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Deamidation of human proteins

Robinson, N. E. and Robinson, A. B. (2001) Deamidation of human proteins. Proceedings of the National Academy of Sciences of the United States of America, 98 (22). pp. 12409-12413. ISSN 0027-8424. https://resolver.caltech.edu/CaltechAUTHORS:20141119-132604985

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Abstract

Deamidation of asparaginyl and glutaminyl residues causes time-dependent changes in charge and conformation of peptides and proteins. Quantitative and experimentally verified predictive calculations of the deamidation rates of 1,371 asparaginyl residues in a representative collection of 126 human proteins have been performed. These rates suggest that deamidation is a biologically relevant phenomenon in a remarkably large percentage of human proteins.


Item Type:Article
Related URLs:
URLURL TypeDescription
http://dx.doi.org/10.1073/pnas.221463198DOIArticle
http://www.pnas.org/content/98/22/12409PublisherArticle
Additional Information:© 2001 National Academy of Sciences. Communicated by Frederick Seitz, The Rockefeller University, New York, NY, August 31, 2001 (received for review May 8, 2001). Published ahead of print October 16, 2001. We thank Professor and Mrs. R. B. Merrifield for advice and encouragement, and the Kinsman foundation and other donors to the Oregon Institute of Science and Medicine for financial support. Additional information is available at www.deamidation.org. The publication costs of this article were defrayed in part by page charge payment. This article must therefore be hereby marked “advertisement” in accordance with 18 U.S.C. §1734 solely to indicate this fact.
Funders:
Funding AgencyGrant Number
Kinsman FoundationUNSPECIFIED
Oregon Institute of Science and MedicineUNSPECIFIED
Subject Keywords:in vivo deamidation; asparaginyl residues
Issue or Number:22
Record Number:CaltechAUTHORS:20141119-132604985
Persistent URL:https://resolver.caltech.edu/CaltechAUTHORS:20141119-132604985
Official Citation:Robinson, N. E., & Robinson, A. B. (2001). Deamidation of human proteins. Proceedings of the National Academy of Sciences, 98(22), 12409-12413. doi: 10.1073/pnas.221463198
Usage Policy:No commercial reproduction, distribution, display or performance rights in this work are provided.
ID Code:51973
Collection:CaltechAUTHORS
Deposited By: Jason Perez
Deposited On:19 Nov 2014 22:19
Last Modified:03 Oct 2019 07:38

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