Evidence map›Paper›PMID 28363936›Full record

ArticleThe Journal of biological chemistry2017

ω-

Emily E Scott

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing 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

4 citing papers in PubMed, 6 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Computational Insight Into Vitamin KFrontiers in pharmacology · 2018
    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

1 author at 1 institution in 1 country.

Emily E ScottFrom the Departments of Medicinal Chemistry, Pharmacology, and Biophysics, University of Michigan, Ann Arbor, Michigan 48109 scottee@umich.edu.
University of Michigan–Ann Arbor · US

Funding

Structural Basis of Cytochrome P450 Activity-Equipment SupplementR37GM076343 · NIGMS · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI SCOTT, EMILY E · 2015 to 2024
$3.7M
NIGMS NIH HHS R37 GM076343
6 · The paper itself

Abstract

Many family 4 cytochrome P450s play key roles in fatty acid hydroxylation at the terminal, or ω, carbon, but the mechanistic basis for this energetically disfavored regiostereochemistry has been less clear. A co-crystal structure of the rabbit family 4 enzyme CYP4B1 with its substrate octane reveals that the propensity for ω-hydroxylation is orchestrated by active-site sterics, partially mediated by an unusual heme-polypeptide ester bond.

Indexed as

AnimalsAryl Hydrocarbon HydroxylasesBinding SitesCrystallography, X-RayFatty AcidsHydroxylationOctanesRabbitsSubstrate SpecificityAryl Hydrocarbon Hydroxylasescytochrome P-450 CYP4B1Fatty AcidsoctaneOctanes

Identifiers

PMID28363936
PMCPMC5392704
OpenAlexW2601968246

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.