Advertisement
MCP
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
 QUICK SEARCH:   [advanced]


     


Originally published In Press as doi:10.1074/mcp.M500064-MCP200 on April 28, 2005.
This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Supplemental Data
Right arrow All Versions of this Article:
M500064-MCP200v1
4/7/1002    most recent
Right arrow Submit a response
Right arrow Alert me when this article is cited
Right arrow Alert me when eLetters are posted
Right arrow Alert me if a correction is posted
Right arrow Citation Map
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrowRequest Permissions
Right arrow Glossary
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Roth, M. J.
Right arrow Articles by Kelleher, N. L.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Roth, M. J.
Right arrow Articles by Kelleher, N. L.
Social Bookmarking
 Add to CiteULike   Add to Complore   Add to Connotea   Add to Del.icio.us   Add to Digg   Add to Reddit   Add to Technorati  
What's this?

Molecular & Cellular Proteomics 4:1002-1008, 2005.
© 2005 by The American Society for Biochemistry and Molecular Biology, Inc.


Research

Precise and Parallel Characterization of Coding Polymorphisms, Alternative Splicing, and Modifications in Human Proteins by Mass Spectrometry*,S

Michael J. Roth, Andrew J. Forbes, Michael T. Boyne, II, Yong-Bin Kim, Dana E. Robinson and Neil L. Kelleher{ddagger}

Department of Chemistry, University of Illinois Urbana-Champaign, Urbana, Illinois 61801

The human proteome is a highly complex extension of the genome wherein a single gene often produces distinct protein forms due to alternative splicing, RNA editing, polymorphisms, and posttranslational modifications. Such biological variation compounded by the high sequence identity within gene families currently overwhelms the complete and routine characterization of mammalian proteins by MS. A new data base of human proteins (and their possible variants) was created and searched using tandem mass spectrometric data from intact proteins. This first application of top down MS/MS to wild-type human proteins demonstrates both gene-specific identification and the unambiguous characterization of multifaceted mass shifts ({Delta}m values). Such {Delta}m values found from the precise identification of 45 protein forms from HeLa cells reveal 34 coding single nucleotide polymorphisms, two protein forms from alternative splicing, and 12 diverse modifications (not including simple N-terminal processing), including a previously unknown phosphorylation at 10% occupancy. Automated protein identification was achieved with a median expectation value of 10–13 and often occurred simultaneously with dissection of diverse sources of protein variability as they occur in combination. Top down MS therefore has a bright future for enabling precise annotation of gene products expressed from the human genome by non-mass spectrometrists.


{ddagger} To whom correspondence should be addressed: Dept. of Chemistry, University of Illinois Urbana-Champaign, 39 RAL, 600 S. Matthews, Urbana, IL 61801. E-mail: Kelleher{at}scs.uiuc.edu


Add to CiteULike CiteULike   Add to Complore Complore   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us   Add to Digg Digg   Add to Reddit Reddit   Add to Technorati Technorati    What's this?


This article has been cited by other articles:


Home page
Mol. Cell. ProteomicsHome page
N. M. Karabacak, L. Li, A. Tiwari, L. J. Hayward, P. Hong, M. L. Easterling, and J. N. Agar
Sensitive and Specific Identification of Wild Type and Variant Proteins from 8 to 669 kDa Using Top-down Mass Spectrometry
Mol. Cell. Proteomics, April 1, 2009; 8(4): 846 - 856.
[Abstract] [Full Text] [PDF]


Home page
Proc. Natl. Acad. Sci. USAHome page
M. Mann and N. L. Kelleher
Mass Spectrometry Special Feature: Precision proteomics: The case for high resolution and high mass accuracy
PNAS, November 25, 2008; 105(47): 18132 - 18138.
[Abstract] [Full Text] [PDF]


Home page
J. Nutr.Home page
J. Astle, J. T. Ferguson, J. B. German, G. G. Harrigan, N. L. Kelleher, T. Kodadek, B. A. Parks, M. J. Roth, K. W. Singletary, C. D. Wenger, et al.
Characterization of Proteomic and Metabolomic Responses to Dietary Factors and Supplements
J. Nutr., December 1, 2007; 137(12): 2787 - 2793.
[Abstract] [Full Text] [PDF]


Home page
Mol. Cell. ProteomicsHome page
J. J. Pesavento, B. A. Garcia, J. A. Streeky, N. L. Kelleher, and C. A. Mizzen
Mild Performic Acid Oxidation Enhances Chromatographic and Top Down Mass Spectrometric Analyses of Histones
Mol. Cell. Proteomics, September 1, 2007; 6(9): 1510 - 1526.
[Abstract] [Full Text] [PDF]


Home page
Nucleic Acids ResHome page
L. Zamdborg, R. D. LeDuc, K. J. Glowacz, Y.-B. Kim, V. Viswanathan, I. T. Spaulding, B. P. Early, E. J. Bluhm, S. Babai, and N. L. Kelleher
ProSight PTM 2.0: improved protein identification and characterization for top down mass spectrometry
Nucleic Acids Res., July 13, 2007; 35(suppl_2): W701 - W706.
[Abstract] [Full Text] [PDF]


Home page
Genome ResHome page
S. Tanner, Z. Shen, J. Ng, L. Florea, R. Guigo, S. P. Briggs, and V. Bafna
Improving gene annotation using peptide mass spectrometry
Genome Res., February 1, 2007; 17(2): 231 - 239.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
I. Paarmann, B. Schmitt, B. Meyer, M. Karas, and H. Betz
Mass Spectrometric Analysis of Glycine Receptor-associated Gephyrin Splice Variants
J. Biol. Chem., November 17, 2006; 281(46): 34918 - 34925.
[Abstract] [Full Text] [PDF]


Home page
Mol. Cell. ProteomicsHome page
S. M. Patrie, J. T. Ferguson, D. E. Robinson, D. Whipple, M. Rother, W. W. Metcalf, and N. L. Kelleher
Top Down Mass Spectrometry of <60-kDa Proteins from Methanosarcina acetivorans Using Quadrupole FTMS with Automated Octopole Collisionally Activated Dissociation
Mol. Cell. Proteomics, January 1, 2006; 5(1): 14 - 25.
[Abstract] [Full Text] [PDF]




HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
 All ASBMB Journals   Journal of Biological Chemistry 
 Journal of Lipid Research   ASBMB Today 
Copyright © 2005 by the American Society for Biochemistry and Molecular Biology.
Advertisement
spacer
Advertisement
Advertisement