C
Christopher M. Overall
Researcher at University of British Columbia
Publications - 314
Citations - 31412
Christopher M. Overall is an academic researcher from University of British Columbia. The author has contributed to research in topics: Matrix metalloproteinase & Proteases. The author has an hindex of 90, co-authored 302 publications receiving 28860 citations. Previous affiliations of Christopher M. Overall include University of Toronto & Canadian Institutes of Health Research.
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Journal ArticleDOI
Research on the Human Proteome Reaches a Major Milestone: >90% of Predicted Human Proteins Now Credibly Detected, According to the HUPO Human Proteome Project.
Gilbert S. Omenn,Gilbert S. Omenn,Lydie Lane,Christopher M. Overall,Ileana M. Cristea,Fernando J. Corrales,Cecilia Lindskog,Young Ki Paik,Jennifer E. Van Eyk,Siqi Liu,Stephen R. Pennington,Michael Snyder,Mark S. Baker,Nuno Bandeira,Ruedi Aebersold,Robert L. Moritz,Eric W. Deutsch +16 more
TL;DR: According to the 2020 Metrics of the HUPO Human Proteome Project (HPP), expression has now been detected at the protein level for >90% of the 19,773 predicted proteins coded in the human genome.
Journal ArticleDOI
Traumatic brain injury induced matrix metalloproteinase2 cleaves CXCL12α (stromal cell derived factor 1α) and causes neurodegeneration.
P. M. Abdul-Muneer,Adriano Andrea Conte,Debanjan Haldar,Mathew Long,Rachel K. Patel,Vijayalakshmi Santhakumar,Christopher M. Overall,Bryan J. Pfister +7 more
TL;DR: It is hypothesized that TBI leads to MMP2 activation and cleavage of the N-terminal 4 amino acid residues of CXCL12α with generation of the highly neurotoxic fragment SDF-1(5-67), and the cleaved form of SDF leads to apoptotic cell death in neurons.
Journal ArticleDOI
Absolute proteomic quantification of the activity state of proteases and proteolytic cleavages using proteolytic signature peptides and isobaric tags.
TL;DR: A method for the absolute quantification of proteolysis that is compatible with existing quantitative proteomic applications and could be applied on a protein-family wide scale is described.
Book ChapterDOI
Identification of cellular MMP substrates using quantitative proteomics: isotope-coded affinity tags (ICAT) and isobaric tags for relative and absolute quantification (iTRAQ).
TL;DR: Two protein labeling techniques, Isotope-Coded Affinity Tags (ICAT and Isobaric Tags for Relative and Absolute Quantification (iTRAQ) are used successfully to identify novel matrix metalloproteinase (MMP) substrates in cell culture systems.
Journal ArticleDOI
Precision De Novo Peptide Sequencing Using Mirror Proteases of Ac-LysargiNase and Trypsin for Large-scale Proteomics.
Hao Yang,Yanchang Li,Mingzhi Zhao,Feilin Wu,Xi Wang,Weidi Xiao,Yi-Hao Wang,Junling Zhang,Fuqiang Wang,Feng Xu,Wen-Feng Zeng,Christopher M. Overall,Si-Min He,Hao Chi,Ping Xu,Ping Xu,Ping Xu +16 more
TL;DR: The developed acetylated LysargiNase, with superior activity and stability, provides complementary ion types compared with trypsin for MS/MS analysis and a novel de novo sequencing algorithm, pNovoM, which performed with higher efficiency and accuracy compared with other software tools.