Evidence map›Paper›PMID 27159632›Full record

ArticleJournal of computational biology : a journal of computational molecular cell biology2016

Constructing Structure Ensembles of Intrinsically Disordered Proteins from Chemical Shift Data.

Huichao Gong, Sai Zhang, Jiangdian Wang, Haipeng Gong, Jianyang Zeng

Open access · greenAbstract read
In one paragraph

Article in Journal of computational biology : a journal of computational molecular cell biology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing papers in PubMed
2.2field-weighted citation impact, top 12% 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

5 citing papers in PubMed, 12 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Review
  5. Constructing Structure Ensembles of Intrinsically Disordered Proteins from Chemical Shift Data.Journal of computational biology : a journal of computational molecular cell biology · 2016
    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 1 institution in 1 country.

Huichao Gong1 Institute for Interdisciplinary Information Sciences, Tsinghua University , Beijing, China .
Sai Zhang1 Institute for Interdisciplinary Information Sciences, Tsinghua University , Beijing, China .
Jiangdian Wang2 Biostatistics and Research Decision Sciences-Asia Pacific, Merck Research Laboratory , Beijing, China .
Haipeng Gong3 School of Life Sciences, Tsinghua University , Beijing, China .
Jianyang Zeng1 Institute for Interdisciplinary Information Sciences, Tsinghua University , Beijing, China .
Tsinghua University · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Modeling the structural ensemble of intrinsically disordered proteins (IDPs), which lack fixed structures, is essential in understanding their cellular functions and revealing their regulation mechanisms in signaling pathways of related diseases (e.g., cancers and neurodegenerative disorders). Though the ensemble concept has been widely believed to be the most accurate way to depict 3D structures of IDPs, few of the traditional ensemble-based approaches effectively address the degeneracy problem that occurs when multiple solutions are consistent with experimental data and is the main challenge in the IDP ensemble construction task. In this article, based on a predefined conformational library, we formalize the structure ensemble construction problem into a least squares framework, which provides the optimal solution when the data constraints outnumber unknown variables. To deal with the degeneracy problem, we further propose a regularized regression approach based on the elastic net technique with the assumption that the weights to be estimated for individual structures in the ensemble are sparse. We have validated our methods through a reference ensemble approach as well as by testing the real biological data of three proteins, including alpha-synuclein, the translocation domain of Colocin N, and the K18 domain of Tau protein.

Indexed as

Computational BiologyHumansIntrinsically Disordered ProteinsModels, MolecularNuclear Magnetic Resonance, BiomolecularProtein ConformationIntrinsically Disordered Proteinschemical shiftelastic netintrinsically disordered proteinsleast squares

Identifiers

PMID27159632
PMCPMC4876552
OpenAlexW2345702771

What OpenQuestion holds

Textmetadata
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.