Evidence map›Paper›PMID 28646173›Full record

ArticleScientific reports2017

Transmembrane Interactions of Full-length Mammalian Bitopic Cytochrome-P450-Cytochrome-b

Kazutoshi Yamamoto, Marc A Caporini, Sang-Choul Im, Lucy Waskell, Ayyalusamy Ramamoorthy

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
2.5field-weighted citation impact, top 11% 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

18 citing papers in PubMed, 35 citations in OpenAlex.

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  11. Expression, purification, and functional reconstitution ofBiochimica et biophysica acta. Biomembranes · 2020
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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

5 authors at 3 institutions in 1 country.

Kazutoshi YamamotoBiophysics and Department of Chemistry, University of Michigan, Ann Arbor, MI, 48109-1055, USA.
Marc A CaporiniBruker Biospin Corporation, 15 Fortune Drive, Billerica, MA, 01821, USA.
Sang-Choul ImDepartment of Anesthesiology, VA Medical Center, University of Michigan, Ann Arbor, MI, 48105, USA.
Lucy WaskellDepartment of Anesthesiology, VA Medical Center, University of Michigan, Ann Arbor, MI, 48105, USA.
Ayyalusamy RamamoorthyBiophysics and Department of Chemistry, University of Michigan, Ann Arbor, MI, 48109-1055, USA. ramamoor@umich.edu.
University of Michigan–Ann Arbor · USAnn Arbor VA Medical Center · USBruker (United States) · 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
NIGMS NIH HHS R01 GM084018NIGMS NIH HHS R01 GM095640
6 · The paper itself

Abstract

The dynamic protein-protein and protein-ligand interactions of integral bitopic membrane proteins with a single membrane-spanning helix play a plethora of vital roles in the cellular processes associated with human health and diseases, including signaling and enzymatic catalysis. While an increasing number of high-resolution structural studies of membrane proteins have successfully manifested an in-depth understanding of their biological functions, intact membrane-bound bitopic protein-protein complexes pose tremendous challenges for structural studies by crystallography or solution NMR spectroscopy. Therefore, there is a growing interest in developing approaches to investigate the functional interactions of bitopic membrane proteins embedded in lipid bilayers at atomic-level. Here we demonstrate the feasibility of dynamic nuclear polarization (DNP) magic-angle-spinning NMR techniques, along with a judiciously designed stable isotope labeling scheme, to measure atomistic-resolution transmembrane-transmembrane interactions of full-length mammalian ~72-kDa cytochrome P450-cytochrome b

Indexed as

Nuclear Magnetic Resonance, BiomolecularAmino Acid SequenceAnimalsCarbon-13 Magnetic Resonance SpectroscopyCytochrome P-450 Enzyme SystemCytochromes b5HumansLipid BilayersModels, MolecularMultiprotein ComplexesProtein BindingProtein ConformationCytochrome P-450 Enzyme SystemCytochromes b5Lipid BilayersMultiprotein Complexes

Identifiers

PMID28646173
PMCPMC5482851
OpenAlexW2662105881

What OpenQuestion holds

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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.