Evidence map›Paper›PMID 20446763›Full record

ReviewAntioxidants & redox signaling2010

Conformational plasticity and structure/function relationships in cytochromes P450.

Thomas C Pochapsky, Sophia Kazanis, Marina Dang

Abstract readReview
In one paragraph

Review in Antioxidants & redox signaling, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 66 papers.

0numbers the graph read from it
0cells of the map it votes in
66citing papers in PubMed
13.4field-weighted citation impact, top 1% 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

66 citing papers in PubMed, 124 citations in OpenAlex.

  1. Article
  2. Identification of Pathogenic Variants inInternational journal of molecular sciences · 2026
    Article
  3. Article
  4. Article
  5. Article
  6. Secondary Binding Site of CYP17A1 in Enhanced Sampling Simulations.Journal of chemical information and modeling · 2024
    Article
  7. Article
  8. Article
  9. Generation of new inhibitors of selected cytochrome P450 subtypes-Computational and structural biotechnology journal · 2022
    Article
  10. Article
  11. Review
  12. Article
  13. Functional Characterization of 21 Rare AllelicJournal of personalized medicine · 2021
    Article
  14. Review
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. The Biosynthesis of Enzymatically Oxidized Lipids.Frontiers in endocrinology · 2020
    Review

6 more citing papers are in PubMed but not listed here.

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

3 authors at 1 institution in 1 country.

Thomas C PochapskyDepartment of Chemistry, Brandeis University, Waltham, Massachusetts 02454-9110, USA. pochapsk@brandeis.edu
Sophia Kazanis
Marina Dang
Brandeis University · US

Funding

STRUCTURE AND DYNAMICS OF METAL-CONTAINING PROTEINSR01GM044191 · NIGMS · BRANDEIS UNIVERSITY · PI POCHAPSKY, THOMAS CHARLES · 1995 to 2012
$3.4M
NIGMS NIH HHS R01 GM044191NIGMS NIH HHS R01-GM44191
6 · The paper itself

Abstract

The cytochrome P450s are a superfamily of enzymes that are found in all kingdoms of living organisms, and typically catalyze the oxidative addition of atomic oxygen to an unactivated C-C or C-H bond. Over 8000 nonredundant sequences of putative and confirmed P450 enzymes have been identified, but three-dimensional structures have been determined for only a small fraction of these. While all P450 enzymes for which structures have been determined share a common global fold, the flexibility and modularity of structure around the active site account for the ability of P450 enzymes to accommodate a vast number of structurally dissimilar substrates and support a wide range of selective oxidations. In this review, known P450 structures are compared, and some structural criteria for prediction of substrate selectivity and reaction type are suggested. The importance of dynamic processes such as redox-dependent and effector-induced conformational changes in determining catalytic competence and regio- and stereoselectivity is discussed, and noncrystallographic methods for characterizing P450 structures and dynamics, in particular, mass spectrometry and nuclear magnetic resonance spectroscopy are reviewed.

Indexed as

Cytochrome P-450 Enzyme SystemEukaryotic CellsMass SpectrometryNuclear Magnetic Resonance, BiomolecularProkaryotic CellsProtein ConformationStructure-Activity RelationshipCytochrome P-450 Enzyme System

Identifiers

PMID20446763
PMCPMC2959183
OpenAlexW2080580475

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.