Evidence map›Paper›PMID 28716760›Full record

ArticleThe Journal of steroid biochemistry and molecular biology2018

Properties of purified CYP2R1 in a reconstituted membrane environment and its 25-hydroxylation of 20-hydroxyvitamin D3.

Chloe Y S Cheng, Tae-Kang Kim, Saowanee Jeayeng, Andrzej T Slominski, Robert C Tuckey

Open access · greenAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in The Journal of steroid biochemistry and molecular biology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing papers in PubMed
1.1field-weighted citation impact, top 23% 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

6 citing papers in PubMed, 12 citations in OpenAlex.

  1. Review
  2. Review
  3. Review
  4. An Update on Vitamin D Metabolism.International journal of molecular sciences · 2020
    Review
  5. The serum vitamin D metabolome: What we know and what is still to discover.The Journal of steroid biochemistry and molecular biology · 2019
    Review
  6. 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

5 authors at 4 institutions in 3 countries.

Chloe Y S ChengSchool of Molecular Sciences, The University of Western Australia, Perth, WA, 6009, Australia.
Tae-Kang KimDepartment of Dermatology, University of Alabama at Birmingham, AL, 35294, USA.
Saowanee JeayengDepartment of Dermatology, University of Alabama at Birmingham, AL, 35294, USA; Department of Pharmacology, Faculty of Medicine Siriraj Hospital, Mahidol University, Bangkok, 10700, Thailand.
Andrzej T SlominskiDepartment of Dermatology, University of Alabama at Birmingham, AL, 35294, USA; VA Medical Center, Birmingham, AL, 35294, USA.
Robert C TuckeySchool of Molecular Sciences, The University of Western Australia, Perth, WA, 6009, Australia. Electronic address: robert.tuckey@uwa.edu.au.
University of Western Australia · AUBirmingham VA Medical Center · USSiriraj Hospital · THUniversity of Alabama at Birmingham · US

Funding

Significance of metabolic activation of lumisterol in the skinR01AR071189 · NIAMS · UNIVERSITY OF ALABAMA AT BIRMINGHAM · PI SLOMINSKI, ANDRZEJ T · 2017 to 2021
$1.6M
Role of Exogenous Melatonin in Skin BiologyR01AR056666 · NIAMS · UNIVERSITY OF TENNESSEE HEALTH SCI CTR · PI SLOMINSKI, ANDRZEJ T · 2011 to 2015
$1.6M
Mechanism of action of 20-hydroxyvitamin D3 in dermal fibroblastsR21AR066505 · NIAMS · UNIVERSITY OF TENNESSEE HEALTH SCI CTR · PI SLOMINSKI, ANDRZEJ T · 2014 to 2015
$355k
NIAMS NIH HHS R01 AR056666NIAMS NIH HHS R01 AR071189NIAMS NIH HHS R21 AR066505
6 · The paper itself

Abstract

Recent studies indicate that CYP2R1 is the major 25-hydroxylase catalyzing the first step in vitamin D activation. Since the catalytic properties of CYP2R1 have been poorly studied to date and it is a membrane protein, we examined the purified enzyme in a membrane environment. CYP2R1 was expressed in E. coli and purified by nickel affinity- and hydrophobic interaction-chromatography and assayed in a reconstituted membrane system comprising phospholipid vesicles plus purified human NADPH-P450 oxidoreductase. CYP2R1 converted vitamin D3 in the vesicle membrane to 25-hydroxyvitamin D3 [25(OH)D3] with good adherence to Michaelis-Menten kinetics. The kinetic parameters for 25-hydroxylation of vitamin D3 by the two major vitamin D 25-hydroxylases, CYP2R1 and CYP27A1, were examined in vesicles under identical conditions. CYP2R1 displayed a slightly lower k

Indexed as

CalcifediolCell MembraneCell ProliferationCells, CulturedCholestanetriol 26-MonooxygenaseCytochrome P-450 Enzyme SystemCytochrome P450 Family 2Escherichia coliFibroblastsHumansHydroxylationMelanocytesNuclear Receptor Subfamily 1, Group F, Member 1Vitamins20-hydroxyvitamin D3CalcifediolCholestanetriol 26-MonooxygenaseCYP27A1 protein, humanCYP2R1 protein, humanCytochrome P-450 Enzyme SystemCytochrome P450 Family 2Nuclear Receptor Subfamily 1, Group F, Member 1POR protein, humanRORA protein, humanVitamins25-hydroxylaseCYP2R1Phospholipid vesiclesVitamin D3

Identifiers

PMID28716760
PMCPMC5767547
OpenAlexW2734408806

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.