Evidence map›Paper›PMID 26221066›Full record

ArticleTsinghua science and technology2015

A New Hidden Markov Model for Protein Quality Assessment Using Compatibility Between Protein Sequence and Structure.

Zhiquan He, Wenji Ma, Jingfen Zhang, Dong Xu

Abstract read
In one paragraph

Article in Tsinghua science and technology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing 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

2 citing papers in PubMed.

  1. MUfoldQA_G: High-accuracy protein model QA via retraining and transformation.Computational and structural biotechnology journal · 2021
    Article
  2. Two New Heuristic Methods for Protein Model Quality Assessment.IEEE/ACM transactions on computational biology and bioinformatics
    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

4 authors.

Zhiquan HeDepartment of Computer Science and Christopher S. Bond Life Sciences Center, University of Missouri, MO 65211, USA. zhy78@mizzou.edu.
Wenji MaChristopher S. Bond Life Sciences Center, University of Missouri, MO 65211, USA and Department of Computer Science, City University of Hong Kong, Hong Kong, China. wenjima821@gmail.com.
Jingfen ZhangDepartment of Computer Science and Christopher S. Bond Life Sciences Center, University of Missouri, MO 65211, USA. zhangjingf@gmail.com.
Dong XuDepartment of Computer Science and Christopher S. Bond Life Sciences Center, University of Missouri, MO 65211, USA.

Funding

Development of MUFOLD for Building High-Accuracy Protein Structure ModelsR01GM100701 · NIGMS · UNIVERSITY OF MISSOURI-COLUMBIA · PI XU, DONG · 2012 to 2016
$1.4M
New Scoring, Assembly and Evaulation Techiniques for Protein Structure PredictionR33GM078601 · NIGMS · UNIVERSITY OF MISSOURI-COLUMBIA · PI XU, DONG · 2008 to 2010
$659k
New Scoring, Assembly and Evaulation Techiniques for Protein Structure PredictionR21GM078601 · NIGMS · UNIVERSITY OF MISSOURI-COLUMBIA · PI XU, DONG · 2006 to 2007
$280k
NIGMS NIH HHS R01 GM100701NIGMS NIH HHS R21 GM078601NIGMS NIH HHS R33 GM078601
6 · The paper itself

Abstract

Protein structure Quality Assessment (QA) is an essential component in protein structure prediction and analysis. The relationship between protein sequence and structure often serves as a basis for protein structure QA. In this work, we developed a new Hidden Markov Model (HMM) to assess the compatibility of protein sequence and structure for capturing their complex relationship. More specifically, the emission of the HMM consists of protein local structures in angular space, secondary structures, and sequence profiles. This model has two capabilities: (1) encoding local structure of each position by jointly considering sequence and structure information, and (2) assigning a global score to estimate the overall quality of a predicted structure, as well as local scores to assess the quality of specific regions of a structure, which provides useful guidance for targeted structure refinement. We compared the HMM model to state-of-art single structure quality assessment methods OPUSCA, DFIRE, GOAP, and RW in protein structure selection. Computational results showed our new score HMM.Z can achieve better overall selection performance on the benchmark datasets.

Indexed as

Hidden Markov Model (HMM)protein structure predictionstructure quality assessment

Identifiers

PMID26221066
PMCPMC4515432

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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.