Evidence map›Paper›PMID 29590589›Full record

ArticleBiophysical journal2018

Molecular Mechanisms of Tight Binding through Fuzzy Interactions.

Qingliang Shen, Jie Shi, Danyun Zeng, Baoyu Zhao, Pingwei Li, Wonmuk Hwang, Jae-Hyun Cho

Open access · bronzeAbstract read
In one paragraph

Article in Biophysical journal, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.

0numbers the graph read from it
0cells of the map it votes in
9citing papers in PubMed
1.2field-weighted citation impact, top 21% 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

9 citing papers in PubMed, 19 citations in OpenAlex.

  1. Vital for Viruses: Intrinsically Disordered Proteins.Journal of molecular biology · 2023
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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

7 authors at 2 institutions in 2 countries.

Qingliang ShenDepartment of Biochemistry and Biophysics, Texas A&M University, College Station, Texas.
Jie ShiDepartment of Biomedical Engineering, Texas A&M University, College Station, Texas.
Danyun ZengDepartment of Biochemistry and Biophysics, Texas A&M University, College Station, Texas.
Baoyu ZhaoDepartment of Biochemistry and Biophysics, Texas A&M University, College Station, Texas.
Pingwei LiDepartment of Biochemistry and Biophysics, Texas A&M University, College Station, Texas.
Wonmuk HwangDepartment of Biomedical Engineering, Texas A&M University, College Station, Texas; Department of Materials Science and Engineering, Texas A&M University, College Station, Texas; School of Computational Sciences, Korea Institute for Advanced Study, Seoul, South Korea. Electronic address: hwm@tamu.edu.
Jae-Hyun ChoDepartment of Biochemistry and Biophysics, Texas A&M University, College Station, Texas. Electronic address: jaehyuncho@tamu.edu.
Texas A&M University · USKorea Institute for Advanced Study · KR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Many intrinsically disordered proteins (IDPs) form fuzzy complexes upon binding to their targets. Although many IDPs are weakly bound in fuzzy complexes, some IDPs form high-affinity complexes. One example is the nonstructural protein 1 (NS1) of the 1918 Spanish influenza A virus, which hijacks cellular CRKII through the strong binding affinity (K

Indexed as

Amino Acid MotifsIntrinsically Disordered ProteinsMolecular Dynamics SimulationProlineProtein BindingProtein DomainsStatic ElectricityIntrinsically Disordered ProteinsProline

Identifiers

PMID29590589
PMCPMC5883614
OpenAlexW2794527405

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.