Evidence map›Paper›PMID 22208531›Full record

ReviewCurrent drug metabolism2012

Plasticity of CYP2B enzymes: structural and solution biophysical methods.

P Ross Wilderman, James R Halpert

Open access · greenAbstract readReview
In one paragraph

Review in Current drug metabolism, 2012. 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
7.3field-weighted citation impact, top 3% 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.

  1. Article
  2. Paroxetine-Overview of the Molecular Mechanisms of Action.International journal of molecular sciences · 2021
    Review
  3. So many roads traveled: A career in science and administration.The Journal of biological chemistry · 2020
    Article
  4. Review
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Review
  11. Article
  12. The dynamics of camphor in the cytochrome P450 CYP101D2.Protein science : a publication of the Protein Society · 2013
    Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. 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

2 authors at 1 institution in 1 country.

P Ross WildermanSkaggs School of Pharmacy and Pharmaceutical Sciences, University of California San Diego, La Jolla, 92093-0703, USA. pwilderman@ucsd.edu
James R Halpert
University of Montana · US

Funding

STRUCTURAL BASIS OF SELECTIVE P-450 INACTIVATIONR01ES003619 · NIEHS · UNIVERSITY OF TEXAS MEDICAL BR GALVESTON · PI HALPERT, JAMES R · 1985 to 2016
$6.2M
HEMOGLOBIN AND BLOOD PROTEIN CHEMISTRYT32DK007233 · NIDDK · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI KOMIVES, ELIZABETH A. · 1986 to 2012
$4.6M
NIDDK NIH HHS T32 DK007233NIDDK NIH HHS T32-DK007233NIEHS NIH HHS ES003619NIEHS NIH HHS R01 ES003619
6 · The paper itself

Abstract

In the past three years, major advances in understanding cytochrome P450 2B (CYP2B) structure-function relationships have been made through determination of multiple ligand-bound and one ligand-free X-ray crystal structure of CYP2B4 and one ligand-bound X-ray crystal structure of CYP2B6. These structures have provided insight into the features that provide the high degree of plasticity of the enzymes. A combination of a phenylalanine cluster that allows for concerted movement of helices F through G and a conserved set of electrostatic interactions involving Arg(262) facilitates movement of this region to accommodate binding of ligands of various sizes without perturbing most of the P450 fold. Integrating solution based techniques such as NMR or deuterium exchange mass spectrometry (DXMS) with computational methods including molecular docking has provided further insight into enzyme behavior upon ligand binding. In addition, extended molecular dynamics simulations have provided a link between an open and a closed conformation of ligand-free CYP2B4 found in crystal structures. Other studies revealed the utility of rational engineering in improving stability of P450s to facilitate structural studies. The solution and computational results combined with the X-ray crystal structures yield a comprehensive picture of how these enzymes adopt different conformations to bind various ligands.

Indexed as

AnimalsAryl Hydrocarbon HydroxylasesCrystallography, X-RayHumansModels, MolecularProtein ConformationProtein EngineeringSpectrum AnalysisSteroid HydroxylasesAryl Hydrocarbon HydroxylasesSteroid Hydroxylases

Identifiers

PMID22208531
PMCPMC3879780
OpenAlexW2048533382

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.