Evidence map›Paper›PMID 33674390›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2021

Collagen's enigmatic, highly conserved

Rasia C Li, Madeline Y Wong, Andrew S DiChiara, Azade S Hosseini, Matthew D Shoulders

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
1.4field-weighted citation impact, top 19% 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

18 citing papers in PubMed, 22 citations in OpenAlex.

  1. Article
  2. Article
  3. Collagen IV biosynthesis: Intracellular choreography of post-translational modifications.Matrix biology : journal of the International Society for Matrix Biology · 2025
    Review
  4. Review
  5. The life cycle of type IV collagen.Matrix biology : journal of the International Society for Matrix Biology · 2025
    Review
  6. [Research progress on collagen secretion mechanisms in scarring].Zhejiang da xue xue bao. Yi xue ban = Journal of Zhejiang University. Medical sciences · 2025
    Review
  7. Review
  8. Article
  9. Article
  10. An outcome-defining role for the triple-helical domain in regulating collagen-I assembly.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  11. Article
  12. Review
  13. Review
  14. Article
  15. Article
  16. Review
  17. Article
  18. 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

5 authors at 1 institution in 1 country.

Rasia C LiDepartment of Chemistry, Massachusetts Institute of Technology, Cambridge, MA 02139.
Madeline Y WongDepartment of Chemistry, Massachusetts Institute of Technology, Cambridge, MA 02139.
Andrew S DiChiaraDepartment of Chemistry, Massachusetts Institute of Technology, Cambridge, MA 02139.ORCID 0000-0002-9438-0643
Azade S HosseiniDepartment of Chemistry, Massachusetts Institute of Technology, Cambridge, MA 02139.
Matthew D ShouldersDepartment of Chemistry, Massachusetts Institute of Technology, Cambridge, MA 02139 mshoulde@mit.edu.
Massachusetts Institute of Technology · US

Funding

TOXICOLOGY CORE UNITP30ES002109 · NIEHS · MASSACHUSETTS INSTITUTE OF TECHNOLOGY · PI ENGELWARD, BEVIN P. · 1985 to 2020
$25.6M
Defining and Modulating Mechanisms of Collagen ProteostasisR01AR071443 · NIAMS · MASSACHUSETTS INSTITUTE OF TECHNOLOGY · PI SHOULDERS, MATTHEW DONALD · 2017 to 2021
$1.7M
A Novel Approach to Osteogenesis Imperfecta_ The Collagen Protein Folding ProblemF31AR067615 · NIAMS · MASSACHUSETTS INSTITUTE OF TECHNOLOGY · PI DICHIARA, ANDREW STEPHEN · 2015 to 2017
$127k
NIAMS NIH HHS F31 AR067615NIAMS NIH HHS R01 AR071443NIEHS NIH HHS P30 ES002109
6 · The paper itself

Abstract

Intracellular procollagen folding begins at the protein's C-terminal propeptide (C-Pro) domain, which initiates triple-helix assembly and defines the composition and chain register of fibrillar collagen trimers. The C-Pro domain is later proteolytically cleaved and excreted from the body, while the mature triple helix is incorporated into the extracellular matrix. The procollagen C-Pro domain possesses a single

Indexed as

ProteostasisCollagenExtracellular MatrixGlycosylationHumansProcollagenProtein DomainsProteoglycansCollagenglycosylated collagenProcollagenProteoglycanscalnexin and calreticulincollagen folding and proteostasisER protein foldingextracellular matrix biosynthesisN-glycosylation

Identifiers

PMID33674390
PMCPMC7958235
OpenAlexW3134325625

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.