Evidence map›Paper›PMID 36178621›Full record

ArticleMethods in molecular biology (Clifton, N.J.)2023

Limited Proteolysis-Mass Spectrometry to Identify Metabolite-Protein Interactions.

Aleš Holfeld, Jan-Philipp Quast, Roland Bruderer, Lukas Reiter, Natalie de Souza, Paola Picotti

Abstract read
PubMed Publisher
In one paragraph

Article in Methods in molecular biology (Clifton, N.J.), 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
10.5field-weighted citation impact, top 1% 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

12 citing papers in PubMed, 23 citations in OpenAlex.

  1. Review
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  8. Stability-based approaches in chemoproteomics.Expert reviews in molecular medicine · 2024
    Review
  9. Article
  10. Review
  11. The Knowns and Unknowns in Protein-Metabolite Interactions.International journal of molecular sciences · 2023
    Review
  12. 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

6 authors at 2 institutions in 1 country.

Aleš Holfeld *Institute of Molecular Systems Biology, Department of Biology, ETH Zurich, Zurich, Switzerland.
Jan-Philipp Quast *Institute of Molecular Systems Biology, Department of Biology, ETH Zurich, Zurich, Switzerland.
Roland BrudererBiognosys AG, Schlieren, Switzerland.
Lukas ReiterBiognosys AG, Schlieren, Switzerland.
Natalie de SouzaInstitute of Molecular Systems Biology, Department of Biology, ETH Zurich, Zurich, Switzerland.
Paola PicottiInstitute of Molecular Systems Biology, Department of Biology, ETH Zurich, Zurich, Switzerland. picotti@imsb.biol.ethz.ch.
ETH Zurich · CHBiognosys (Switzerland) · CH

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Metabolite-protein interactions regulate diverse cellular processes, prompting the development of methods to investigate the metabolite-protein interactome at a global scale. One such method is our previously developed structural proteomics approach, limited proteolysis-mass spectrometry (LiP-MS), which detects proteome-wide metabolite-protein and drug-protein interactions in native bacterial, yeast, and mammalian systems, and allows identification of binding sites without chemical modification. Here we describe a detailed experimental and analytical workflow for conducting a LiP-MS experiment to detect small molecule-protein interactions, either in a single-dose (LiP-SMap) or a multiple-dose (LiP-Quant) format. LiP-Quant analysis combines the peptide-level resolution of LiP-MS with a machine learning-based framework to prioritize true protein targets of a small molecule of interest. We provide an updated R script for LiP-Quant analysis via a GitHub repository accessible at https://github.com/RolandBruderer/MiMB-LiP-Quant .

Indexed as

ProteomeProteomicsAnimalsMammalsMass SpectrometryPeptidesProteolysisPeptidesProteomeLimited proteolysisLiP–QuantLiP–SMapMachine learningMass spectrometryMetaboliteProtein interactionsProteomicsStructural proteomics

Identifiers

PMID36178621
OpenAlexW4298088972

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.