Evidence map›Paper›PMID 18598898›Full record

ArticleJournal of the American Society for Mass Spectrometry2008

Surface-induced dissociation shows potential to be more informative than collision-induced dissociation for structural studies of large systems.

Vicki H Wysocki, Christopher M Jones, Asiri S Galhena, Anne E Blackwell

Abstract read
In one paragraph

Article in Journal of the American Society for Mass Spectrometry, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.

0numbers the graph read from it
0cells of the map it votes in
33citing papers in PubMed
3.1field-weighted citation impact, top 9% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

33 citing papers in PubMed, 84 citations in OpenAlex.

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  19. Controlling dissociation channels of gas-phase protein complexes using charge manipulation.Journal of the American Society for Mass Spectrometry · 2014
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

4 authors at 1 institution in 1 country.

Vicki H WysockiDepartment of Chemistry, Department of Biochemistry and Molecular Biophysics, University of Arizona, Tucson, Arizona 857-0041, USA. vwysocki@email.arizona.edu
Christopher M Jones
Asiri S Galhena
Anne E Blackwell
University of Arizona · US

Funding

Influence of Peptide Structure on DissociationR01GM051387 · NIGMS · VIRGINIA COMMONWEALTH UNIVERSITY · PI WYSOCKI, VICKI H. · 1994 to 2010
$2.4M
NIGMS NIH HHS 5R01 GM-051387NIGMS NIH HHS R01 GM051387
6 · The paper itself

Abstract

The ability to preserve noncovalent, macromolecular assemblies intact in the gas phase has paved the way for mass spectrometry to characterize ions of increasing size and become a powerful tool in the field of structural biology. Tandem mass spectrometry experiments have the potential to expand the capabilities of this technique through the gas-phase dissociation of macromolecular complexes, but collisions with small gas atoms currently provide very limited fragmentation. One alternative for dissociating large ions is to collide them into a surface, a more massive target. Here, we demonstrate the ability and benefit of fragmenting large protein complexes and inorganic salt clusters by surface-induced dissociation (SID), which provides more extensive fragmentation of these systems and shows promise as an activation method for ions of increasing size.

Indexed as

Protein ConformationAnimalsHumansMultiprotein ComplexesSpectrometry, Mass, Electrospray IonizationSurface PropertiesMultiprotein Complexes

Identifiers

PMID18598898
PMCPMC4186222
OpenAlexW2050060187

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.