Evidence map›Paper›PMID 25546807›Full record

ReviewProteomics2015

Studying macromolecular complex stoichiometries by peptide-based mass spectrometry.

Ingo Wohlgemuth, Christof Lenz, Henning Urlaub

Abstract readReview
In one paragraph

Review in Proteomics, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
–field-weighted citation impact
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

13 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Review
  7. Article
  8. Article
  9. Review
  10. Article
  11. Review
  12. Protein turnover measurement using selected reaction monitoring-mass spectrometry (SRM-MS).Philosophical transactions. Series A, Mathematical, physical, and engineering sciences · 2016
    Article
  13. Revealing Higher Order Protein Structure Using Mass Spectrometry.Journal of the American Society for Mass Spectrometry · 2016
    Article
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

3 authors.

Ingo WohlgemuthDepartment of Physical Biochemistry, Max Planck Institute for Biophysical Chemistry, Goettingen, Germany.
Christof Lenz
Henning Urlaub

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

A majority of cellular functions are carried out by macromolecular complexes. A host of biochemical and spectroscopic methods exists to characterize especially protein/protein complexes, however there has been a lack of a universal method to determine protein stoichiometries. Peptide-based MS, especially as a complementary method to the MS analysis of intact protein complexes, has now been developed to a point where it can be employed to assay protein stoichiometries in a routine manner. While the experimental demands are still significant, peptide-based MS has been successfully applied to analyze stoichiometries for a variety of protein complexes from very different biological backgrounds. In this review, we discuss the requirements especially for targeted MS acquisition strategies to be used in this context, with a special focus on the interconnected experimental aspects of sample preparation, protein digestion, and peptide stability. In addition, different strategies for the introduction of quantitative peptide standards and their suitability for different scenarios are compared.

Indexed as

Macromolecular SubstancesPeptidesMass SpectrometryProteomicsMacromolecular SubstancesPeptidesMass spectrometryProtein complexSRMStoichiometryTechnology

Identifiers

PMID25546807
PMCPMC5024058

What OpenQuestion holds

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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.