Evidence map›Paper›PMID 27183028›Full record

ArticleBiochemistry2016

Human Collagen Prolyl 4-Hydroxylase Is Activated by Ligands for Its Iron Center.

James D Vasta, Ronald T Raines

Abstract read
In one paragraph

Article in Biochemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
1.0field-weighted citation impact, top 25% 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

17 citing papers in PubMed, 28 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Review
  6. Article
  7. Article
  8. Article
  9. Review
  10. Roxadustat: Not just for anemia.Frontiers in pharmacology · 2022
    Review
  11. Collagen release by human hepatic stellate cells requires vitamin C and is efficiently blocked by hydroxylase inhibition.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2021
    Article
  12. Review
  13. Roles of vitamins in stem cells.Cellular and molecular life sciences : CMLS · 2020
    Review
  14. Collagen Prolyl 4-Hydroxylase as a Therapeutic Target.Journal of medicinal chemistry · 2018
    Review
  15. Article
  16. Article
  17. 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 1 institution in 1 country.

James D VastaDepartment of Biochemistry and ‡Department of Chemistry, University of Wisconsin-Madison , Madison, Wisconsin 53706, United States.
Ronald T RainesDepartment of Biochemistry and ‡Department of Chemistry, University of Wisconsin-Madison , Madison, Wisconsin 53706, United States.
University of Wisconsin–Madison · US

Funding

GRADUATE TRAINING IN MOLECULAR BIOSCIENCEST32GM007215 · NIGMS · UNIVERSITY OF WISCONSIN-MADISON · PI HULL, CHRISTINA M · 1985 to 2018
$22.5M
TR&D 3: TECHNOLOGY DEVELOPMENT FOR NMR STUDIES OF SMALL MOLECULES (METABOLOMICS, NATURAL PRODUCTS, METABOLITE-PROTEIN INTERACTIONS) pp.537-585 P41GM103399 · NIGMS · UNIVERSITY OF WISCONSIN-MADISON · PI MARKLEY, JOHN LUTE · 2012 to 2019
$9.4M
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 P41 GM103399NIGMS NIH HHS T32 GM007215
6 · The paper itself

Abstract

Collagen is the most abundant protein in animals. The posttranslational hydroxylation of proline residues in collagen contributes greatly to its conformational stability. Deficient hydroxylation is associated with a variety of disease states, including scurvy. The hydroxylation of proline residues in collagen is catalyzed by an Fe(II)- and α-ketoglutarate-dependent dioxygenase, collagen prolyl 4-hydroxylase (CP4H). CP4H has long been known to suffer oxidative inactivation during catalysis, and the cofactor ascorbate (vitamin C) is required to reactivate the enzyme by reducing its iron center from Fe(III) to Fe(II). Herein, we report on the discovery of the first synthetic activators of CP4H. Specifically, we find that 2,2'-bipyridine-4-carboxylate and 2,2'-bipyridine-5-carboxylate serve as ligands for the iron center in human CP4H that enhance the rate of ascorbate-dependent reactivation. This new mode of CP4H activation is available to other biheteroaryl compounds but does not necessarily extend to other prolyl 4-hydroxylases. As collagen is weakened in many indications, analogous activators of CP4H could have therapeutic benefits.

Indexed as

2,2'-DipyridylAscorbic AcidCatalysisCatalytic DomainHumansHydroxylationIronKineticsLigandsProlineProlyl Hydroxylases2,2'-DipyridylAscorbic AcidIronLigandsProlineProlyl Hydroxylases

Identifiers

PMID27183028
PMCPMC5141248
OpenAlexW2403625569

What OpenQuestion holds

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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.