V

Viswanatham Katta

Intarcia Therapeutics (United States)

Publishes on Mass Spectrometry Techniques and Applications, Protein purification and stability, Advanced Proteomics Techniques and Applications. 60 papers and 6k citations.

60Publications
6kTotal Citations

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Top publicationsby citations

Probing conformational changes in proteins by mass spectrometry
Swapan K. Chowdhury, Viswanatham Katta, Brian T. Chait|Journal of the American Chemical Society|1990
Cited by 638

ADVERTISEMENT RETURN TO ISSUEPREVArticleNEXTProbing conformational changes in proteins by mass spectrometrySwapan K. Chowdhury, Viswanatham Katta, and Brian T. ChaitCite this: J. Am. Chem. Soc. 1990, 112, 24, 9012–9013Publication Date (Print):November 1, 1990Publication History Published online1 May 2002Published inissue 1 November 1990https://pubs.acs.org/doi/10.1021/ja00180a074https://doi.org/10.1021/ja00180a074research-articleACS PublicationsRequest reuse permissionsArticle Views1741Altmetric-Citations558LEARN 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

Observation of the heme-globin complex in native myoglobin by electrospray-ionization mass spectrometry
Viswanatham Katta, Brian T. Chait|Journal of the American Chemical Society|1991
Cited by 462

ADVERTISEMENT RETURN TO ISSUEPREVArticleNEXTObservation of the heme-globin complex in native myoglobin by electrospray-ionization mass spectrometryViswanatham Katta and Brian T. ChaitCite this: J. Am. Chem. Soc. 1991, 113, 22, 8534–8535Publication Date (Print):October 1, 1991Publication History Published online1 May 2002Published inissue 1 October 1991https://pubs.acs.org/doi/10.1021/ja00022a058https://doi.org/10.1021/ja00022a058research-articleACS PublicationsRequest reuse permissionsArticle Views1674Altmetric-Citations404LEARN 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

Conformational changes in proteins probed by hydrogen‐exchange electrospray‐ionization mass spectrometry
Viswanatham Katta, Brian T. Chait, Steven A. Carr|Rapid Communications in Mass Spectrometry|1991
Cited by 449

Hydrogen-exchange electrospray-ionization mass spectrometry is demonstrated to be an effective new method for probing conformational changes of proteins in solutions. The method is based on the mass spectrometric measurement of the extent of hydrogen/deuterium exchange that occurs in different protein conformers over defined periods of time. Results are presented in which hydrogen-exchange electrospray-ionization mass spectrometry is used to probe conformational changes in bovine ubiquitin induced by the addition of methanol to aqueous acidic solutions of the protein.