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Enhanced Dissociation of Intact Proteins with High Capacity Electron Transfer Dissociation

Overview of attention for article published in Journal of the American Society for Mass Spectrometry, November 2015
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About this Attention Score

  • In the top 25% of all research outputs scored by Altmetric
  • High Attention Score compared to outputs of the same age (83rd percentile)
  • High Attention Score compared to outputs of the same age and source (87th percentile)

Mentioned by

blogs
1 blog
twitter
3 tweeters

Citations

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22 Dimensions

Readers on

mendeley
36 Mendeley
Title
Enhanced Dissociation of Intact Proteins with High Capacity Electron Transfer Dissociation
Published in
Journal of the American Society for Mass Spectrometry, November 2015
DOI 10.1007/s13361-015-1306-8
Pubmed ID
Authors

Nicholas M. Riley, Christopher Mullen, Chad R. Weisbrod, Seema Sharma, Michael W. Senko, Vlad Zabrouskov, Michael S. Westphall, John E. P. Syka, Joshua J. Coon

Abstract

Electron transfer dissociation (ETD) is a valuable tool for protein sequence analysis, especially for the fragmentation of intact proteins. However, low product ion signal-to-noise often requires some degree of signal averaging to achieve high quality MS/MS spectra of intact proteins. Here we describe a new implementation of ETD on the newest generation of quadrupole-Orbitrap-linear ion trap Tribrid, the Orbitrap Fusion Lumos, for improved product ion signal-to-noise via ETD reactions on larger precursor populations. In this new high precursor capacity ETD implementation, precursor cations are accumulated in the center section of the high pressure cell in the dual pressure linear ion trap prior to charge-sign independent trapping, rather than precursor ion sequestration in only the back section as is done for standard ETD. This new scheme increases the charge capacity of the precursor accumulation event, enabling storage of approximately 3-fold more precursor charges. High capacity ETD boosts the number of matching fragments identified in a single MS/MS event, reducing the need for spectral averaging. These improvements in intra-scan dynamic range via reaction of larger precursor populations, which have been previously demonstrated through custom modified hardware, are now available on a commercial platform, offering considerable benefits for intact protein analysis and top down proteomics. In this work, we characterize the advantages of high precursor capacity ETD through studies with myoglobin and carbonic anhydrase. Graphical Abstract ᅟ.

Twitter Demographics

The data shown below were collected from the profiles of 3 tweeters who shared this research output. Click here to find out more about how the information was compiled.

Mendeley readers

The data shown below were compiled from readership statistics for 36 Mendeley readers of this research output. Click here to see the associated Mendeley record.

Geographical breakdown

Country Count As %
Netherlands 1 3%
Canada 1 3%
Unknown 34 94%

Demographic breakdown

Readers by professional status Count As %
Student > Ph. D. Student 15 42%
Researcher 9 25%
Student > Doctoral Student 4 11%
Student > Postgraduate 2 6%
Unspecified 2 6%
Other 4 11%
Readers by discipline Count As %
Chemistry 16 44%
Agricultural and Biological Sciences 8 22%
Unspecified 5 14%
Biochemistry, Genetics and Molecular Biology 5 14%
Pharmacology, Toxicology and Pharmaceutical Science 1 3%
Other 1 3%

Attention Score in Context

This research output has an Altmetric Attention Score of 9. 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 25 February 2016.
All research outputs
#1,893,061
of 13,157,683 outputs
Outputs from Journal of the American Society for Mass Spectrometry
#132
of 2,294 outputs
Outputs of similar age
#56,868
of 353,772 outputs
Outputs of similar age from Journal of the American Society for Mass Spectrometry
#4
of 33 outputs
Altmetric has tracked 13,157,683 research outputs across all sources so far. Compared to these this one has done well and is in the 85th percentile: it's in the top 25% of all research outputs ever tracked by Altmetric.
So far Altmetric has tracked 2,294 research outputs from this source. They receive a mean Attention Score of 2.8. This one has done particularly well, scoring higher than 94% 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 353,772 tracked outputs that were published within six weeks on either side of this one in any source. This one has done well, scoring higher than 83% of its contemporaries.
We're also able to compare this research output to 33 others from the same source and published within six weeks on either side of this one. This one has done well, scoring higher than 87% of its contemporaries.