Evidence map›Paper›PMID 23436394›Full record

ArticleBiopolymers2013

Exploring the structural requirements of collagen-binding peptides.

Wael R Abd-Elgaliel, Ching-Hsuan Tung

Open access · bronzeAbstract read
In one paragraph

Article in Biopolymers, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
0.2field-weighted citation impact, top 45% 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

1 citing paper in PubMed, 3 citations in OpenAlex.

  1. Review
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

2 authors at 1 institution in 1 country.

Wael R Abd-ElgalielDepartment of Translational Imaging, Methodist Hospital Research Institute, Weill Cornell Medical College, Houston, TX.
Ching-Hsuan Tung
Cornell University · US

Funding

Dendritic nanomedicine for cancer imaging and treatmentR01CA135312 · NCI · METHODIST HOSPITAL RESEARCH INSTITUTE · PI TUNG, CHING-HSUAN · 2008 to 2012
$1.5M
NCI NIH HHS CA135312NCI NIH HHS R01 CA135312
6 · The paper itself

Abstract

Collagen synthesis and tissue remodeling are involved in many diseases; therefore, collagen-specific binding agents have been developed to study collagen changes in various tissues. Based on a recently reported collagen binding peptide, which contains unnatural biphenylalanine (Bip) amino acid residue, constructs with various structure variations were synthesized to explore the contributions of unnatural Bip residue, conformational restrain, and amino acid sequence in collagen recognition. Their binding efficiency to collagens was evaluated in vitro using pure collagens. The results indicate that the C-terminal unnatural Bip residue, rather than the peptide sequence or conformational restrain, dominated the collagen I binding. Subsequent tissue binding study showed that the selected peptide did not offer preferential selectivity over collagen I in tissue, suggesting that a simple in vitro binding assay cannot adequately model the complex biological environment.

Indexed as

Amino Acid SequencePeptidesCollagenHumansMolecular Sequence DataProtein BindingCollagenPeptides

Identifiers

PMID23436394
PMCPMC3637416
OpenAlexW1606561897

What OpenQuestion holds

Textmetadata
LicenceTDM
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.