Evidence map›Paper›PMID 35044719›Full record

ArticleMolecular systems biology2022

Proteome-scale mapping of binding sites in the unstructured regions of the human proteome.

Caroline Benz, Muhammad Ali, Izabella Krystkowiak, Leandro Simonetti, Ahmed Sayadi, Filip Mihalic, Johanna Kliche, Eva Andersson, Per Jemth, Norman E Davey and 1 more

Abstract read
In one paragraph

Article in Molecular systems biology, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 50 papers.

0numbers the graph read from it
0cells of the map it votes in
50citing 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

50 citing papers in PubMed.

  1. Article
  2. Article
  3. Uncovering cancer dependencies in peptide-interacting protein pockets.bioRxiv : the preprint server for biology · 2026
    Article
  4. Article
  5. A proteome-wide dependency map of protein interaction motifs.Nature structural & molecular biology · 2026
    Article
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  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Review
  13. Article
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  15. Article
  16. Review
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  19. Article
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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

11 authors.

Caroline BenzDepartment of Chemistry - BMC, Uppsala University, Uppsala, Sweden.ORCID 0000-0002-5166-3598
Muhammad AliDepartment of Chemistry - BMC, Uppsala University, Uppsala, Sweden.ORCID 0000-0002-8858-6776
Izabella KrystkowiakDivision of Cancer Biology, The Institute of Cancer Research, London, UK.ORCID 0000-0002-8863-7086
Leandro SimonettiDepartment of Chemistry - BMC, Uppsala University, Uppsala, Sweden.ORCID 0000-0003-1283-9770
Ahmed SayadiDepartment of Chemistry - BMC, Uppsala University, Uppsala, Sweden.
Filip MihalicDepartment of Medical Biochemistry and Microbiology, Uppsala University, Uppsala, Sweden.ORCID 0000-0002-6840-2319
Johanna KlicheDepartment of Chemistry - BMC, Uppsala University, Uppsala, Sweden.ORCID 0000-0003-3179-4635
Eva AnderssonDepartment of Medical Biochemistry and Microbiology, Uppsala University, Uppsala, Sweden.
Per JemthDepartment of Medical Biochemistry and Microbiology, Uppsala University, Uppsala, Sweden.ORCID 0000-0003-1516-7228
Norman E DaveyDivision of Cancer Biology, The Institute of Cancer Research, London, UK.ORCID 0000-0001-6988-4850
Ylva IvarssonDepartment of Chemistry - BMC, Uppsala University, Uppsala, Sweden.ORCID 0000-0002-7081-3846

Funding

Cancer Research UK 28159
6 · The paper itself

Abstract

Specific protein-protein interactions are central to all processes that underlie cell physiology. Numerous studies have together identified hundreds of thousands of human protein-protein interactions. However, many interactions remain to be discovered, and low affinity, conditional, and cell type-specific interactions are likely to be disproportionately underrepresented. Here, we describe an optimized proteomic peptide-phage display library that tiles all disordered regions of the human proteome and allows the screening of ~ 1,000,000 overlapping peptides in a single binding assay. We define guidelines for processing, filtering, and ranking the results and provide PepTools, a toolkit to annotate the identified hits. We uncovered >2,000 interaction pairs for 35 known short linear motif (SLiM)-binding domains and confirmed the quality of the produced data by complementary biophysical or cell-based assays. Finally, we show how the amino acid resolution-binding site information can be used to pinpoint functionally important disease mutations and phosphorylation events in intrinsically disordered regions of the proteome. The optimized human disorderome library paired with PepTools represents a powerful pipeline for unbiased proteome-wide discovery of SLiM-based interactions.

Indexed as

ProteomeProteomicsBinding SitesHumansPeptide LibraryPeptidesProtein BindingPeptide LibraryPeptidesProteomeintrinsically disordered regionspeptidesphage displayprotein-protein interactionsshort linear motifs

Identifiers

PMID35044719
PMCPMC8769072

What OpenQuestion holds

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LicenceCC BY
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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.