Evidence map›Paper›PMID 16372357›Full record

ArticleProteins2006

Multipass membrane protein structure prediction using Rosetta.

Vladimir Yarov-Yarovoy, Jack Schonbrun, David Baker

Abstract read
In one paragraph

Article in Proteins, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 187 papers.

0numbers the graph read from it
0cells of the map it votes in
187citing 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

187 citing papers in PubMed.

  1. Article
  2. Article
  3. Atomistic mechanisms of the regulation of small-conductance CaProceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  4. Review
  5. Article
  6. Article
  7. Article
  8. Recent Advances in NMR Protein Structure Prediction with ROSETTA.International journal of molecular sciences · 2023
    Review
  9. Elucidation of a dynamic interplay between a beta-2 adrenergic receptor, its agonist, and stimulatory G protein.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  10. Article
  11. Review
  12. Integrated AlphaFold2 and DEER investigation of the conformational dynamics of a pH-dependent APC antiporter.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  13. Article
  14. The seizure-inducing plastic explosive RDX inhibits the α1β2γ2 GABAAnnals of clinical and translational neurology · 2022
    Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Diverse Scientific Benchmarks for Implicit Membrane Energy Functions.Journal of chemical theory and computation · 2021
    Article
  20. Article

127 more citing papers are in PubMed but not listed here.

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

3 authors.

Vladimir Yarov-YarovoyDepartment of Pharmacology, University of Washington, Seattle, Washington 98195, USA.
Jack Schonbrun
David Baker

Funding

VOLTAGE-SENSITIVE SODIUM CHANNELS IN BRAINR01NS015751 · NINDS · UNIVERSITY OF WASHINGTON · PI CATTERALL, WILLIAM A · 1985 to 2018
$6.0M
Structural Modeling of Brain Sodium and Calcium ChannelsK01MH067625 · NIMH · UNIVERSITY OF WASHINGTON · PI YAROV-YAROVOY, VLADIMIR M. · 2003 to 2007
$552k
NIMH NIH HHS K01 MH067625NIMH NIH HHS K01 MH067625-01NIMH NIH HHS K01 MH067625-02NIMH NIH HHS K01 MH067625-03NIMH NIH HHS K01 MH67625NINDS NIH HHS R01 NS015751NINDS NIH HHS R01 NS15751
6 · The paper itself

Abstract

We describe the adaptation of the Rosetta de novo structure prediction method for prediction of helical transmembrane protein structures. The membrane environment is modeled by embedding the protein chain into a model membrane represented by parallel planes defining hydrophobic, interface, and polar membrane layers for each energy evaluation. The optimal embedding is determined by maximizing the exposure of surface hydrophobic residues within the membrane and minimizing hydrophobic exposure outside of the membrane. Protein conformations are built up using the Rosetta fragment assembly method and evaluated using a new membrane-specific version of the Rosetta low-resolution energy function in which residue-residue and residue-environment interactions are functions of the membrane layer in addition to amino acid identity, distance, and density. We find that lower energy and more native-like structures are achieved by sequential addition of helices to a growing chain, which may mimic some aspects of helical protein biogenesis after translocation, rather than folding the whole chain simultaneously as in the Rosetta soluble protein prediction method. In tests on 12 membrane proteins for which the structure is known, between 51 and 145 residues were predicted with root-mean-square deviation <4 A from the native structure.

Indexed as

EnzymesMembrane ProteinsModels, MolecularModels, TheoreticalProtein BindingProtein Structure, SecondarySolubilitySolutionsSuccinate DehydrogenaseWaterEnzymesMembrane ProteinsSolutionsSuccinate DehydrogenaseWater

Identifiers

PMID16372357
PMCPMC1479309

What OpenQuestion holds

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Read underepoch 390

Registered trials

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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.