Evidence map›Paper›PMID 20306218›Full record

ArticleJournal of computer-aided molecular design2010

Docking study of the precursor peptide of mastoparan onto its putative processing enzyme, dipeptidyl peptidase IV: a revisit to molecular ticketing.

Soonmin Jang, Tse-Yu Chung, Jungho Shin, Kai-Lun Lin, Jason T C Tzen, Feng-Yin Li

Abstract read
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In one paragraph

Article in Journal of computer-aided molecular design, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing 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

2 citing papers in PubMed.

  1. Article
  2. 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

6 authors.

Soonmin JangDepartment of Chemistry and Institute for Chemical Biology, Sejong University, Seoul, 143-747, Korea.
Tse-Yu Chung
Jungho Shin
Kai-Lun Lin
Jason T C Tzen
Feng-Yin Li

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Stepwise-cleavage process of promastoparans to reach maturity was investigated theoretically by combining ab initio folding and unbounded docking. The comparison between the structures of the promastoparans both before and after docking were examined along with the hydrogen bonding interaction pattern between the dipetidyl peptidase IV (DPPIV) and promastoparans to reveal how the endpoint of this stepwise cleavage is recognized among these promastoparans with highly resemble amino acid sequences. The current approach of folding and docking study provides structural insight on the stepwise cleavage process.

Indexed as

Molecular Dynamics SimulationAmino Acid SequenceDipeptidyl Peptidase 4Hydrogen BondingIntercellular Signaling Peptides and ProteinsMolecular Sequence DataPeptidesProtein BindingProtein FoldingSurface-Active AgentsWasp VenomsDipeptidyl Peptidase 4Intercellular Signaling Peptides and ProteinsmastoparanPeptidesSurface-Active AgentsWasp Venoms

Identifiers

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.