J

Jane E. Ladner

University of Essex

Publishes on Enzyme Structure and Function, RNA and protein synthesis mechanisms, Protein Structure and Dynamics. 91 papers and 4.7k citations.

91Publications
4.7kTotal Citations

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Influence of globin structure on the state of the heme. I. Human deoxyhemoglobin
M. F. Perutz, Jane E. Ladner, Sanford R. Simon et al.|Biochemistry|1974
Cited by 291

ADVERTISEMENT RETURN TO ISSUEPREVArticleNEXTInfluence of globin structure on the state of the heme. I. Human deoxyhemoglobinMax F. Perutz, Jane E. Ladner, Sanford R. Simon, and Chien HoCite this: Biochemistry 1974, 13, 10, 2163–2173Publication Date (Print):May 1, 1974Publication History Published online1 May 2002Published inissue 1 May 1974https://pubs.acs.org/doi/10.1021/bi00707a026https://doi.org/10.1021/bi00707a026research-articleACS PublicationsRequest reuse permissionsArticle Views563Altmetric-Citations225LEARN 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

Structure of yeast phenylalanine transfer RNA at 2.5 A resolution.
Jane E. Ladner, Anthony Abraham Jack, Jon D. Robertus et al.|Proceedings of the National Academy of Sciences|1975
Cited by 278Open Access

The x-ray analysis of the monoclinic form of yeast tRNAPhe has been taken to a resolution of 2.5 A by the method of isomorphous replacement. The model proposed at 3 A has been confirmed and extended to reveal additional features of the tertiary structure and of the stereochemistry. An extensive hydrogen bonding network is described involving specific interactions between bases and the ribose-phosphate backbone. The structure of a G-U base pair has been solved.