Evidence map›Paper›PMID 20204190›Full record

ReviewOrganic & biomolecular chemistry2010

Synthesis and biological applications of collagen-model triple-helical peptides.

Gregg B Fields

Abstract readReview
In one paragraph

Review in Organic & biomolecular chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 papers.

0numbers the graph read from it
0cells of the map it votes in
40citing 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

40 citing papers in PubMed.

  1. Article
  2. Article
  3. Around the collagen triple helix: an introduction to studying associated genetic and acquired diseases.Matrix biology : journal of the International Society for Matrix Biology · 2025
    Review
  4. Article
  5. Article
  6. Review
  7. Article
  8. Article
  9. Hollow Octadecameric Self-Assembly of Collagen-like Peptides.Journal of the American Chemical Society · 2023
    Article
  10. Article
  11. Article
  12. Peptide-Based Functional Biomaterials for Soft-Tissue Repair.Frontiers in bioengineering and biotechnology · 2019
    Review
  13. A pendant peptide endows a sunscreen with water-resistance.Organic & biomolecular chemistry · 2018
    Article
  14. Article
  15. Article
  16. Article
  17. Review
  18. Article
  19. Anchoring a cytoactive factor in a wound bed promotes healing.Journal of tissue engineering and regenerative medicine · 2016
    Article
  20. 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

1 author.

Gregg B FieldsUniversity of Texas Health Science Center, Department of Biochemistry, 7703 Floyd Curl Drive, San Antonio, TX 78229, USA. fieldsg@uthscsa.edu

Funding

Mechanism &Inhibition of Collagenolytic ActivityR01CA098799 · NCI · UNIVERSITY OF TEXAS HLTH SCIENCE CENTER · PI FIELDS, GREGG B · 2003 to 2017
$4.5M
TISSUE ENGINEERING USING PEPTIDE AMPHIPHILE BIOMIMETICSR01EB000289 · NIBIB · UNIVERSITY OF TEXAS HLTH SCIENCE CENTER · PI FIELDS, GREGG B · 2002 to 2008
$1.3M
NCI NIH HHS CA98799NCI NIH HHS R01 CA098799NIBIB NIH HHS EB000289NIBIB NIH HHS R01 EB000289NIMH NIH HHS MH078948
6 · The paper itself

Abstract

Triple-helical peptides (THPs) have been utilized as collagen models since the 1960s. The original focus for THP-based research was to unravel the structural determinants of collagen. In the last two decades, virtually all aspects of collagen structural biochemistry have been explored with THP models. More specifically, secondary amino acid analogs have been incorporated into THPs to more fully understand the forces that stabilize triple-helical structure. Heterotrimeric THPs have been utilized to better appreciate the contributions of chain sequence diversity on collagen function. The role of collagen as a cell signaling protein has been dissected using THPs that represent ligands for specific receptors. The mechanisms of collagenolysis have been investigated using THP substrates and inhibitors. Finally, THPs have been developed for biomaterial applications. These aspects of THP-based research are overviewed herein.

Indexed as

Models, MolecularAmino Acid SequenceAnimalsBiocompatible MaterialsCollagenHumansMolecular Sequence DataPeptidesProtein BindingProtein StabilityProtein Structure, SecondaryBiocompatible MaterialsCollagenPeptides

Identifiers

PMID20204190
PMCPMC3951274

What OpenQuestion holds

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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.