Evidence map›Paper›PMID 21541061›Full record

ArticleInternational journal of molecular sciences2011

Accounting for large amplitude protein deformation during in silico macromolecular docking.

Karine Bastard, Adrien Saladin, Chantal Prévost

Abstract read
In one paragraph

Article in International journal of molecular sciences, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing 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

4 citing papers in PubMed.

  1. Review
  2. Pushing the Backbone in Protein-Protein Docking.Structure (London, England : 1993) · 2016
    Article
  3. Article
  4. 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

3 authors.

Karine BastardLABIS, Genoscope, CEA, 2 rue Gaston Cremieux, F-91057 Evry Cedex, France; E-Mail: kbastard@genoscope.cns.fr.
Adrien Saladin
Chantal Prévost

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Rapid progress of theoretical methods and computer calculation resources has turned in silico methods into a conceivable tool to predict the 3D structure of macromolecular assemblages, starting from the structure of their separate elements. Still, some classes of complexes represent a real challenge for macromolecular docking methods. In these complexes, protein parts like loops or domains undergo large amplitude deformations upon association, thus remodeling the surface accessible to the partner protein or DNA. We discuss the problems linked with managing such rearrangements in docking methods and we review strategies that are presently being explored, as well as their limitations and success.

Indexed as

AlgorithmsAmino Acid SequenceDNA-Binding ProteinsMolecular Docking SimulationMolecular Dynamics SimulationMolecular Sequence DataDNA-Binding Proteinsflexibilitymacromolecular dockingprotein loops and domains

Identifiers

PMID21541061
PMCPMC3083708

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.