Evidence map›Paper›PMID 35481632›Full record

ArticleProtein science : a publication of the Protein Society2022

Membranome 3.0: Database of single-pass membrane proteins with AlphaFold models.

Andrei L Lomize, Kevin A Schnitzer, Spencer C Todd, Stanislav Cherepanov, Carlos Outeiral, Charlotte M Deane, Irina D Pogozheva

Abstract read
In one paragraph

Article in Protein science : a publication of the Protein Society, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing 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

21 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Emerging role ofFrontiers in molecular neuroscience · 2026
    Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Review
  16. AFTM: a database of transmembrane regions in the human proteome predicted by AlphaFold.Database : the journal of biological databases and curation · 2023
    Article
  17. Article
  18. A journey from molecule to physiology andFrontiers in pharmacology · 2023
    Review
  19. Review
  20. AlphaFold, Artificial Intelligence (AI), and Allostery.The journal of physical chemistry. B · 2022
    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.

Andrei L LomizeDepartment of Medicinal Chemistry, College of Pharmacy, University of Michigan, Ann Arbor, Michigan, USA.ORCID 0000-0002-3044-7597
Kevin A SchnitzerDepartment of Electrical Engineering and Computer Science, College of Engineering, University of Michigan, Ann Arbor, Michigan, USA.ORCID 0000-0002-6490-9323
Spencer C ToddDepartment of Electrical Engineering and Computer Science, College of Engineering, University of Michigan, Ann Arbor, Michigan, USA.ORCID 0000-0002-0120-7674
Stanislav CherepanovDepartment of Biophysics, University of Michigan, Ann Arbor, Michigan, USA.ORCID 0000-0001-9459-1849
Carlos OuteiralDepartment of Statistics, University of Oxford, UK.ORCID 0000-0003-1408-5554
Charlotte M DeaneDepartment of Statistics, University of Oxford, UK.ORCID 0000-0003-1388-2252
Irina D PogozhevaDepartment of Medicinal Chemistry, College of Pharmacy, University of Michigan, Ann Arbor, Michigan, USA.ORCID 0000-0002-3024-9574

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The Membranome database provides comprehensive structural information on single-pass (i.e., bitopic) membrane proteins from six evolutionarily distant organisms, including protein-protein interactions, complexes, mutations, experimental structures, and models of transmembrane α-helical dimers. We present a new version of this database, Membranome 3.0, which was significantly updated by revising the set of 5,758 bitopic proteins and incorporating models generated by AlphaFold 2 in the database. The AlphaFold models were parsed into structural domains located at the different membrane sides, modified to exclude low-confidence unstructured terminal regions and signal sequences, validated through comparison with available experimental structures, and positioned with respect to membrane boundaries. Membranome 3.0 was re-developed to facilitate visualization and comparative analysis of multiple 3D structures of proteins that belong to a specified family, complex, biological pathway, or membrane type. New tools for advanced search and analysis of proteins, their interactions, complexes, and mutations were included. The database is freely accessible at https://membranome.org.

Indexed as

Membrane ProteinsDatabases, ProteinProtein Conformation, alpha-HelicalMembrane Proteinsfull-length protein modelnetwork analysisvisualizationweb tool

Identifiers

PMID35481632
PMCPMC9047035

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.