Evidence map›Paper›PMID 34117311›Full record

ArticleScientific reports2021

Uncovering of cytochrome P450 anatomy by SecStrAnnotator.

Adam Midlik, Veronika Navrátilová, Taraka Ramji Moturu, Jaroslav Koča, Radka Svobodová, Karel Berka

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
2.9field-weighted citation impact, top 10% 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

15 citing papers in PubMed, 29 citations in OpenAlex.

  1. Characterization of a CYP107 family vitamin DArchives of biochemistry and biophysics · 2026
    Article
  2. Article
  3. Review
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. SSDraw: Software for generating comparative protein secondary structure diagrams.Protein science : a publication of the Protein Society · 2023
    Article
  10. Article
  11. Article
  12. Article
  13. Review
  14. Article
  15. Molecular and Structural Evolution of Cytochrome P450 Aromatase.International journal of molecular sciences · 2021
    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

6 authors at 4 institutions in 1 country.

Adam MidlikCEITEC - Central European Institute of Technology, Masaryk University, Brno, 625 00, Czech Republic.
Veronika NavrátilováDepartment of Physical Chemistry, Faculty of Science, Palacký University, Olomouc, 771 46, Czech Republic.
Taraka Ramji MoturuCEITEC - Central European Institute of Technology, Masaryk University, Brno, 625 00, Czech Republic.
Jaroslav KočaCEITEC - Central European Institute of Technology, Masaryk University, Brno, 625 00, Czech Republic.
Radka SvobodováCEITEC - Central European Institute of Technology, Masaryk University, Brno, 625 00, Czech Republic. radka.svobodova@ceitec.muni.cz.
Karel BerkaDepartment of Physical Chemistry, Faculty of Science, Palacký University, Olomouc, 771 46, Czech Republic. karel.berka@upol.cz.
Masaryk University · CZPalacký University Olomouc · CZCentral European Institute of Technology · CZCentral European Institute of Technology – Masaryk University · CZ

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Protein structural families are groups of homologous proteins defined by the organization of secondary structure elements (SSEs). Nowadays, many families contain vast numbers of structures, and the SSEs can help to orient within them. Communities around specific protein families have even developed specialized SSE annotations, always assigning the same name to the equivalent SSEs in homologous proteins. A detailed analysis of the groups of equivalent SSEs provides an overview of the studied family and enriches the analysis of any particular protein at hand. We developed a workflow for the analysis of the secondary structure anatomy of a protein family. We applied this analysis to the model family of cytochromes P450 (CYPs)-a family of important biotransformation enzymes with a community-wide used SSE annotation. We report the occurrence, typical length and amino acid sequence for the equivalent SSE groups, the conservation/variability of these properties and relationship to the substrate recognition sites. We also suggest a generic residue numbering scheme for the CYP family. Comparing the bacterial and eukaryotic part of the family highlights the significant differences and reveals a well-known anomalous group of bacterial CYPs with some typically eukaryotic features. Our workflow for SSE annotation for CYP and other families can be freely used at address https://sestra.ncbr.muni.cz .

Indexed as

SoftwareAnimalsCytochrome P-450 Enzyme SystemHumansMolecular Dynamics SimulationSequence Analysis, ProteinCytochrome P-450 Enzyme System

Identifiers

PMID34117311
PMCPMC8196199
OpenAlexW3166375275

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.