Evidence map›Paper›PMID 28955897›Full record

ArticleBiochemistry and biophysics reports2016

Probing the polarity and water environment at the protein-peptide binding interface using tryptophan analogues.

Yi-Ting Chen, Wei-Chih Chao, Hsiou-Ting Kuo, Jiun-Yi Shen, I-Han Chen, Hsiao-Ching Yang, Jinn-Shyan Wang, Jyh-Feng Lu, Richard P Cheng, Pi-Tai Chou

Open access · goldAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Biochemistry and biophysics reports, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
0.5field-weighted citation impact, top 29% 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

4 citing papers in PubMed, 10 citations in OpenAlex.

  1. Unveiling the Excited State Dynamics of Indole in Solution.Journal of chemical theory and computation · 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

10 authors at 2 institutions in 1 country.

Yi-Ting ChenDepartment of Chemistry, National Taiwan University, Taipei 10617, Taiwan.
Wei-Chih ChaoDepartment of Chemistry, Fu-Jen Catholic University, New Taipei City 24205, Taiwan.
Hsiou-Ting KuoDepartment of Chemistry, National Taiwan University, Taipei 10617, Taiwan.
Jiun-Yi ShenDepartment of Chemistry, National Taiwan University, Taipei 10617, Taiwan.
I-Han ChenDepartment of Chemistry, National Taiwan University, Taipei 10617, Taiwan.
Hsiao-Ching YangDepartment of Chemistry, Fu-Jen Catholic University, New Taipei City 24205, Taiwan.
Jinn-Shyan WangSchool of Medicine, Fu-Jen Catholic University, New Taipei City 24205, Taiwan.
Jyh-Feng LuSchool of Medicine, Fu-Jen Catholic University, New Taipei City 24205, Taiwan.
Richard P ChengDepartment of Chemistry, National Taiwan University, Taipei 10617, Taiwan.
Pi-Tai ChouDepartment of Chemistry, National Taiwan University, Taipei 10617, Taiwan.
National Taiwan University · TWFu Jen Catholic University · TW

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

7-Azatryptophan and 2,7-diazatryptophan are sensitive to polarity changes and water content, respectively, and should be ideal for studying protein-protein and protein-peptide interactions. In this study, we replaced the tryptophan in peptide

Indexed as

CalmodulinCalmodulin binding peptideUnnatural tryptophan analoguesWater catalyzed excited state proton transfer

Identifiers

PMID28955897
PMCPMC5613298
OpenAlexW2408827919

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.