Evidence map›Paper›PMID 19944064›Full record

ArticleArchives of biochemistry and biophysics2010

Rational engineering of cytochromes P450 2B6 and 2B11 for enhanced stability: Insights into structural importance of residue 334.

Jyothi C Talakad, P Ross Wilderman, Dmitri R Davydov, Santosh Kumar, James R Halpert

Open access · greenAbstract read
In one paragraph

Article in Archives of biochemistry and biophysics, 2010. 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
3.1field-weighted citation impact, top 9% 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, 22 citations in OpenAlex.

  1. Article
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  5. Article
  6. Review
  7. Article
  8. Comparison of in vitro metabolism of ticlopidine by human cytochrome P450 2B6 and rabbit cytochrome P450 2B4.Drug metabolism and disposition: the biological fate of chemicals · 2011
    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

5 authors at 2 institutions in 1 country.

Jyothi C TalakadSkaggs School of Pharmacy and Pharmaceutical Sciences, University of California San Diego, La Jolla, CA 92093-0703, USA. jtalakad@ucsd.edu
P Ross Wilderman
Dmitri R Davydov
Santosh Kumar
James R Halpert
University of California, San Diego · USUniversity of Missouri–Kansas City · US

Funding

Synthetic Organic Chemistry CoreP30ES006676 · NIEHS · UNIVERSITY OF TEXAS MEDICAL BR GALVESTON · PI ELFERINK, CORNELIS JOHAN · 1995 to 2017
$21.7M
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-DK07233NIEHS NIH HHS ES003619NIEHS NIH HHS ES006676NIEHS NIH HHS P30 ES006676NIEHS NIH HHS R01 ES003619
6 · The paper itself

Abstract

Rational mutagenesis was used to improve the thermal stability of human cytochrome P450 2B6 and canine P450 2B11. Comparison of the amino acid sequences revealed seven sites that are conserved between the stable 2B1 and 2B4 but different from those found in the less stable 2B6 and 2B11. P334S was the only mutant that showed increased heterologous expression levels and thermal stability in both 2B6 and 2B11. The mechanism of this effect was explored with pressure-perturbation spectroscopy. Compressibility of the heme pocket in variants of all four CYP2B enzymes containing proline at position 334 are characterized by lower compressibility than their more stable serine 334 counterpart. Therefore, the stabilizing effect of P334S is associated with increased conformational flexibility in the region of the heme pocket. Improved stability of P334S 2B6 and 2B11 may facilitate the studies of these enzymes by X-ray crystallography and biophysical techniques.

Indexed as

Protein EngineeringAmino Acid SequenceAmino Acid SubstitutionAnimalsAryl Hydrocarbon HydroxylasesBiocatalysisCrystallography, X-RayCytochrome P-450 Enzyme SystemCytochrome P450 Family 2CytochromesDogsEnzyme StabilityHemeHumansMolecular Sequence DataMutagenesis, Site-DirectedAryl Hydrocarbon Hydroxylasescytochrome P420cytochrome P-450 CYP2B11 (dog)Cytochrome P-450 Enzyme SystemCytochrome P450 Family 2CytochromesHemeProtein IsoformsSteroid Hydroxylases

Identifiers

PMID19944064
PMCPMC2819625
OpenAlexW2014967843

What OpenQuestion holds

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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.