Evidence map›Paper›PMID 28232886›Full record

ArticleIntrinsically disordered proteins2015

An optimized N

Natsuko Goda, Naoki Matsuo, Takeshi Tenno, Sonoko Ishino, Yoshizumi Ishino, Satoshi Fukuchi, Motonori Ota, Hidekazu Hiroaki

Open access · bronzeAbstract read
In one paragraph

Article in Intrinsically disordered proteins, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
0.6field-weighted citation impact, top 30% 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

11 citing papers in PubMed, 22 citations in OpenAlex.

  1. Article
  2. Article
  3. Investigating Protein-Protein Interactions of Autophagy-Involved TNIP1.Methods in molecular biology (Clifton, N.J.) · 2025
    Article
  4. Article
  5. Article
  6. Article
  7. UsingProtein science : a publication of the Protein Society · 2018
    Article
  8. Article
  9. Review
  10. Article
  11. 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

8 authors at 5 institutions in 2 countries.

Natsuko GodaLaboratory of Structural Molecular Pharmacology; Graduate School of Pharmaceutical Sciences; Nagoya University; Furocho, Chikusa-ku, Nagoya, Japan; These authors equally contributed to the work.
Naoki MatsuoLaboratory of Structural Molecular Pharmacology; Graduate School of Pharmaceutical Sciences; Nagoya University; Furocho, Chikusa-ku, Nagoya, Japan; These authors equally contributed to the work.
Takeshi TennoLaboratory of Structural Molecular Pharmacology; Graduate School of Pharmaceutical Sciences; Nagoya University; Furocho, Chikusa-ku, Nagoya, Japan; The Structural Biology Research Center and Division of Biological Science; Graduate School of Science; Nagoya University; Furocho, Nagoya, Japan.
Sonoko IshinoDepartment of Bioscience and Biotechnology; Graduate School of Bioresource and Bioenvironmental Sciences and Faculty of Agriculture; Kyushu University ; Fukuoka, Japan.
Yoshizumi IshinoDepartment of Bioscience and Biotechnology; Graduate School of Bioresource and Bioenvironmental Sciences and Faculty of Agriculture; Kyushu University ; Fukuoka, Japan.
Satoshi FukuchiFaculty of Engineering, Maebashi Institute of Technology ; Maebashi, Japan.
Motonori OtaDepartment of Complex Systems Science; Graduate School of Information Sciences; Nagoya University ; Nagoya, Japan.
Hidekazu HiroakiLaboratory of Structural Molecular Pharmacology; Graduate School of Pharmaceutical Sciences; Nagoya University; Furocho, Chikusa-ku, Nagoya, Japan; The Structural Biology Research Center and Division of Biological Science; Graduate School of Science; Nagoya University; Furocho, Nagoya, Japan.
Kumamoto University · JPKyushu University · JPNagoya University · JPGraduate School USA · USMaebashi Institute of Technology · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Intrinsically disordered proteins (IDPs) are an emerging concept. IDPs have high flexibility in their polypeptide chains, lacking a stable 3-dimensional structure. Because of the difficulty in performing X-ray crystallography for IDPs, nuclear magnetic resonance (NMR) spectroscopy is the first choice for atomic-level investigation of their nature. Given that isotopically labeled IDP samples are necessary for NMR study, a robust and cost-effective protocol for bacterial expression and purification of IDP is also needed. We employed the N

Identifiers

PMID28232886
PMCPMC5314886
OpenAlexW2339549715

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.