PMID- 23124093
OWN - NLM
STAT- MEDLINE
DCOM- 20130910
LR  - 20160518
IS  - 1876-7737 (Electronic)
IS  - 1874-3919 (Linking)
VI  - 81
DP  - 2013 Apr 9
TI  - Targeted protein identification, quantification and reporting for high-resolution 
      nanoflow targeted peptide monitoring.
PG  - 159-72
LID - S1874-3919(12)00715-4 [pii]
LID - 10.1016/j.jprot.2012.10.020 [doi]
AB  - Mass spectrometry-based targeted proteomic assays are experiencing a surge in 
      awareness due to the diverse possibilities arising from the re-application of 
      traditional LC-SRM technology. The FDA-approved quantitative LC-SRM-pipeline in 
      drug discovery motivates the use to quantitatively validate putative proteomic 
      biomarkers. However, complexity of biological specimens bears a huge challenge to 
      identify, in parallel, specific peptides and proteins of interest from large 
      biomarker candidate lists. Methods have been devised to increase scan speeds, 
      improve detection specificity and verify quantitative SRM-features. In contrast, 
      high-resolution mass spectrometers could be used to improve reliability and 
      precision of targeted proteomics assays. Here, we present a new method for 
      identifying, quantifying and reporting peptides in high-resolution targeted 
      proteomics experiments performed on an orbitrap hybrid instrument using stable 
      isotope-labeled internal reference peptides. This high precision targeted peptide 
      monitoring (TPM) method has unique advantages over existing techniques, including 
      the need to only detect the most abundant product ion of a given target for 
      confident peptide identification using a scoring function that evaluates assay 
      performance based on 1) m/z-mass accuracy, 2) retention time accuracy of observed 
      species relative to prediction, and 3) retention time accuracy relative to 
      internal reference peptides. Further, we show management of multiplexed precision 
      TPM-assays using sentinel peptide standards. This article is part of a Special 
      Issue entitled: From protein structures to clinical applications.
CI  - Copyright (c) 2012. Published by Elsevier B.V.
FAU - Hewel, Johannes A
AU  - Hewel JA
AD  - Banting and Best Department of Medical Research, University of Toronto, Toronto, 
      Ontario, Canada. johannes.hewel@gmail.com
FAU - Phanse, Sadhna
AU  - Phanse S
FAU - Liu, Jian
AU  - Liu J
FAU - Bousette, Nicolas
AU  - Bousette N
FAU - Gramolini, Anthony
AU  - Gramolini A
FAU - Emili, Andrew
AU  - Emili A
LA  - eng
PT  - Journal Article
DEP - 20121102
PL  - Netherlands
TA  - J Proteomics
JT  - Journal of proteomics
JID - 101475056
RN  - 0 (Biomarkers)
RN  - 0 (Muscle Proteins)
RN  - 0 (Peptides)
SB  - IM
MH  - Animals
MH  - Biomarkers/chemistry/metabolism
MH  - *Mass Spectrometry/instrumentation/methods
MH  - Mice
MH  - *Muscle Proteins/analysis/chemistry/metabolism
MH  - *Myocardium/chemistry/metabolism
MH  - *Peptides/analysis/chemistry/metabolism
MH  - *Proteomics/instrumentation/methods
EDAT- 2012/11/06 06:00
MHDA- 2013/09/11 06:00
CRDT- 2012/11/06 06:00
PHST- 2012/07/13 00:00 [received]
PHST- 2012/10/16 00:00 [revised]
PHST- 2012/10/20 00:00 [accepted]
PHST- 2012/11/06 06:00 [entrez]
PHST- 2012/11/06 06:00 [pubmed]
PHST- 2013/09/11 06:00 [medline]
AID - S1874-3919(12)00715-4 [pii]
AID - 10.1016/j.jprot.2012.10.020 [doi]
PST - ppublish
SO  - J Proteomics. 2013 Apr 9;81:159-72. doi: 10.1016/j.jprot.2012.10.020. Epub 2012 
      Nov 2.