Evidence map›Paper›PMID 8710858›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America1996

Sequence tag identification of intact proteins by matching tanden mass spectral data against sequence data bases.

E Mørtz, P B O'Connor, P Roepstorff, N L Kelleher, T D Wood, F W McLafferty, M Mann

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 1996. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 papers.

0numbers the graph read from it
0cells of the map it votes in
42citing papers in PubMed
7.1field-weighted citation impact, top 2% 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

42 citing papers in PubMed, 220 citations in OpenAlex.

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  16. Top-Down Mass Spectrometry of Supercharged Native Protein-Ligand Complexes.International journal of mass spectrometry · 2011
    Article
  17. Article
  18. Article
  19. Article
  20. Gas-phase chemistry of multiply charged bioions in analytical mass spectrometry.Annual review of analytical chemistry (Palo Alto, Calif.) · 2010
    Review
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

7 authors.

E MørtzDepartment of Molecular Biology, Odense University, Denmark.
P B O'Connor
P Roepstorff
N L Kelleher
T D Wood
F W McLafferty
M Mann

Funding

PREDOCTORAL TRAINING IN CELLULAR AND MOLECULAR BIOLOGYT32GM007273 · NIGMS · CORNELL UNIVERSITY ITHACA · PI BRETSCHER, ANTHONY P. · 1985 to 2019
$11.6M
MASS SPECTROMETRY IN BIOMEDICAL RESEARCHR01GM016609 · NIGMS · CORNELL UNIVERSITY ITHACA · PI MC LAFFERTY, FRED WARREN · 1985 to 2010
$1.9M
MASS SPECTROMETRY IN BIOMEDICAL RESEARCHR37GM016609 · NIGMS · CORNELL UNIVERSITY ITHACA · PI MC LAFFERTY, FRED W · 1992 to 2001
$639k
NIGMS NIH HHS 08-T2GM07273NIGMS NIH HHS GM16609
6 · The paper itself

Abstract

Molecular and fragment ion data of intact 8- to 43-kDa proteins from electrospray Fourier-transform tandem mass spectrometry are matched against the corresponding data in sequence data bases. Extending the sequence tag concept of Mann and Wilm for matching peptides, a partial amino acid sequence in the unknown is first identified from the mass differences of a series of fragment ions, and the mass position of this sequence is defined from molecular weight and the fragment ion masses. For three studied proteins, a single sequence tag retrieved only the correct protein from the data base; a fourth protein required the input of two sequence tags. However, three of the data base proteins differed by having an extra methionine or by missing an acetyl or heme substitution. The positions of these modifications in the protein examined were greatly restricted by the mass differences of its molecular and fragment ions versus those of the data base. To characterize the primary structure of an unknown represented in the data base, this method is fast and specific and does not require prior enzymatic or chemical degradation.

Indexed as

Amino Acid SequenceAnimalsCarbonic AnhydrasesChickensCreatine KinaseCytochrome c GroupDatabases, FactualFourier AnalysisHumansMass SpectrometryMolecular Sequence DataProteinsUbiquitinsCarbonic AnhydrasesCreatine KinaseCytochrome c GroupProteinsUbiquitins

Identifiers

PMID8710858
PMCPMC38658
OpenAlexW1982401705

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.