Evidence map›Paper›PMID 27530203›Full record

ReviewProtein science : a publication of the Protein Society2016

Carboxylic ester hydrolases: Classification and database derived from their primary, secondary, and tertiary structures.

Yingfei Chen, Daniel S Black, Peter J Reilly

Open access · bronzeAbstract readReview
In one paragraph

Review in Protein science : a publication of the Protein Society, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
2.1field-weighted citation impact, top 13% 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

19 citing papers in PubMed, 59 citations in OpenAlex.

  1. Article
  2. Review
  3. Identification of Black Cumin (Plants (Basel, Switzerland) · 2024
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  6. Article
  7. Article
  8. Article
  9. RevisitingBiomolecules · 2021
    Article
  10. Article
  11. Review
  12. DUB esterase activity further decodes ubiquitin's enigma.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  13. Article
  14. Article
  15. Article
  16. Characterization and Immobilization of a Novel SGNH Family Esterase (International journal of molecular sciences · 2019
    Article
  17. Article
  18. Article
  19. A Feasibility Study on the Identification of Potential Biomarkers in Pulmonary Embolism Using Proteomic Analysis.Clinical and applied thrombosis/hemostasis : official journal of the International Academy of Clinical and Applied Thrombosis/Hemostasis
    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

3 authors at 1 institution in 1 country.

Yingfei ChenDepartment of Chemical and Biological Engineering, Iowa State University, Ames, Iowa, 50011.
Daniel S BlackInformation Technology Services, Iowa State University, Ames, Iowa, 50011.
Peter J ReillyDepartment of Chemical and Biological Engineering, Iowa State University, Ames, Iowa, 50011. reilly@iastate.edu.
Iowa State University · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

We classified the carboxylic ester hydrolases (CEHs) into families and clans by use of multiple sequence alignments, secondary structure analysis, and tertiary structure superpositions. Our work for the first time has fully established their systematic structural classification. Family members have similar primary, secondary, and tertiary structures, and their active sites and reaction mechanisms are conserved. Families may be gathered into clans by their having similar secondary and tertiary structures, even though primary structures of members of different families are not similar. CEHs were gathered from public databases by use of Basic Local Alignment Search Tool (BLAST) and divided into 91 families, with 36 families being grouped into five clans. Members of one clan have standard α/β-hydrolase folds, while those of other two clans have similar folds but with different sequences of their β-strands. The other two clans have members with six-bladed β-propeller and three-α-helix bundle tertiary structures. Those families not in clans have a large variety of structures or have no members with known structures. At the time of writing, the 91 families contained 321,830 primary structures and 1378 tertiary structures. From these data, we constructed an accessible database: CASTLE (CArboxylic eSTer hydroLasEs, http://www.castle.cbe.iastate.edu).

Indexed as

Databases, ProteinProtein FoldingCarboxylesteraseProtein DomainsProtein Structure, SecondaryCarboxylesterasecarboxylesterasescholinesterasescocaine esterasescutinaseslysopholipasesphospholipasestriacylglycerol lipases

Identifiers

PMID27530203
PMCPMC5079261
OpenAlexW2516883256

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.