Evidence map›Paper›PMID 27799304›Full record

ArticleThe Journal of biological chemistry2016

Consequences of Glycine Mutations in the Fibronectin-binding Sequence of Collagen.

Panharith Chhum, Hongtao Yu, Bo An, Brian R Doyon, Yu-Shan Lin, Barbara Brodsky

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
1.8field-weighted citation impact, top 16% 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

15 citing papers in PubMed, 24 citations in OpenAlex.

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  4. Review
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  6. Review
  7. Contrasting Local and Macroscopic Effects of Collagen Hydroxylation.International journal of molecular sciences · 2021
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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

6 authors at 1 institution in 1 country.

Panharith ChhumFrom the Departments of Biomedical Engineering and.
Hongtao YuFrom the Departments of Biomedical Engineering and.
Bo AnFrom the Departments of Biomedical Engineering and.
Brian R DoyonFrom the Departments of Biomedical Engineering and.
Yu-Shan LinChemistry, Tufts University, Medford, Massachusetts 02155 Yu-Shan.Lin@tufts.edu.
Barbara BrodskyFrom the Departments of Biomedical Engineering and Barbara.Brodsky@tufts.edu.
Tufts University · US

Funding

Stuctural studies of triple-helical proteinsR01GM060048 · NIGMS · UNIV OF MED/DENT NJ-R W JOHNSON MED SCH · PI BRODSKY, BARBARA M · 1999 to 2016
$5.1M
NIGMS NIH HHS R01 GM060048
6 · The paper itself

Abstract

Collagen and fibronectin (Fn) are two key extracellular matrix proteins, which are known to interact and jointly shape matrix structure and function. Most proteins that interact with collagen bind only to the native triple-helical form, whereas Fn is unusual in binding strongly to denatured collagen and more weakly to native collagen. The consequences of replacing a Gly by Ser at each position in the required (Gly-Xaa-Yaa)

Indexed as

Amino Acid SequenceBinding SitesCircular DichroismCollagen Type ICollagen Type IICrystallography, X-RayFibronectinsGlycineHumansMutant ProteinsMutationProtein BindingProtein ConformationCollagen Type ICollagen Type IIFibronectinsFN1 protein, humanGlycineMutant Proteinscollagenextracellular matrixextracellular matrix proteinfibronectinmolecular dynamicsmutationosteogenesis imperfectapeptidesrecombinant protein expression

Identifiers

PMID27799304
PMCPMC5207138
OpenAlexW2543413412

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.