Evidence map›Paper›PMID 29986141›Full record

ReviewJournal of medicinal chemistry2018

Collagen Prolyl 4-Hydroxylase as a Therapeutic Target.

James D Vasta, Ronald T Raines

Open access · greenAbstract readReview
In one paragraph

Review in Journal of medicinal chemistry, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 50 papers.

0numbers the graph read from it
0cells of the map it votes in
50citing papers in PubMed
5.7field-weighted citation impact, top 4% 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

50 citing papers in PubMed, 77 citations in OpenAlex.

  1. Collagen Prolyl 4-Hydroxylase: An Emerging Key Player in Cardiac Fibrosis.Journal of cardiovascular translational research · 2026
    Review
  2. Article
  3. The Regulatory Role of Iron Transporter SLC39A13 in Liver Fibrosis.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026
    Article
  4. Review
  5. Article
  6. Therapy-Induced ECM Remodeling Creates a Transient Immune Barrier in Residual Melanoma.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025
    Article
  7. Article
  8. Article
  9. Article
  10. Review
  11. 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
  12. Article
  13. Review
  14. Article
  15. Article
  16. Comprehensive analysis of the effects ofFrontiers in cell and developmental biology · 2025
    Article
  17. Article
  18. Article
  19. Review
  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

2 authors at 2 institutions in 1 country.

James D Vasta
Ronald T RainesDepartment of Chemistry , Massachusetts Institute of Technology , Cambridge , Massachusetts 02139 , United States.ORCID 0000-0001-7164-1719
Massachusetts Institute of Technology · USUniversity of Wisconsin–Madison · US

Funding

GRADUATE TRAINING IN MOLECULAR BIOSCIENCEST32GM007215 · NIGMS · UNIVERSITY OF WISCONSIN-MADISON · PI HULL, CHRISTINA M · 1985 to 2018
$22.5M
COLLAGEN STRUCTURE AND STABILITY IN VITRO AND IN VIVOR01AR044276 · NIAMS · UNIVERSITY OF WISCONSIN-MADISON · PI RAINES, RONALD T · 1996 to 2017
$5.6M
NIAMS NIH HHS R01 AR044276NIGMS NIH HHS T32 GM007215
6 · The paper itself

Abstract

Collagen is the dominant protein of the extracellular matrix. Its distinguishing feature is a three-stranded helix of great tensile strength. (2 S,4 R)-4-Hydroxyproline residues are essential for the stability of this triple helix. These residues arise from the post-translational modification of (2 S)-proline residues by collagen prolyl 4-hydroxylases (CP4Hs), which are members of the Fe(II)- and α-ketoglutarate (AKG)-dependent dioxygenase family. Here, we provide a framework for the inhibition of CP4Hs as the basis for treating fibrotic diseases and cancer metastasis. We begin with a summary of the structure and enzymatic reaction mechanism of CP4Hs. Then, we review the metal ions, metal chelators, mimetics of AKG and collagen strands, and natural products that are known to inhibit CP4Hs. Our focus is on inhibitors with potential utility in the clinic. We conclude with a prospectus for more effective inhibitors.

Indexed as

AnimalsCollagenHumansMolecular Targeted TherapyProlyl-Hydroxylase InhibitorsProlyl HydroxylasesCollagenProlyl-Hydroxylase InhibitorsProlyl Hydroxylases

Identifiers

PMID29986141
PMCPMC6344319
OpenAlexW2869462691

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.