Evidence map›Paper›PMID 28864201›Full record

ArticleJournal of molecular biology2017

OPUS-DOSP: A Distance- and Orientation-Dependent All-Atom Potential Derived from Side-Chain Packing.

Gang Xu, Tianqi Ma, Tianwu Zang, Weitao Sun, Qinghua Wang, Jianpeng Ma

Abstract read
In one paragraph

Article in Journal of molecular biology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.

0numbers the graph read from it
0cells of the map it votes in
8citing 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

8 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Review
  7. Article
  8. OPUS-SSF: A side-chain-inclusive scoring function for ranking protein structural models.Protein science : a publication of the Protein Society · 2019
    Article
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

6 authors.

Gang XuSchool of Life Sciences, Tsinghua University, Beijing 100084, China.
Tianqi MaApplied Physics Program, Rice University, Houston, TX 77005, United States; Department of Bioengineering, Rice University, Houston, TX 77005, United States.
Tianwu ZangApplied Physics Program, Rice University, Houston, TX 77005, United States; Department of Bioengineering, Rice University, Houston, TX 77005, United States.
Weitao SunZhou Pei-Yuan Center for Applied Mathematics, Tsinghua University, Beijing 100084, China.
Qinghua WangVerna and Marrs Mclean Department of Biochemistry and Molecular Biology, Baylor College of Medicine, Houston, TX 77030, United States.
Jianpeng MaSchool of Life Sciences, Tsinghua University, Beijing 100084, China; Applied Physics Program, Rice University, Houston, TX 77005, United States; Department of Bioengineering, Rice University, Houston, TX 77005, United States; Verna and Marrs Mclean Department of Biochemistry and Molecular Biology, Baylor College of Medicine, Houston, TX 77030, United States. Electronic address: jpma@bcm.edu.

Funding

New Simulation Methods at Multi-Scales and -ResolutionsR01GM067801 · NIGMS · BAYLOR COLLEGE OF MEDICINE · PI MA, JIANPENG · 2003 to 2015
$3.4M
Structural and Functional Study of Influenza Virus HemagglutininR01AI067839 · NIAID · BAYLOR COLLEGE OF MEDICINE · PI WANG, QINGHUA · 2009 to 2013
$1.5M
Molecular Mechanisms of Actin Cytoskeleton DynamicsR01GM116280 · NIGMS · BAYLOR COLLEGE OF MEDICINE · PI MA, JIANPENG, WANG, QINGHUA · 2016 to 2019
$1.4M
NIAID NIH HHS R01 AI067839NIGMS NIH HHS R01 GM067801NIGMS NIH HHS R01 GM116280
6 · The paper itself

Abstract

We report a new distance- and orientation-dependent, all-atom statistical potential derived from side-chain packing, named OPUS-DOSP, for protein structure modeling. The framework of OPUS-DOSP is based on OPUS-PSP, previously developed by us [JMB (2008), 376, 288-301], with refinement and new features. In particular, distance or orientation contribution is considered depending on the range of contact distance. A new auxiliary function in energy function is also introduced, in addition to the traditional Boltzmann term, in order to adjust the contributions of extreme cases. OPUS-DOSP was tested on 11 decoy sets commonly used for statistical potential benchmarking. Among 278 native structures, 239 and 249 native structures were recognized by OPUS-DOSP without and with the auxiliary function, respectively. The results show that OPUS-DOSP has an increased decoy recognition capability comparing with those of other relevant potentials to date.

Indexed as

Models, MolecularChemistryComputational BiologyModels, StatisticalMolecular Biologydecoy recognitionempirical potential functionprotein foldingprotein structure predictionside-chain packing

Identifiers

PMID28864201
PMCPMC6193766

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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.