Mass Spectrometry-Based Detection and Assignment of Protein Posttranslational Modifications

Sophia Doll; Alma L. Burlingame

doi:10.1021/cb500904b

journal article Dec 26, 2014

Mass Spectrometry-Based Detection and Assignment of Protein Posttranslational Modifications

Sophia Doll Alma L. Burlingame

ACS Chemical Biology Vol. 10 No. 1 pp. 63-71 · American Chemical Society (ACS)

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References

99

[1]

Finishing the euchromatic sequence of the human genome

Nature 2004 10.1038/nature03001

[2]

Modification-specific proteomics: characterization of post-translational modifications by mass spectrometry

Ole Nørregaard Jensen

Current Opinion in Chemical Biology 2004 10.1016/j.cbpa.2003.12.009

[3]

RNA-Seq: a revolutionary tool for transcriptomics

Zhong Wang, Mark Gerstein, Michael Snyder

Nature Reviews Genetics 2009 10.1038/nrg2484

[4]

Walsh, C. T. (2006) Posttranslational Modification of Proteins: Expanding Nature’s Inventory,1st ed., pp1–490,Roberts and Company, Publishers,Greenwood Village, CO.

[5]

Hebert A. S. Mol. Cell. Proteomics (2014) 10.1074/mcp.m113.034769

[6]

Imamura H. J. Proteome Res. (2014) 10.1021/pr500319y

[7]

Masuda T. Anal. Chem. (2011) 10.1021/ac201093g

[8]

Trinidad J. C. Mol. Cell. Proteomics (2012) 10.1074/mcp.o112.018366

[9]

Quantitative Phosphoproteomics Reveals Widespread Full Phosphorylation Site Occupancy During Mitosis

Jesper V. Olsen, Michiel Vermeulen, Anna Santamaria et al.

Science Signaling 10.1126/scisignal.2000475

[10]

Lysine Acetylation Targets Protein Complexes and Co-Regulates Major Cellular Functions

Chunaram Choudhary, Chanchal Kumar, Florian Gnad et al.

Science 2009 10.1126/science.1175371

[11]

Zielinska D. F. Mol. Cell (2012) 10.1016/j.molcel.2012.04.031

[12]

Systematic and Quantitative Assessment of the Ubiquitin-Modified Proteome

Woong Kim, Eric J. Bennett, Edward L. Huttlin et al.

Molecular Cell 2011 10.1016/j.molcel.2011.08.025

[13]

Hendriks I. A. Nat. Struct. Mol. Biol. (2014) 10.1038/nsmb.2890

[14]

Eliuk S. M. Mol. Cell. Proteomics (2010) 10.1074/mcp.m900569-mcp200

[15]

Syka J. E. P. Proc. Natl. Acad. Sci. U.S.A. (2004) 10.1073/pnas.0402700101

[16]

Jünger M. A. Wiley Interdiscip. Rev. Dev. Biol. (2014) 10.1002/wdev.121

[17]

Myers S. A. Proteomics (2013) 10.1002/pmic.201200332

[18]

Ramström M. Eur. J. Mass Spectrom. (2011) 10.1255/ejms.1149

[19]

Moremen K. W. Nat. Rev. Mol. Cell Biol. (2012) 10.1038/nrm3383

[20]

Han X. Mass Spectrom. Rev. (2012) 10.1002/mas.20342

[21]

Trypsin Cleaves Exclusively C-terminal to Arginine and Lysine Residues

Jesper V. Olsen, Shao-En Ong, Matthias Mann

Molecular & Cellular Proteomics 2004 10.1074/mcp.t400003-mcp200

[22]

Gilmore J. M. Anal. Bioanal. Chem. (2012) 10.1007/s00216-011-5466-5

[23]

www.phosphosite.org.

