Evidence map›Paper›PMID 28280526›Full record

ArticleComputational and structural biotechnology journal2017

Protein Structure Classification and Loop Modeling Using Multiple Ramachandran Distributions.

Seyed Morteza Najibi, Mehdi Maadooliat, Lan Zhou, Jianhua Z Huang, Xin Gao

Open access · goldAbstract read
In one paragraph

Article in Computational and structural biotechnology journal, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
1.2field-weighted citation impact, top 22% of its field
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

3 citing papers in PubMed, 26 citations in OpenAlex.

  1. Mechanistic insights into ligand selectivity inActa pharmaceutica Sinica. B · 2026
    Article
  2. Exploring the Inhibitory Potential ofTheScientificWorldJournal · 2024
    Article
  3. 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 at 4 institutions in 3 countries.

Seyed Morteza NajibiDepartment of Statistics, College of Sciences, Shiraz University, Shiraz, Iran.
Mehdi MaadooliatDepartment of Mathematics, Statistics and Computer Science, Marquette University, WI 53201-1881, USA; Center for Human Genetics, Marshfield Clinic Research Institute, Marshfield, WI 54449, USA.
Lan ZhouDepartment of Statistics, Texas A&M University, TX 77843-3143, USA.
Jianhua Z HuangDepartment of Statistics, Texas A&M University, TX 77843-3143, USA.
Xin GaoComputational Bioscience Research Center (CBRC), Computer, Electrical and Mathematical Sciences and Engineering Division, King Abdullah University of Science and Technology (KAUST), Thuwal 23955-6900, Saudi Arabia.
Texas A&M University · USKing Abdullah University of Science and Technology · SAMarquette University · USShiraz University · IR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Recently, the study of protein structures using angular representations has attracted much attention among structural biologists. The main challenge is how to efficiently model the continuous conformational space of the protein structures based on the differences and similarities between different Ramachandran plots. Despite the presence of statistical methods for modeling angular data of proteins, there is still a substantial need for more sophisticated and faster statistical tools to model the large-scale circular datasets. To address this need, we have developed a nonparametric method for collective estimation of multiple bivariate density functions for a collection of populations of protein backbone angles. The proposed method takes into account the circular nature of the angular data using trigonometric spline which is more efficient compared to existing methods. This collective density estimation approach is widely applicable when there is a need to estimate multiple density functions from different populations with common features. Moreover, the coefficients of adaptive basis expansion for the fitted densities provide a low-dimensional representation that is useful for visualization, clustering, and classification of the densities. The proposed method provides a novel and unique perspective to two important and challenging problems in protein structure research: structure-based protein classification and angular-sampling-based protein loop structure prediction.

Indexed as

Bivariate splinesLog-spline density estimationProtein classificationProtein structureRamachandran distributionRoughness penaltySCOPTrigonometric B-spline

Identifiers

PMID28280526
PMCPMC5331158
OpenAlexW2586883482

What OpenQuestion holds

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LicenceCC BY
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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.