Evidence map›Paper›PMID 24203295›Full record

ArticleJournal of the American Society for Mass Spectrometry1996

Identification of phosphorylation sites in phosphopeptides by positive and negative mode electrospray ionization-tandem mass spectrometry.

M Busman, K L Schey, J E Oatis, D R Knapp

Abstract read
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In one paragraph

Article in Journal of the American Society for Mass Spectrometry, 1996. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.

0numbers the graph read from it
0cells of the map it votes in
9citing papers in PubMed
2.2field-weighted citation impact, top 14% 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

9 citing papers in PubMed, 37 citations in OpenAlex.

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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.

M BusmanDepartment of Pharmacology, Medical University of South Carolina, 29425-2251, Charleston, SC.
K L Schey
J E Oatis
D R Knapp
Medical University of South Carolina · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

A series of synthetic mono- and diphosphorylated peptides has been analyzed by positive and negative mode electrospray ionization-tandem mass spectrometry. The synthetic peptides are serine- and threonine-phosphorylated analogs of proteolytic fragments from the C-terminal region of rhodopsin. Use of positive and negative modes of electrospray ionization to produce ions for tandem mass spectrometry via low energy collision-induced dissociation was explored. For some of the peptides, the complementary use of experimental results allowed determination of the phosphorylation sites when either mode alone gave incomplete information. Other peptides, however, gave negative ion spectra not interpretable in terms of backbone cleavages. However, use of positive ion tandem mass spectrometry of different charge state precursor ions gave sufficient information in most cases to assign sites of phosphorylation. These results illustrate the utility of obtaining complementary information by tandem mass spectrometry by using precursor ions of different charge polarity or number.

Identifiers

PMID24203295
OpenAlexW1988661674

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.