[24]

Gruhler A. Mol. Cell. Proteomics (2005) 10.1074/mcp.m400219-mcp200

[25]

Pinkse M. W. H. Anal. Chem. (2004) 10.1021/ac0498617

[26]

Schmidt A. Mol. Cell. Proteomics (2014) 10.1074/mcp.m113.032292

[27]

Engholm-Keller K. Proteomics (2013) 10.1002/pmic.201200484

[28]

Thingholm T. E. Mol. Cell. Proteomics (2008) 10.1074/mcp.m700362-mcp200

[29]

Larsen M. R. Mol. Cell. Proteomics (2004) 10.1074/mcp.m300105-mcp200

[30]

Zhou H. Mol. Cell. Proteomics (2011)

[31]

Svane S. Angew. Chem., Int. Ed. Engl. (2012) 10.1002/anie.201108481

[32]

Global, In Vivo, and Site-Specific Phosphorylation Dynamics in Signaling Networks

Jesper V. Olsen, Blagoy Blagoev, Florian Gnad et al.

Cell 2006 10.1016/j.cell.2006.09.026

[33]

Rush J. Nat. Biotechnol. (2005) 10.1038/nbt1046

[34]

Pighi C. Cell. Oncol. (Dordr.) (2011) 10.1007/s13402-011-0019-7

[35]

Udeshi N. D. Mol. Cell. Proteomics (2013) 10.1074/mcp.o112.027094

[36]

Carlson S. M. J. Mol. Biol. (2014) 10.1016/j.jmb.2014.04.024

[37]

Yoshihara H. A. I. Bioorg. Med. Chem. Lett. (2008) 10.1016/j.bmcl.2008.08.044

[38]

Wiita A. P. Methods Enzymol. (2014) 10.1016/b978-0-12-417158-9.00013-3

[39]

Meyer J. G. Mol. Cell. Proteomics (2014) 10.1074/mcp.m113.034710

[40]

Mertins P. Nat. Methods (2013) 10.1038/nmeth.2518

[41]

Christophorou M. A. Nature (2014) 10.1038/nature12942

[42]

Deeg M. A. Methods Enzymol. (1995) 10.1016/0076-6879(95)50101-0

[43]

Qu Z. J. Proteome Res. (2014) 10.1021/pr401179v

[44]

Ge Y. Proc. Natl. Acad. Sci. U.S.A. (2009) 10.1073/pnas.0813369106

[45]

Boyne M. T. J. Proteome Res. (2006) 10.1021/pr050269n

[46]

Zhang H. Circ.: Cardiovasc. Genet. (2011)

[47]

Guan S. Mol. Cell. Proteomics (2010) 10.1074/mcp.m900431-mcp200

[48]

Fisk J. C. Mol. Cell. Proteomics (2013) 10.1074/mcp.m112.022533

[49]

Zhang J. J. Am. Soc. Mass Spectrom. (2010) 10.1016/j.jasms.2010.02.005

[50]

Fragmentation pathways of protonated peptides

Béla Paizs, Sándor Suhai

Mass Spectrometry Reviews 2005 10.1002/mas.20024

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Details

Published: Dec 26, 2014
Vol/Issue: 10(1)
Pages: 63-71
License: View

Authors

S

Sophia Doll

Department of Pharmaceutical Chemistry, University of California, San Francisco, California 94158-2517, United States; Department of Proteomics and Signal Transduction, Max Planck Institute of Biochemistry, Martinsried, 82152, Germany

A

Alma L. Burlingame

Department of Pharmaceutical Chemistry, University of California, San Francisco, California 94158-2517, United States

Funding

National Institute of General Medical Sciences Award: 8P41GM103481

Dr. Miriam and Sheldon G. Adelson Medical Research Foundation

Cite This Article

Sophia Doll, Alma L. Burlingame (2014). Mass Spectrometry-Based Detection and Assignment of Protein Posttranslational Modifications. ACS Chemical Biology, 10(1), 63-71. https://doi.org/10.1021/cb500904b

Mass Spectrometry-Based Detection and Assignment of Protein Posttranslational Modifications

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