Evidence map›Paper›PMID 33635637›Full record

ArticleJournal of chemical information and modeling2021

Transmembrane Protein Docking with JabberDock.

Lucas S P Rudden, Matteo T Degiacomi

Abstract read
In one paragraph

Article in Journal of chemical information and modeling, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing 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

11 citing papers in PubMed.

  1. Article
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  4. Article
  5. Challenges of Protein-Protein Docking of the Membrane Proteins.Methods in molecular biology (Clifton, N.J.) · 2024
    Article
  6. Review
  7. 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

2 authors.

Lucas S P RuddenDepartment of Physics, Durham University, South Road, DH1 3LE Durham, United Kingdom.
Matteo T DegiacomiDepartment of Physics, Durham University, South Road, DH1 3LE Durham, United Kingdom.ORCID 0000-0003-4672-471X

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Transmembrane proteins act as an intermediary for a broad range of biological process. Making up 20% to 30% of the proteome, their ubiquitous nature has resulted in them comprising 50% of all targets in drug design. Despite their importance, they make up only 4% of all structures in the PDB database, primarily owing to difficulties associated with isolating and characterizing them. Membrane protein docking algorithms could help to fill this knowledge gap, yet only few exist. Moreover, these existing methods achieve success rates lower than the current best soluble proteins docking software. We present and test a pipeline using our software, JabberDock, to dock membrane proteins. JabberDock docks shapes representative of membrane protein structure and dynamics in their biphasic environment. We verify JabberDock's ability to yield accurate predictions by applying it to a benchmark of 20 transmembrane dimers, returning a success rate of 75.0%. This makes our software very competitive among available membrane protein-protein docking tools.

Indexed as

AlgorithmsSoftwareDatabases, ProteinDrug DesignLigandsMembrane ProteinsMolecular Docking SimulationProtein BindingLigandsMembrane Proteins

Identifiers

PMID33635637
PMCPMC8041277

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.