Evidence map›Paper›PMID 23989972›Full record

ArticleScientific reports2013

Probing the transmembrane structure and topology of microsomal cytochrome-p450 by solid-state NMR on temperature-resistant bicelles.

Kazutoshi Yamamoto, Melissa Gildenberg, Shivani Ahuja, Sang-Choul Im, Paige Pearcy, Lucy Waskell, Ayyalusamy Ramamoorthy

Abstract read
In one paragraph

Article in Scientific reports, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.

0numbers the graph read from it
0cells of the map it votes in
29citing papers in PubMed
–field-weighted citation impact
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

29 citing papers in PubMed.

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  7. 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

7 authors.

Kazutoshi YamamotoBiophysics and Department of Chemistry, University of Michigan, Ann Arbor, MI 48109-1055, USA.
Melissa Gildenberg
Shivani Ahuja
Sang-Choul Im
Paige Pearcy
Lucy Waskell
Ayyalusamy Ramamoorthy

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
PARTICIPATION OF CYTOCHROME B5 IN ANESTHETIC METABOLISMR01GM035533 · NIGMS · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI WASKELL, LUCY A · 1985 to 2010
$2.7M
Microsomal Cytochromes P450 and their Interactions with their Redox PartnersR01GM094209 · NIGMS · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI WASKELL, LUCY A · 2011 to 2014
$1.5M
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 GM084018NIGMS NIH HHS GM095640NIGMS NIH HHS GM35533NIGMS NIH HHS R01 GM035533NIGMS NIH HHS R01 GM084018NIGMS NIH HHS R01 GM094209NIGMS NIH HHS R01 GM095640
6 · The paper itself

Abstract

Though the importance of high-resolution structure and dynamics of membrane proteins has been well recognized, optimizing sample conditions to retain the native-like folding and function of membrane proteins for Nuclear Magnetic Resonance (NMR) or X-ray measurements has been a major challenge. While bicelles have been shown to stabilize the function of membrane proteins and are increasingly utilized as model membranes, the loss of their magnetic-alignment at low temperatures makes them unsuitable to study heat-sensitive membrane proteins like cytochrome-P450 and protein-protein complexes. In this study, we report temperature resistant bicelles that can magnetically-align for a broad range of temperatures and demonstrate their advantages in the structural studies of full-length microsomal cytochrome-P450 and cytochrome-b5 by solid-state NMR spectroscopy. Our results reveal that the N-terminal region of rabbit cytochrome-P4502B4, that is usually cleaved off to obtain crystal structures, is helical and has a transmembrane orientation with ~17° tilt from the lipid bilayer normal.

Indexed as

Cytochrome P-450 Enzyme SystemHumansLipid BilayersMagnetic Resonance SpectroscopyMicrosomes, LiverSpecimen HandlingCytochrome P-450 Enzyme SystemLipid Bilayers

Identifiers

PMID23989972
PMCPMC3757361

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Registered trials

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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.