian Academy of Sciences, POB 521, 6701 Szeged, HungarySearch for more papers by this authorÁrpád Balogh, Árpád Balogh Institute of Plant Physiology, Biological Research Center, Hungarian Academy of Sciences, POB 521, 6701 Szeged, HungarySearch for more papers by this authorGábor L. Farkas, Gábor L. Farkas Institute of Plant Physiology, Biological Research Center, Hungarian Academy of Sciences, POB 521, 6701 Szeged, HungarySearch for more papers by this author First published: April 06, 1981 https://doi.org/10.1016/0014-5793(81)81039-3Citations: 29AboutReferencesRelatedInformationPDFPDF ToolsRequest permissionExport citationAdd to favoritesTrack citation ShareShare Give accessShare full text accessClose modalShare full-text accessPlease review our Terms and Conditions of Use and check box below to share full-text version of article.I have read and accept the Wiley Online Library Terms and Conditions of UseShareable LinkUse the link below to share a full-text version of this article with your friends and colleagues. Learn more.Copy URL References 1 Á. Balogh, G. Borbély, Cs. Cséke, J. Udvardy, G.L. Farkas, FEBS Lett., 105, (1979), 158– 162. 2 S.S. Cohen, Nature, 168, (1951), 746– 747. 3 H.R. Loeb, S.S. Cohen, J. Biol. Chem., 234, (1959), 364– 369. 4 E.M. Wright, H.Z. Sable, J.L. Bailey, J. Bacteriol., 81, (1961), 845– 851. 5 H.R. Levy, Adv. Enzymol., 48, (1979), 97– 192. 6 R.S. Safferman, T.O. Diener, P.R. Desjardins, M.E. Morris, Virology, 47, (1972), 105– 113. 7 J. Udvardy, B. Sivók, G. Borbély, G.L. Farkas, J. Bacteriol., 126, (1976), 630– 633. 8 G. Borbély, M. Kölcsei, G.L. Farkas, Mol. Biol. Rep., 3, (1976), 139– 142. 9 G. Borbély, Cs. Kari, A. Gulyás, G.L. Farkas, J. Bacteriol., 144, (1980), 859– 864. 10 Cs. Cséke, G.L. Farkas, J. Bacteriol., 137, (1979), 667– 669. 11 J. Biggins, J. Bacteriol., 99, (1969), 570– 575. 12 F. Schaeffer, R.Y. Stanier, Arch. Microbiol., 116, (1978), 9– 19. 13 L.E. Anderson, M. Gibbs E. Latzko Photosynthesis II. Photosynthetic Carbon Metabolism and Related Processes (1979), Springer Berlin, New York 271– 281. 14 B.B. Buchanan, Annu. Rev. Plant. Physiol., 31, (1980), 341– 374. 15 R.A. Wolosiuk, B.B. Buchanan, N.A. Crawford, FEBS Lett., 81, (1977), 253– 258. 16 L. Thelander, P. Reichard, Annu. Rev. Biochem., 48, (1979), 133– 158. 17 J. Glenn, D.H. Duckworth, Arch. Biochem. Biophys., 201, (1980), 576– 585. Citing Literature Volume126, Issue1April 06, 1981Pages 85-88 ReferencesRelatedInformation
Publication Year: 1981
Publication Date: 1981-04-06
Language: en
Type: article
Indexed In: ['crossref', 'pubmed']
Access and Citation
Cited By Count: 31
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