The DOI matches its Crossref record; 15 of the 15 references it cites were found in a registry or an index.
Flavin coenzymes: at the crossroads of biological redox chemistry
Abstract
ADVERTISEMENT RETURN TO ISSUEPREVArticleNEXTFlavin coenzymes: at the crossroads of biological redox chemistryChristopher WalshCite this: Acc. Chem. Res. 1980, 13, 5, 148–155Publication Date (Print):May 1, 1980Publication History Published online1 May 2002Published inissue 1 May 1980https://pubs.acs.org/doi/10.1021/ar50149a004https://doi.org/10.1021/ar50149a004research-articleACS PublicationsRequest reuse permissionsArticle Views1812Altmetric-Citations360LEARN ABOUT THESE METRICSArticle Views are the COUNTER-compliant sum of full text article downloads since November 2008 (both PDF and HTML) across all institutions and individuals. These metrics are regularly updated to reflect usage leading up to the last few days.Citations are the number of other articles citing this article, calculated by Crossref and updated daily. Find more information about Crossref citation counts.The Altmetric Attention Score is a quantitative measure of the attention that a research article has received online. Clicking on the donut icon will load a page at altmetric.com with additional details about the score and the social media presence for the given article. Find more information on the Altmetric Attention Score and how the score is calculated. Share Add toView InAdd Full Text with ReferenceAdd Description ExportRISCitationCitation and abstractCitation and referencesMore Options Share onFacebookTwitterWechatLinked InRedditEmail Other access optionsGet e-Alertsclose Get e-Alerts
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Citations
Cites
Abeles, R. H., & Maycock, A. L. (1976) · Accounts of Chemical Research · doi:10.1021/ar50105a001 · Cited by 369
Proposed structure for coenzyme F420 from methanobacterium
Eirich, L. D., Vogels, G. D., & Wolfe, R. S. (1978) · Biochemistry · doi:10.1021/bi00615a002 · Cited by 343
Walsh, C. (1980) · Accounts of Chemical Research · Cited by 254
Self-citationHastings, J. W., Balny, C., Peuch, C. L., & Douzou, P. (1973) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.70.12.3468 · Cited by 194
Synthetic approaches to the active sites of iron-sulfur proteins
Holm, R. H. (1977) · Accounts of Chemical Research · doi:10.1021/ar50120a001 · Cited by 175
Porter, D. J. T., Voet, J. G., & Bright, H. J. (1973) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)43784-8 · Cited by 151
Kemal, C., & Bruice, T. C. (1976) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.73.4.995 · Cited by 145
Madyastha, K. M., Meehan, T. D., & Coscia, C. J. (1976) · Biochemistry · doi:10.1021/bi00650a023 · Cited by 145
Maycock, A. L., Abeles, R. H., Salach, J. I., & Singer, T. P. (1976) · Biochemistry · doi:10.1021/bi00646a018 · Cited by 123
ROSEOFLAVIN, A NEW ANTIMICROBIAL PIGMENT FROM STREPTOMYCES
Otani, S., Takatsu, M., Nakano, M., Kasai, S., Miura, R., & Matsui, K. (1974) · The Journal of Antibiotics · doi:10.7164/antibiotics.27.88 · Cited by 93
Cited by
Mechanisms of flavoprotein‐catalyzed reactions
GHISLA, S., & MASSEY, V. (1989) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1989.tb14688.x · Cited by 566
Non-innocent ligands in bioinorganic chemistry—An overview
Kaim, W., & Schwederski, B. (2010) · Coordination Chemistry Reviews · doi:10.1016/j.ccr.2010.01.009 · Cited by 564
Function and Structure of Complex II of the Respiratory Chain
Cecchini, G. (2003) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.72.121801.161700 · Cited by 556
The NADPH oxidase of professional phagocytes—prototype of the NOX electron transport chain systems
Cross, A. R., & Segal, A. W. (2004) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2004.03.008 · Cited by 489
Flavoenzymes: Versatile catalysts in biosynthetic pathways
Walsh, C. T., & Wencewicz, T. A. (2013) · Nat. Prod. Rep. · doi:10.1039/c2np20069d · Cited by 373
Self-citationZhu, X.-Q., Zhang, M.-T., Yu, A., Wang, C.-H., & Cheng, J.-P. (2008) · Journal of the American Chemical Society · doi:10.1021/ja075523m · Cited by 368
Correll, C. C., Batie, C. J., Ballou, D. P., & Ludwig, M. L. (1992) · Science · doi:10.1126/science.1280857 · Cited by 296
Photo, thermal and chemical degradation of riboflavin
Sheraz, M. A., Kazi, S. H., Ahmed, S., Anwar, Z., & Ahmad, I. (2014) · Beilstein Journal of Organic Chemistry · doi:10.3762/bjoc.10.208 · Cited by 275
Ultrafast Dynamics of Flavins in Five Redox States
Kao, Y.-T., Saxena, C., He, T.-F., Guo, L., Wang, L., Sancar, A., & Zhong, D. (2008) · Journal of the American Chemical Society · doi:10.1021/ja8045469 · Cited by 261
Photolyase: Dynamics and electron-transfer mechanisms of DNA repair
Zhang, M., Wang, L., & Zhong, D. (2017) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2017.08.007 · Cited by 115
Dynamics and mechanisms of DNA repair by photolyase
Liu, Z., Wang, L., & Zhong, D. (2015) · Physical Chemistry Chemical Physics · doi:10.1039/c4cp05286b · Cited by 86
Metadata
- Authors
- Walsh, C.
- Venue
- Accounts of Chemical Research
- Publisher
- American Chemical Society (ACS)
- Published
- 1980-05-01
- Volume
- 13
- Issue
- 5
- Pages
- 148-155
- ISSN
- 0001-4842 (ISSN-L)
- 1520-4898
- OpenAlex
- W2051090871
- Cited by
- 405
- References
- 15
- FWCI
- 14.88
- Type
- journal article
- Language
- en
- Open access
- closed
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