Evidence map›Paper›PMID 11266604›Full record

ArticleProtein science : a publication of the Protein Society2001

Understanding thermostability in cytochrome P450 by combinatorial mutagenesis.

S A Maves, S G Sligar

Open access · greenAbstract read
In one paragraph

Article in Protein science : a publication of the Protein Society, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
1.3field-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

17 citing papers in PubMed, 38 citations in OpenAlex.

  1. Article
  2. Functions of ROS in Macrophages and Antimicrobial Immunity.Antioxidants (Basel, Switzerland) · 2021
    Review
  3. Article
  4. Article
  5. Article
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  7. Article
  8. Entropic contribution to enhanced thermal stability in the thermostable P450 CYP119.Proceedings of the National Academy of Sciences of the United States of America · 2018
    Article
  9. Article
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  11. Article
  12. Article
  13. Article
  14. Article
  15. X-ray absorption spectroscopic characterization of a cytochrome P450 compound II derivative.Proceedings of the National Academy of Sciences of the United States of America · 2008
    Article
  16. Article
  17. 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.

S A MavesThe Beckman Institute for Advanced Science and Technology and the Department of Biochemistry, University of Illinois, Urbana, Illinois 61801, USA.
S G Sligar
University of Illinois Urbana-Champaign · US

Funding

METALLOENZYME MECHANISMSR01GM033775 · NIGMS · UNIVERSITY OF ILLINOIS URBANA-CHAMPAIGN · PI SLIGAR, STEPHEN G. · 1985 to 2014
$5.2M
HEME PROTEIN REDUCTASESR01GM031756 · NIGMS · UNIVERSITY OF ILLINOIS URBANA-CHAMPAIGN · PI SLIGAR, STEPHEN G. · 1985 to 2012
$1.5M
NIGMS NIH HHS R01 GM031756NIGMS NIH HHS R01 GM033775NIGMS NIH HHS R01-GM 31756NIGMS NIH HHS R01-GM 33775
6 · The paper itself

Abstract

The cytochromes P450 are an important class of mono-oxygenases involved in xenobiotic metabolism and steroid biosynthesis in a diverse set of life forms. Discovery of CYP-119, a P450 from the archea Sulfolobus solfataricus has provided a means for understanding nature's method of stabilizing this important protein superfamily. To identify classes of stabilizing interactions used by CYP-119, we have generated a randomized library of point mutants and screened for mutants that are less thermostable than the wild type by monitoring the characteristic Soret band in the visible region of the cell lysis. The selected mutants were characterized by differential scanning calorimetry to compare the temperatures of the melting transitions of the various mutants. The identified mutations suggested that electrostatic interactions involving salt links and charge-charge interactions, as well as contributions from other interactions such as aromatic stacking, and side chain volume of hydrophobic residues contribute to enhanced thermostability in this cytochrome P450.

Indexed as

Cytochrome P-450 Enzyme SystemEnzyme StabilityModels, MolecularMutagenesisProtein EngineeringSulfolobusThermodynamicsCytochrome P-450 Enzyme System

Identifiers

PMID11266604
PMCPMC2249849
OpenAlexW2077253713

What OpenQuestion holds

Textmetadata
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.