Evidence map›Paper›PMID 26404856›Full record

ArticleProteins2015

Extension of a protein docking algorithm to membranes and applications to amyloid precursor protein dimerization.

Shruthi Viswanath, Laura Dominguez, Leigh S Foster, John E Straub, Ron Elber

Abstract read
In one paragraph

Article in Proteins, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing 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

10 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Review
  6. Article
  7. Transmembrane Protein Docking with JabberDock.Journal of chemical information and modeling · 2021
    Article
  8. Article
  9. Article
  10. Structure of APP-C99Biochimica et biophysica acta. Biomembranes · 2018
    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

5 authors.

Shruthi ViswanathDepartment of Computer Science, University of Texas at Austin, Austin, Texas, 78712.
Laura DominguezDepartment of Chemistry, Boston University, Boston, Massachusetts, 02215.
Leigh S FosterDepartment of Chemistry, Boston University, Boston, Massachusetts, 02215.
John E StraubDepartment of Chemistry, Boston University, Boston, Massachusetts, 02215.
Ron ElberInstitute for Computational Engineering and Sciences, University of Texas at Austin, Austin, Texas, 78712.

Funding

LONG TIME DYNAMICS OF BIOMOLECULESR01GM059796 · NIGMS · UNIVERSITY OF TEXAS AT AUSTIN · PI ELBER, RON · 2000 to 2021
$5.7M
Probing the roles of membrane and cholesterol on Aβ biogenesis and prion protein interactionsR01GM107703 · NIGMS · BOSTON UNIVERSITY (CHARLES RIVER CAMPUS) · PI STRAUB, JOHN E., THIRUMALAI, DEVARAJAN · 2015 to 2022
$2.7M
Optimization of Stuctures and Networks of ProteinsR01GM067823 · NIGMS · UNIVERSITY OF TEXAS AT AUSTIN · PI ELBER, RON · 2004 to 2010
$1.9M
Probing the Principles Governing Protein AggregationR01GM076688 · NIGMS · BOSTON UNIVERSITY (CHARLES RIVER CAMPUS) · PI STRAUB, JOHN E. · 2006 to 2009
$1.5M
NIGMS NIH HHS R01 GM059796NIGMS NIH HHS R01 GM067823NIGMS NIH HHS R01 GM076688NIGMS NIH HHS R01 GM107703
6 · The paper itself

Abstract

Novel adjustments are introduced to the docking algorithm, DOCK/PIERR, for the purpose of predicting structures of transmembrane protein complexes. Incorporating knowledge about the membrane environment is shown to significantly improve docking accuracy. The extended version of DOCK/PIERR is shown to perform comparably to other leading docking packages. This membrane version of DOCK/PIERR is applied to the prediction of coiled-coil homodimer structures of the transmembrane region of the C-terminal peptide of amyloid precursor protein (C99). Results from MD simulation of the C99 homodimer in POPC bilayer and docking are compared. Docking results are found to capture key aspects of the homodimer ensemble, including the existence of three topologically distinct conformers. Furthermore, the extended version of DOCK/PIERR is successful in capturing the effects of solvation in membrane and micelle. Specifically, DOCK/PIERR reproduces essential differences in the homodimer ensembles simulated in POPC bilayer and DPC micelle, where configurational entropy and surface curvature effects bias the handedness and topology of the homodimer ensemble.

Indexed as

AlgorithmsAmyloid beta-Protein PrecursorCell MembraneEntropyLipid BilayersMicellesMolecular Docking SimulationMolecular Dynamics SimulationPhosphatidylcholinesProtein Multimerization1-palmitoyl-2-oleoylphosphatidylcholineAmyloid beta-Protein PrecursorLipid BilayersMicellesPhosphatidylcholinesall-atom MD simulationamyloid precursor proteinexplicit and implicit solventmembrane potentialmicelle and bilayer environmentsprotein-protein dockingtransmembrane complexes

Identifiers

PMID26404856
PMCPMC4715591

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.