Evidence map›Paper›PMID 21453708›Full record

ArticleJournal of theoretical biology2011

A hetero-dimer model for concerted action of vitamin K carboxylase and vitamin K reductase in vitamin K cycle.

Sangwook Wu, Shubin Liu, Charles H Davis, Darrel W Stafford, John D Kulman, Lee G Pedersen

Open access · bronzeAbstract read
In one paragraph

Article in Journal of theoretical biology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
1.8field-weighted citation impact, top 16% 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

11 citing papers in PubMed, 17 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Article
  6. Dietary reference values for vitamin K.EFSA journal. European Food Safety Authority · 2017
    Article
  7. Review
  8. Article
  9. Article
  10. Article
  11. 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

6 authors at 2 institutions in 1 country.

Sangwook WuDepartment of Chemistry, University of North Carolina, Chapel Hill, NC 27599-3290, USA.
Shubin Liu
Charles H Davis
Darrel W Stafford
John D Kulman
Lee G Pedersen
University of North Carolina at Chapel Hill · USUniversity of Washington · US

Funding

THE ROLE OF THE VITAMIN K CYCLE IN COAGULATIONP01HL006350 · NHLBI · UNIV OF NORTH CAROLINA CHAPEL HILL · PI STAFFORD, DARREL W · 1985 to 2013
$17.5M
Macromolecular ModelingZICES043010 · NIEHS · NATIONAL INSTITUTE OF ENVIRONMENTAL HEALTH SCIENCES · PI COPELAND, WILLIAM · 2012 to 2025
$5.7M
Characterization of Vitamin K Epoxide ReductaseR01HL077740 · NHLBI · UNIV OF NORTH CAROLINA CHAPEL HILL · PI STAFFORD, DARREL W, TIE, JIANKE · 2005 to 2015
$3.9M
NHLBI NIH HHS HL-06350NHLBI NIH HHS P01 HL006350NHLBI NIH HHS R01 HL077740
6 · The paper itself

Abstract

Vitamin K carboxylase (VKC) is believed to convert vitamin K, in the vitamin K cycle, to an alkoxide-epoxide form which then reacts with CO(2) and glutamate to generate γ-carboxyglutamic acid (Gla). Subsequently, vitamin K epoxide reductase (VKOR) is thought to convert the alkoxide-epoxide to a hydroquinone form. By recycling vitamin K, the two integral-membrane proteins, VKC and VKOR, maintain vitamin K levels and sustain the blood coagulation cascade. Unfortunately, NMR or X-ray crystal structures of the two proteins have not been characterized. Thus, our understanding of the vitamin K cycle is only partial at the molecular level. In this study, based on prior biochemical experiments on VKC and VKOR, we propose a hetero-dimeric form of VKC and VKOR that may explain the efficient oxidation and reduction of vitamin K during the vitamin K cycle.

Indexed as

Models, BiologicalProtein MultimerizationCarbon-Carbon LigasesCatalytic DomainMutationNAD(P)H Dehydrogenase (Quinone)Protein Structure, SecondaryQuantum TheoryVitamin KWarfarinCarbon-Carbon Ligasesglutamyl carboxylaseNAD(P)H Dehydrogenase (Quinone)Vitamin KWarfarin

Identifiers

PMID21453708
PMCPMC3108363
OpenAlexW2154493405

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.