Channels at the catalytic site of glycogen phosphorylase b: binding and kinetic studies with the .beta.-glycosidase inhibitor D-gluconohydroximo-1,5-lactone N-phenylurethane
1988; American Chemical Society; Volume: 27; Issue: 18 Linguagem: Inglês
10.1021/bi00418a014
ISSN1943-295X
AutoresDavid Barford, John W. R. Schwabe, N.G. Oikonomakos, K. Ravi Acharya, János Hajdu, Anastassios C. Papageorgiou, Jennifer L. Martin, J. C. A. Knott, Andrea Vasella, L.N. Johnson,
Tópico(s)Enzyme Structure and Function
ResumoADVERTISEMENT RETURN TO ISSUEPREVArticleNEXTChannels at the catalytic site of glycogen phosphorylase b: binding and kinetic studies with the .beta.-glycosidase inhibitor D-gluconohydroximo-1,5-lactone N-phenylurethaneD. Barford, J. W. R. Schwabe, N. G. Oikonomakos, K. R. Acharya, J. Hajdu, A. C. Papageorgiou, J. L. Martin, J. C. A. Knott, A. Vasella, and L. N. JohnsonCite this: Biochemistry 1988, 27, 18, 6733–6741Publication Date (Print):September 6, 1988Publication History Published online1 May 2002Published inissue 6 September 1988https://pubs.acs.org/doi/10.1021/bi00418a014https://doi.org/10.1021/bi00418a014research-articleACS PublicationsRequest reuse permissionsArticle Views73Altmetric-Citations26LEARN 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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