Evidence map›Paper›PMID 31953231›Full record

ArticleBiochimica et biophysica acta. Biomembranes2020

Expression, purification, and functional reconstitution of

Jia Bai, Jian Wang, Thirupathi Ravula, Sang-Choul Im, G M Anantharamaiah, Lucy Waskell, Ayyalusamy Ramamoorthy

Open access · greenAbstract read
In one paragraph

Article in Biochimica et biophysica acta. Biomembranes, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.

0numbers the graph read from it
0cells of the map it votes in
9citing papers in PubMed
1.5field-weighted citation impact, top 21% 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

9 citing papers in PubMed, 20 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Review
  5. Article
  6. Nanodiscs: A toolkit for membrane protein science.Protein science : a publication of the Protein Society · 2021
    Review
  7. Structure and function of proteins in membranes and nanodiscs.Biochimica et biophysica acta. Biomembranes · 2021
    Article
  8. Article
  9. 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

7 authors at 1 institution in 1 country.

Jia BaiBiophysics Program, Department of Chemistry, Biomedical Engineering, Macromolecular Science and Engineering, The University of Michigan, Ann Arbor, MI 48109-1055, USA.
Jian WangBiophysics Program, Department of Chemistry, Biomedical Engineering, Macromolecular Science and Engineering, The University of Michigan, Ann Arbor, MI 48109-1055, USA.
Thirupathi RavulaBiophysics Program, Department of Chemistry, Biomedical Engineering, Macromolecular Science and Engineering, The University of Michigan, Ann Arbor, MI 48109-1055, USA.
Sang-Choul ImDepartment of Internal Medicine, The University of Michigan, and VA Medical Center, Ann Arbor, MI 48105, USA.
G M AnantharamaiahDepartment of Medicine, UAB Medical Center, Birmingham, AL 35294, USA.
Lucy WaskellDepartment of Anesthesiology, The University of Michigan, and VA Medical Center, Ann Arbor, MI 48105, USA.
Ayyalusamy RamamoorthyBiophysics Program, Department of Chemistry, Biomedical Engineering, Macromolecular Science and Engineering, The University of Michigan, Ann Arbor, MI 48109-1055, USA. Electronic address: ramamoor@umich.edu.
University of Michigan–Ann Arbor · 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
Development of biophysical approaches to investigate high-resolution structure and dynamics of membrane proteinsR35GM139573 · NIGMS · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI Ayyalusamy Ramamoorthy · 2021 to 2026
$2.0M
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 GM095640NIGMS NIH HHS R35 GM139573
6 · The paper itself

Abstract

Microsomal cytochrome b5 (cytb5) is a membrane-bound protein capable of donating the second electron to cytochrome P450s (cytP450s) in the cytP450s monooxygenase reactions. Recent studies have demonstrated the importance of the transmembrane domain of cytb5 in the interaction with cytP450 by stabilizing its monomeric structure. While recent NMR studies have provided high-resolution insights into the structural interactions between the soluble domains of ~16-kDa cytb5 and ~57-kDa cytP450 in a membrane environment, there is need for studies to probe the residues in the transmembrane region as well as to obtain intermolecular distance constraints to better understand the very large size cytb5-cytP450 complex structure in a near native membrane environment. In this study, we report the expression, purification, functional reconstitution of

Indexed as

AnimalsCytochrome P-450 Enzyme SystemCytochromes b5Magnetic Resonance SpectroscopyMembrane ProteinsModels, MolecularNuclear Magnetic Resonance, BiomolecularOxidation-ReductionProtein BindingProtein DomainsRabbitsCytochrome P-450 Enzyme SystemCytochromes b5Membrane Proteins(19)F NMRCytochrome b5Cytochrome P450Lipid bilayerMembrane proteinNanodisc

Identifiers

PMID31953231
PMCPMC7050362
OpenAlexW3000436964

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.