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A new functional, chemical proteomics technology to identify purine nucleotide binding sites in complex proteomes

Xavier Hanoulle, Jozef Van Damme UGent, An Staes UGent, Lennart Martens UGent, Marc Goethals UGent, Joël Vandekerckhove UGent and Kris Gevaert UGent (2006) JOURNAL OF PROTEOME RESEARCH. 5(12). p.3438-3445
abstract
Adenine nucleotides are small, abundant molecules that bind numerous proteins involved in pivotal cellular processes. These nucleotides are co-factors or substrates for enzymes, regulators of protein function, or structural binding motifs. The identification of nucleotide-binding sites on a proteome-wide scale is tempting in view of the high number of nucleotide-binding proteins, their large in vivo concentration differences, and the various functions they exert. Here, we report on a functional, chemical, gel-free proteomics technology that allows the identification of protein adenine nucleotide-binding site(s) in cell lysates. Our technology uses a synthetic ATP analogue, 5'-rho-fluorosulfonylbenzoylad-enosine (FSBA), as an affinity/activity-based probe for nucleotide-binding sites. When applied on a cellular level, 185 different FSBA-labeled sites in a human Jurkat cell lysate were identified. Functional and structural aspects of the use of FSBA on a proteome-wide scale are discussed.
Please use this url to cite or link to this publication:
author
organization
year
type
journalArticle (original)
publication status
published
subject
keyword
ADENOSINE, 5 '-p-fluorosulfonylbenzoyladenosine (FSBA), MASS-SPECTROMETRY, functional proteomics, affinity/activity-based probe, gel-free proteomics, diagonal chromatography, DEPENDENT PROTEIN-KINASE, ACTIVITY-BASED PROBES, TYROSINE PHOSPHORYLATION, IDENTIFICATION, ATP, CHROMATOGRAPHY, INACTIVATION, INHIBITOR
journal title
JOURNAL OF PROTEOME RESEARCH
J. Proteome Res.
volume
5
issue
12
pages
3438 - 3445
Web of Science type
Article
Web of Science id
000242427800023
JCR category
BIOCHEMICAL RESEARCH METHODS
JCR impact factor
5.151 (2006)
JCR rank
7/56 (2006)
JCR quartile
1 (2006)
ISSN
1535-3893
DOI
10.1021/pr060313e
language
English
UGent publication?
yes
classification
A1
copyright statement
I have transferred the copyright for this publication to the publisher
id
356960
handle
http://hdl.handle.net/1854/LU-356960
date created
2007-03-20 09:28:00
date last changed
2012-03-02 17:01:49
@article{356960,
  abstract     = {Adenine nucleotides are small, abundant molecules that bind numerous proteins involved in pivotal cellular processes. These nucleotides are co-factors or substrates for enzymes, regulators of protein function, or structural binding motifs. The identification of nucleotide-binding sites on a proteome-wide scale is tempting in view of the high number of nucleotide-binding proteins, their large in vivo concentration differences, and the various functions they exert. Here, we report on a functional, chemical, gel-free proteomics technology that allows the identification of protein adenine nucleotide-binding site(s) in cell lysates. Our technology uses a synthetic ATP analogue, 5'-rho-fluorosulfonylbenzoylad-enosine (FSBA), as an affinity/activity-based probe for nucleotide-binding sites. When applied on a cellular level, 185 different FSBA-labeled sites in a human Jurkat cell lysate were identified. Functional and structural aspects of the use of FSBA on a proteome-wide scale are discussed.},
  author       = {Hanoulle, Xavier and Van Damme, Jozef and Staes, An and Martens, Lennart and Goethals, Marc and Vandekerckhove, Jo{\"e}l and Gevaert, Kris},
  issn         = {1535-3893},
  journal      = {JOURNAL OF PROTEOME RESEARCH},
  keyword      = {ADENOSINE,5 '-p-fluorosulfonylbenzoyladenosine (FSBA),MASS-SPECTROMETRY,functional proteomics,affinity/activity-based probe,gel-free proteomics,diagonal chromatography,DEPENDENT PROTEIN-KINASE,ACTIVITY-BASED PROBES,TYROSINE PHOSPHORYLATION,IDENTIFICATION,ATP,CHROMATOGRAPHY,INACTIVATION,INHIBITOR},
  language     = {eng},
  number       = {12},
  pages        = {3438--3445},
  title        = {A new functional, chemical proteomics technology to identify purine nucleotide binding sites in complex proteomes},
  url          = {http://dx.doi.org/10.1021/pr060313e},
  volume       = {5},
  year         = {2006},
}

Chicago
Hanoulle, Xavier, Jozef Van Damme, An Staes, Lennart Martens, Marc Goethals, Joël Vandekerckhove, and Kris Gevaert. 2006. “A New Functional, Chemical Proteomics Technology to Identify Purine Nucleotide Binding Sites in Complex Proteomes.” Journal of Proteome Research 5 (12): 3438–3445.
APA
Hanoulle, X., Van Damme, J., Staes, A., Martens, L., Goethals, M., Vandekerckhove, J., & Gevaert, K. (2006). A new functional, chemical proteomics technology to identify purine nucleotide binding sites in complex proteomes. JOURNAL OF PROTEOME RESEARCH, 5(12), 3438–3445.
Vancouver
1.
Hanoulle X, Van Damme J, Staes A, Martens L, Goethals M, Vandekerckhove J, et al. A new functional, chemical proteomics technology to identify purine nucleotide binding sites in complex proteomes. JOURNAL OF PROTEOME RESEARCH. 2006;5(12):3438–45.
MLA
Hanoulle, Xavier, Jozef Van Damme, An Staes, et al. “A New Functional, Chemical Proteomics Technology to Identify Purine Nucleotide Binding Sites in Complex Proteomes.” JOURNAL OF PROTEOME RESEARCH 5.12 (2006): 3438–3445. Print.