Evidence map›Paper›PMID 33360373›Full record

ReviewCurrent opinion in biotechnology2021

A dynamic understanding of cytochrome P450 structure and function through solution NMR.

Thomas C Pochapsky

Open access · greenAbstract readReview
In one paragraph

Review in Current opinion in biotechnology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing papers in PubMed
1.6field-weighted citation impact, top 17% 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

10 citing papers in PubMed, 15 citations in OpenAlex.

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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

1 author at 1 institution in 1 country.

Thomas C PochapskyDepartments of Chemistry, Biochemistry and The Rosenstiel Institute for Basic Medical Research, Brandeis University, 415 South St., Waltham, MA 02454, USA. Electronic address: pochapsk@brandeis.edu.
Brandeis University · US

Funding

Structure and dynamics of clinically-relevant cytochrome P450 enzymes - Summer undergraduate research experience supplementR01GM130997 · NIGMS · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI POCHAPSKY, THOMAS CHARLES, SCOTT, EMILY E · 2019 to 2022
$1.8M
NIGMS NIH HHS R01 GM130997
6 · The paper itself

Abstract

Many economically important biosyntheses incorporate regiospecific and stereospecific oxidations at unactivated carbons. Such oxidations are commonly catalyzed by cytochrome P450 monooxygenases, heme-containing enzymes that activate molecular oxygen while selectively binding and orienting the substrate for reaction. Despite the plethora of P450-catalyzed reactions, the P450 fold is highly conserved, and static structures are often insufficient for characterizing conformational states that contribute to specificity. High-resolution solution nuclear magnetic resonance (NMR) offers insights into dynamic processes and conformational changes that are required of a P450 in order to attain the combination of specificity and efficiency required for these reactions.

Indexed as

Cytochrome P-450 Enzyme SystemMagnetic Resonance SpectroscopyOxidation-ReductionSubstrate SpecificityCytochrome P-450 Enzyme System

Identifiers

PMID33360373
PMCPMC8215082
OpenAlexW3116283092

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.