Evidence map›Paper›PMID 31697428›Full record

ArticleProteins2020

Performance and enhancement of the LZerD protein assembly pipeline in CAPRI 38-46.

Charles Christoffer, Genki Terashi, Woong-Hee Shin, Tunde Aderinwale, Sai Raghavendra Maddhuri Venkata Subramaniya, Lenna Peterson, Jacob Verburgt, Daisuke Kihara

Abstract read
In one paragraph

Article in Proteins, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing 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

12 citing papers in PubMed.

  1. Article
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  11. Advances to tackle backbone flexibility in protein docking.Current opinion in structural biology · 2021
    Review
  12. LZerD Protein-Protein Docking Webserver Enhanced WithFrontiers in molecular biosciences · 2021
    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

8 authors.

Charles ChristofferDepartment of Computer Science, Purdue University, West Lafayette, Indiana.ORCID 0000-0002-6163-6323
Genki TerashiDepartment of Biological Sciences, Purdue University, West Lafayette, Indiana.
Woong-Hee ShinDepartment of Biological Sciences, Purdue University, West Lafayette, Indiana.
Tunde AderinwaleDepartment of Computer Science, Purdue University, West Lafayette, Indiana.
Sai Raghavendra Maddhuri Venkata SubramaniyaDepartment of Computer Science, Purdue University, West Lafayette, Indiana.
Lenna PetersonDepartment of Biological Sciences, Purdue University, West Lafayette, Indiana.
Jacob VerburgtDepartment of Biological Sciences, Purdue University, West Lafayette, Indiana.
Daisuke KiharaDepartment of Computer Science, Purdue University, West Lafayette, Indiana.ORCID 0000-0003-4091-6614

Funding

Purdue University Molecular Biophysics Training ProgramT32GM132024 · NIGMS · PURDUE UNIVERSITY · PI Angeline Marie Lyon, John Tesmer · 2019 to 2026
$2.0M
Structural Modeling of Multifarious Protein ComplexesR01GM123055 · NIGMS · PURDUE UNIVERSITY · PI KIHARA, DAISUKE · 2017 to 2020
$1.2M
NIGMS NIH HHS R01 GM123055NIGMS NIH HHS T32 GM132024NIGMS NIH HHS T32GM132024NIH HHS R01GM123055
6 · The paper itself

Abstract

We report the performance of the protein docking prediction pipeline of our group and the results for Critical Assessment of Prediction of Interactions (CAPRI) rounds 38-46. The pipeline integrates programs developed in our group as well as other existing scoring functions. The core of the pipeline is the LZerD protein-protein docking algorithm. If templates of the target complex are not found in PDB, the first step of our docking prediction pipeline is to run LZerD for a query protein pair. Meanwhile, in the case of human group prediction, we survey the literature to find information that can guide the modeling, such as protein-protein interface information. In addition to any literature information and binding residue prediction, generated docking decoys were selected by a rank aggregation of statistical scoring functions. The top 10 decoys were relaxed by a short molecular dynamics simulation before submission to remove atom clashes and improve side-chain conformations. In these CAPRI rounds, our group, particularly the LZerD server, showed robust performance. On the other hand, there are failed cases where some other groups were successful. To understand weaknesses of our pipeline, we analyzed sources of errors for failed targets. Since we noted that structure refinement is a step that needs improvement, we newly performed a comparative study of several refinement approaches. Finally, we show several examples that illustrate successful and unsuccessful cases by our group.

Indexed as

Molecular Docking SimulationSoftwareAlgorithmsAmino Acid SequenceBinding SitesHumansLigandsPeptidesProtein BindingProtein Conformation, alpha-HelicalProtein Conformation, beta-StrandProtein Interaction Domains and MotifsProtein Interaction MappingProteinsResearch DesignStructural Homology, ProteinLigandsPeptidesProteinsCAPRILZerDprotein assemblyprotein complex modelingprotein dockingprotein-protein interactionprotein structure prediction

Identifiers

PMID31697428
PMCPMC7685511

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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.