Evidence map›Paper›PMID 18845531›Full record

ArticleThe Journal of biological chemistry2008

Trimerization and triple helix stabilization of the collagen XIX NC2 domain.

Sergei P Boudko, Jürgen Engel, Hans Peter Bächinger

Abstract read
In one paragraph

Article in The Journal of biological chemistry, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing 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

20 citing papers in PubMed.

  1. 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
  2. Article
  3. Review
  4. Article
  5. Review
  6. Article
  7. Reversible Covalent End-Capping of Collagen Model Peptides.Chemistry (Weinheim an der Bergstrasse, Germany) · 2019
    Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. The collagen family.Cold Spring Harbor perspectives in biology · 2011
    Review
  15. Article
  16. Article
  17. Kinetic hysteresis in collagen folding.Biophysical journal · 2010
    Article
  18. Article
  19. 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

3 authors.

Sergei P BoudkoResearch Department, Shriners Hospital for Children, Portland, Oregon 97239, USA.
Jürgen Engel
Hans Peter Bächinger

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The mechanisms of chain selection and assembly of fibril-associated collagens with interrupted triple helices (FACITs) must differ from that of fibrillar collagens, since they lack the characteristic C-propeptide. We analyzed two carboxyl-terminal noncollagenous domains, NC2 and NC1, of collagen XIX as potential trimerization units and found that NC2 forms a stable trimer and substantially stabilizes a collagen triple helix attached to either end. In contrast, the NC1 domain requires formation of an adjacent collagen triple helix to form interchain disulfide bridges. The NC2 domain of collagen XIX and probably of other FACITs is responsible for chain selection and trimerization.

Indexed as

Amino Acid SequenceAnimalsBiophysicsCollagenDimerizationDisulfidesFibril-Associated CollagensFibrillar CollagensHumansMiceMolecular Sequence DataOxygenPeptidesProtein Structure, TertiarySequence Homology, Amino AcidThermodynamicsCOL19A1 protein, humancol19a1 protein, mouseCollagenDisulfidesFibril-Associated CollagensFibrillar CollagensOxygenPeptides

Identifiers

PMID18845531
PMCPMC2662240

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.