Evidence map›Paper›PMID 25995083›Full record

ArticleNature communications2015

Evolutionary-guided de novo structure prediction of self-associated transmembrane helical proteins with near-atomic accuracy.

Y Wang, P Barth

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed
2.9field-weighted citation impact, top 9% 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

27 citing papers in PubMed, 39 citations in OpenAlex.

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  14. De novo designed transmembrane peptides activating the α5β1 integrin.Protein engineering, design & selection : PEDS · 2018
    Article
  15. Article
  16. Forecasting residue-residue contact prediction accuracy.Bioinformatics (Oxford, England) · 2017
    Article
  17. Article
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  20. 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

2 authors at 1 institution in 1 country.

Y WangStructural and Computational Biology and Molecular Biophysics Graduate Program, Baylor College of Medicine, One Baylor Plaza, Houston, Texas 77030, USA.
P Barth1] Structural and Computational Biology and Molecular Biophysics Graduate Program, Baylor College of Medicine, One Baylor Plaza, Houston, Texas 77030, USA [2] Verna and Marrs McLean Department of Biochemistry and Molecular Biology, Baylor College of Medicine, One Baylor Plaza, Houston, Texas 77030, USA [3] Department of Pharmacology, Baylor College of Medicine, One Baylor Plaza, Houston, Texas 77030, USA.
Baylor College of Medicine · US

Funding

EXPLORING STRUCTURE AND SEQUENCE SPACES OF G PROTEIN-COUPLED RECEPTOR SIGNALINGR01GM097207 · NIGMS · BAYLOR COLLEGE OF MEDICINE · PI BARTH, PATRICK DANIEL, WENSEL, THEODORE G · 2012 to 2020
$2.8M
NIGMS NIH HHS 1R01GM097207-01A1NIGMS NIH HHS R01 GM097207
6 · The paper itself

Abstract

How specific protein associations regulate the function of membrane receptors remains poorly understood. Conformational flexibility currently hinders the structure determination of several classes of membrane receptors and associated oligomers. Here we develop EFDOCK-TM, a general method to predict self-associated transmembrane protein helical (TMH) structures from sequence guided by co-evolutionary information. We show that accurate intermolecular contacts can be identified using a combination of protein sequence covariation and TMH binding surfaces predicted from sequence. When applied to diverse TMH oligomers, including receptors characterized in multiple conformational and functional states, the method reaches unprecedented near-atomic accuracy for most targets. Blind predictions of structurally uncharacterized receptor tyrosine kinase TMH oligomers provide a plausible hypothesis on the molecular mechanisms of disease-associated point mutations and binding surfaces for the rational design of selective inhibitors. The method sets the stage for uncovering novel determinants of molecular recognition and signalling in single-spanning eukaryotic membrane receptors.

Indexed as

Evolution, MolecularProtein ConformationAmino Acid SequenceHumansMolecular Sequence DataProtein MultimerizationReceptor Protein-Tyrosine KinasesReceptors, Cell SurfaceSoftwareReceptor Protein-Tyrosine KinasesReceptors, Cell Surface

Identifiers

PMID25995083
PMCPMC4833009
OpenAlexW2259375290

What OpenQuestion holds

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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.