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C-terminomics: targeted analysis of natural and posttranslationally modified protein and peptide C-termini

Sebastian Tanco (UGent) , Kris Gevaert (UGent) and Petra Van Damme (UGent)
(2015) PROTEOMICS. 15(5-6). p.903-914
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Abstract
The C-terminus (where C is carboxyl) of a protein can serve as a recognition signature for a variety of biological processes, including protein trafficking and protein complex formation. Hence, the identity of the in vivo protein C-termini provides valuable information about biological processes. Analysis of protein C-termini is also crucial for the study of C-terminal PTMs, particularly for monitoring proteolytic processing by endopeptidases and carboxypeptidases. Although technical difficulties have limited the study of C-termini, a range of technologies have been proposed in the last couple of years. Here, we review the current proteomics technologies for C-terminal analysis, with a focus on the biological information that can be derived from C-terminomics studies.
Keywords
CARBOXYPEPTIDASE-Y, IDENTIFICATION, N-TERMINI, POSITIONAL PROTEOMICS, BIOCHEMICAL-CHARACTERIZATION, ACETIC-ANHYDRIDE, SEQUENCE-ANALYSIS, SUBSTRATE-SPECIFICITY, ALPHA-CARBOXYL GROUP, MALDI MASS-SPECTROMETRY, Technology, PTMs, Degradomics, C-terminomics, C-terminal sequencing

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Citation

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Chicago
Tanco, Sebastian, Kris Gevaert, and Petra Van Damme. 2015. “C-terminomics: Targeted Analysis of Natural and Posttranslationally Modified Protein and Peptide C-termini.” Proteomics 15 (5-6): 903–914.
APA
Tanco, S., Gevaert, K., & Van Damme, P. (2015). C-terminomics: targeted analysis of natural and posttranslationally modified protein and peptide C-termini. PROTEOMICS, 15(5-6), 903–914.
Vancouver
1.
Tanco S, Gevaert K, Van Damme P. C-terminomics: targeted analysis of natural and posttranslationally modified protein and peptide C-termini. PROTEOMICS. 2015;15(5-6):903–14.
MLA
Tanco, Sebastian, Kris Gevaert, and Petra Van Damme. “C-terminomics: Targeted Analysis of Natural and Posttranslationally Modified Protein and Peptide C-termini.” PROTEOMICS 15.5-6 (2015): 903–914. Print.
@article{6981318,
  abstract     = {The C-terminus (where C is carboxyl) of a protein can serve as a recognition signature for a variety of biological processes, including protein trafficking and protein complex formation. Hence, the identity of the in vivo protein C-termini provides valuable information about biological processes. Analysis of protein C-termini is also crucial for the study of C-terminal PTMs, particularly for monitoring proteolytic processing by endopeptidases and carboxypeptidases. Although technical difficulties have limited the study of C-termini, a range of technologies have been proposed in the last couple of years. Here, we review the current proteomics technologies for C-terminal analysis, with a focus on the biological information that can be derived from C-terminomics studies.},
  author       = {Tanco, Sebastian and Gevaert, Kris and Van Damme, Petra},
  issn         = {1615-9853},
  journal      = {PROTEOMICS},
  keywords     = {CARBOXYPEPTIDASE-Y,IDENTIFICATION,N-TERMINI,POSITIONAL PROTEOMICS,BIOCHEMICAL-CHARACTERIZATION,ACETIC-ANHYDRIDE,SEQUENCE-ANALYSIS,SUBSTRATE-SPECIFICITY,ALPHA-CARBOXYL GROUP,MALDI MASS-SPECTROMETRY,Technology,PTMs,Degradomics,C-terminomics,C-terminal sequencing},
  language     = {eng},
  number       = {5-6},
  pages        = {903--914},
  title        = {C-terminomics: targeted analysis of natural and posttranslationally modified protein and peptide C-termini},
  url          = {http://dx.doi.org/10.1002/pmic.201400301},
  volume       = {15},
  year         = {2015},
}

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