Evidence map›Paper›PMID 27771482›Full record

ArticleJournal of molecular biology2017

ClusPro-DC: Dimer Classification by the Cluspro Server for Protein-Protein Docking.

Christine Yueh, David R Hall, Bing Xia, Dzmitry Padhorny, Dima Kozakov, Sandor Vajda

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 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing 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

23 citing papers in PubMed.

  1. Towards precision epitopes based vaccine againstBiochemistry and biophysics reports · 2025
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  14. Review
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  16. Challenges in protein docking.Current opinion in structural biology · 2020
    Review
  17. Article
  18. Article
  19. Article
  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

6 authors.

Christine YuehDepartment of Biomedical Engineering, Boston University, Boston, MA 02215, USA.
David R HallAcpharis Inc., Holliston, MA 01746, USA.
Bing XiaDepartment of Biomedical Engineering, Boston University, Boston, MA 02215, USA.
Dzmitry PadhornyDepartment of Applied Mathematics and Statistics, Stony Brook University, Stony Brook, NY 11794, USA; Laufer Center for Physical and Quantitative Biology, Stony Brook University, Stony Brook, NY 11794, USA.
Dima KozakovDepartment of Biomedical Engineering, Boston University, Boston, MA 02215, USA; Department of Applied Mathematics and Statistics, Stony Brook University, Stony Brook, NY 11794, USA; Laufer Center for Physical and Quantitative Biology, Stony Brook University, Stony Brook, NY 11794, USA. Electronic address: midas@laufercenter.org.
Sandor VajdaDepartment of Biomedical Engineering, Boston University, Boston, MA 02215, USA. Electronic address: vajda@bu.edu.

Funding

Analysis and Prediction of Molecular InteractionsR35GM118078 · NIGMS · BOSTON UNIVERSITY (CHARLES RIVER CAMPUS) · PI SANDOR VAJDA · 2016 to 2026
$6.5M
A MULTISTAGE APPROACH TO PROTEIN-PROTEIN DOCKINGR01GM061867 · NIGMS · BOSTON UNIVERSITY (CHARLES RIVER CAMPUS) · PI VAJDA, SANDOR · 2000 to 2016
$4.0M
NIGMS NIH HHS R01 GM061867NIGMS NIH HHS R35 GM118078
6 · The paper itself

Abstract

ClusPro-DC (https://cluspro.bu.edu/) implements a straightforward approach to the discrimination between crystallographic and biological dimers by docking the two subunits to exhaustively sample the interaction energy landscape. If a substantial number of low energy docked poses cluster in a narrow vicinity of the native structure of the dimer, then one can assume that there is a well-defined free energy well around the native state, which makes the interaction stable. In contrast, if the interaction sites in the docked poses do not form a large enough cluster around the native structure, then it is unlikely that the subunits form a stable biological dimer. The number of near-native structures is used to estimate the probability of a dimer being biological. Currently, the server examines only the stability of a given interface rather than generating all putative quaternary structures as accomplished by PISA or EPPIC, but it complements the information provided by these methods.

Indexed as

Molecular Docking SimulationProtein Interaction MappingDatabases, ProteinEscherichia coliProtein ConformationProteinsX-RaysProteinsbiological dimercrystallographic dimerenergy landscapeinterface discriminationsolution structure

Identifiers

PMID27771482
PMCPMC5538892

What OpenQuestion holds

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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.