Evidence map›Paper›PMID 28529725›Full record

ReviewF1000Research2017

The catalytic function of cytochrome P450 is entwined with its membrane-bound nature.

Carlo Barnaba, Katherine Gentry, Nirupama Sumangala, Ayyalusamy Ramamoorthy

Open access · goldAbstract readReview
In one paragraph

Review in F1000Research, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.

0numbers the graph read from it
0cells of the map it votes in
30citing papers in PubMed
9.3field-weighted citation impact, top 1% 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

30 citing papers in PubMed, 64 citations in OpenAlex.

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  9. Duplicate mutations of GhCYP450 lead to the production of msTAG. Theoretical and applied genetics. Theoretische und angewandte Genetik · 2023
    Article
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  12. Review
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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

4 authors at 1 institution in 1 country.

Carlo BarnabaBiophysics Program and Department of Chemistry, The University of Michigan, Ann Arbor, MI, USA.ORCID 0000-0003-2170-9695
Katherine GentryBiophysics Program and Department of Chemistry, The University of Michigan, Ann Arbor, MI, USA.
Nirupama SumangalaBiophysics Program and Department of Chemistry, The University of Michigan, Ann Arbor, MI, USA.
Ayyalusamy RamamoorthyBiophysics Program and Department of Chemistry, The University of Michigan, Ann Arbor, MI, USA.ORCID 0000-0003-1964-1900
University of Michigan · US

Funding

Supplement: Investigation of Membrane-Bound Cytochromes-P450-b5 InteractionsR01GM084018 · NIGMS · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI RAMAMOORTHY, AYYALUSAMY · 2009 to 2018
$3.8M
Rapid and efficient production of functional Cytochrome P450 enzymatic complex foR01GM095640 · NIGMS · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI RAMAMOORTHY, AYYALUSAMY · 2010 to 2013
$1.3M
Purchase of a 500 MHz Solid State NMR SpectrometerS10RR023597 · NCRR · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI RAMAMOORTHY, AYYALUSAMY · 2007 to 2007
$500k
NCRR NIH HHS S10 RR023597NIGMS NIH HHS R01 GM095640
6 · The paper itself

Abstract

Cytochrome P450, a family of monooxygenase enzymes, is organized as a catalytic metabolon, which requires enzymatic partners as well as environmental factors that tune its complex dynamic. P450 and its reducing counterparts-cytochrome P450-reductase and cytochrome

Indexed as

cytochrome b5cytochrome P450membraneNADPH-P450 reductasesold-state NMRstructure

Identifiers

PMID28529725
PMCPMC5428493
OpenAlexW2613725002

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.