Evidence map›Paper›PMID 30098073›Full record

ArticleProtein science : a publication of the Protein Society2018

Using

Hiroki Okazaki, Naoki Matsuo, Takeshi Tenno, Natsuko Goda, Yoshiki Shigemitsu, Motonori Ota, Hidekazu Hiroaki

Abstract read
In one paragraph

Article in Protein science : a publication of the Protein Society, 2018. 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
–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

5 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Temperature dependence of NMR chemical shifts: Tracking and statistical analysis.Protein science : a publication of the Protein Society · 2020
    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

7 authors.

Hiroki OkazakiDepartment of Complex Systems Science, Graduate School of Information Sciences, Nagoya University, Nagoya, 464-8601, Japan.
Naoki MatsuoLaboratory of Structural Molecular Pharmacology, Graduate School of Pharmaceutical Sciences, Nagoya University, Nagoya, 464-8601, Japan.
Takeshi TennoLaboratory of Structural Molecular Pharmacology, Graduate School of Pharmaceutical Sciences, Nagoya University, Nagoya, 464-8601, Japan.
Natsuko GodaLaboratory of Structural Molecular Pharmacology, Graduate School of Pharmaceutical Sciences, Nagoya University, Nagoya, 464-8601, Japan.
Yoshiki ShigemitsuLaboratory of Structural Molecular Pharmacology, Graduate School of Pharmaceutical Sciences, Nagoya University, Nagoya, 464-8601, Japan.
Motonori OtaDepartment of Complex Systems Science, Graduate School of Information Sciences, Nagoya University, Nagoya, 464-8601, Japan.
Hidekazu HiroakiLaboratory of Structural Molecular Pharmacology, Graduate School of Pharmaceutical Sciences, Nagoya University, Nagoya, 464-8601, Japan.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

This report describes a cost-effective experimental method for determining an intrinsically disordered protein (IDP) region in a given protein sample. In this area, the most popular (and conventional) means is using the amide (

Indexed as

Nuclear Magnetic Resonance, BiomolecularProtonsTemperatureAmidesIntrinsically Disordered ProteinsProtein ConformationAmidesIntrinsically Disordered ProteinsProtonschemical shift temperature coefficienthydrogen bondintrinsically disordered proteinnuclear magnetic resonance

Identifiers

PMID30098073
PMCPMC6199157

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.