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Trypsin catalyzed 16O-to-18O exchange for comparative proteomics: Tandem mass spectrometry comparison using MALDI-TOF, ESI-QTOF, and ESI-ion trap mass spectrometers

Overview of attention for article published in Journal of the American Society for Mass Spectrometry, July 2003
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About this Attention Score

  • In the top 25% of all research outputs scored by Altmetric
  • Good Attention Score compared to outputs of the same age (73rd percentile)
  • High Attention Score compared to outputs of the same age and source (88th percentile)

Mentioned by

patent
4 patents

Citations

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110 Dimensions

Readers on

mendeley
67 Mendeley
Title
Trypsin catalyzed 16O-to-18O exchange for comparative proteomics: Tandem mass spectrometry comparison using MALDI-TOF, ESI-QTOF, and ESI-ion trap mass spectrometers
Published in
Journal of the American Society for Mass Spectrometry, July 2003
DOI 10.1016/s1044-0305(03)00207-1
Pubmed ID
Authors

Manfred Heller, Hassan Mattou, Christoph Menzel, Xudong Yao

Abstract

Quantitative or comparative proteome analysis was initially performed with 2-dimensional gel electrophoresis with the inherent disadvantages of being biased towards certain proteins and being labor intensive. Alternative mass spectrometry-based approaches in conjunction with gel-free protein/peptide separation have been developed in recent years using various stable isotope labeling techniques. Common to all these techniques is the incorporation, biosynthetically or chemically, of a labeling moiety having either a natural isotope distribution of hydrogen, carbon, oxygen, or nitrogen (light form) or being enriched with heavy isotopes like deuterium, (13)C, (18)O, or (15)N, respectively. By mixing equal amounts of a control sample possessing for instance the light form of the label with a heavy-labeled case sample, differentially labeled peptides are detected by mass spectrometric methods and their intensities serve as a means for direct relative protein quantification. While each of the different labeling methods has its advantages and disadvantages, the endoprotease (16)O-to-(18)O catalyzed oxygen exchange at the C-terminal carboxylic acid is extremely promising because of the specificity assured by the enzymatic reaction and the labeling of essentially every protease-derived peptide. We show here that this methodology is applicable to complex biological samples such as a subfraction of human plasma. Furthermore, despite the relatively small mass difference of 4 Da between the two labeled forms, corresponding to the exchange of two oxygen atoms by two (18)O isotopes, it is possible to quantify differentially labeled proteins on an ion trap mass spectrometer with a mass resolution of about 2000 in automated data dependent LC-MS/MS acquisition mode. Post column sample deposition on a MALDI target parallel to on-line ESI-MS/MS enables the analysis of the same compounds by means of ESI- and MALDI-MS/MS. This has the potential to increase the confidence in the quantification results as well as to increase the sequence coverage of potentially interesting proteins by complementary peptide ionization techniques. Additionally the paired y-ion signals in tandem mass spectra of (16)O/(18)O-labeled peptide pairs provide a means to confirm automatic protein identification results or even to assist de novo sequencing of yet unknown proteins.

Mendeley readers

The data shown below were compiled from readership statistics for 67 Mendeley readers of this research output. Click here to see the associated Mendeley record.

Geographical breakdown

Country Count As %
United States 2 3%
United Kingdom 1 1%
Germany 1 1%
India 1 1%
Italy 1 1%
Brazil 1 1%
Spain 1 1%
Unknown 59 88%

Demographic breakdown

Readers by professional status Count As %
Researcher 28 42%
Student > Ph. D. Student 12 18%
Student > Bachelor 5 7%
Professor > Associate Professor 5 7%
Other 4 6%
Other 13 19%
Readers by discipline Count As %
Agricultural and Biological Sciences 29 43%
Chemistry 15 22%
Biochemistry, Genetics and Molecular Biology 7 10%
Computer Science 6 9%
Unspecified 5 7%
Other 5 7%

Attention Score in Context

This research output has an Altmetric Attention Score of 6. This is our high-level measure of the quality and quantity of online attention that it has received. This Attention Score, as well as the ranking and number of research outputs shown below, was calculated when the research output was last mentioned on 11 March 2014.
All research outputs
#2,113,140
of 12,287,471 outputs
Outputs from Journal of the American Society for Mass Spectrometry
#142
of 2,142 outputs
Outputs of similar age
#70,657
of 265,098 outputs
Outputs of similar age from Journal of the American Society for Mass Spectrometry
#10
of 85 outputs
Altmetric has tracked 12,287,471 research outputs across all sources so far. Compared to these this one has done well and is in the 79th percentile: it's in the top 25% of all research outputs ever tracked by Altmetric.
So far Altmetric has tracked 2,142 research outputs from this source. They receive a mean Attention Score of 2.9. This one has done well, scoring higher than 85% of its peers.
Older research outputs will score higher simply because they've had more time to accumulate mentions. To account for age we can compare this Altmetric Attention Score to the 265,098 tracked outputs that were published within six weeks on either side of this one in any source. This one has gotten more attention than average, scoring higher than 73% of its contemporaries.
We're also able to compare this research output to 85 others from the same source and published within six weeks on either side of this one. This one has done well, scoring higher than 88% of its contemporaries.