Evidence map›Paper›PMID 29184004›Full record

ArticleThe Journal of biological chemistry2018

A global view of structure-function relationships in the tautomerase superfamily.

Rebecca Davidson, Bert-Jan Baas, Eyal Akiva, Gemma L Holliday, Benjamin J Polacco, Jake A LeVieux, Collin R Pullara, Yan Jessie Zhang, Christian P Whitman, Patricia C Babbitt

Abstract read
In one paragraph

Article in The Journal of biological chemistry, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.

0numbers the graph read from it
0cells of the map it votes in
30citing papers in PubMed
–field-weighted citation impact
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

30 citing papers in PubMed.

  1. Review
  2. Article
  3. From duplication to fusion: Expanding Dayhoff's model of protein evolution.Protein science : a publication of the Protein Society · 2025
    Review
  4. Article
  5. Article
  6. Article
  7. The Structural Biology of Catalase Evolution.Sub-cellular biochemistry · 2024
    Review
  8. Article
  9. Article
  10. Review
  11. Article
  12. Article
  13. Unlocking New Reactivities in Enzymes by Iminium Catalysis.Angewandte Chemie (International ed. in English) · 2022
    Review
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. 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

10 authors.

Rebecca DavidsonFrom the Department of Bioengineering and Therapeutic Sciences.
Bert-Jan Baasthe Division of Chemical Biology and Medicinal Chemistry, College of Pharmacy.
Eyal AkivaFrom the Department of Bioengineering and Therapeutic Sciences.
Gemma L HollidayFrom the Department of Bioengineering and Therapeutic Sciences.
Benjamin J PolaccoFrom the Department of Bioengineering and Therapeutic Sciences.
Jake A LeVieuxthe Department of Molecular Biosciences, and.
Collin R Pullarathe Division of Chemical Biology and Medicinal Chemistry, College of Pharmacy.
Yan Jessie Zhangthe Department of Molecular Biosciences, and.
Christian P Whitmanthe Division of Chemical Biology and Medicinal Chemistry, College of Pharmacy, whitman@austin.utexas.edu.
Patricia C BabbittFrom the Department of Bioengineering and Therapeutic Sciences, babbitt@cgl.ucsf.edu.ORCID 0000-0003-0375-9015

Funding

BMI Bioinformatics Training GrantsT32GM067547 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI HERNANDEZ, RYAN D. · 2003 to 2022
$6.6M
Laying the Foundation of Genomic EnzymologyR01GM060595 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI BABBITT, PATRICIA CLEMENT · 2000 to 2018
$5.4M
Integrative Program in Complex Biological System (ipCBS)T32EB009383 · NIBIB · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI MARSHALL, WALLACE, WEINER, ORION D · 2009 to 2022
$3.2M
ENZYMES OF THE META-FISSION PATHWAYR01GM041239 · NIGMS · UNIVERSITY OF TEXAS AUSTIN · PI WHITMAN, CHRISTIAN P. · 1995 to 2017
$3.0M
Pilatus 6mS10OD021832 · OD · UNIVERSITY OF CALIFORNIA BERKELEY · PI ADAMS, PAUL DAVID · 2016 to 2016
$980k
Howard Hughes Medical InstituteNIBIB NIH HHS T32 EB009383NIGMS NIH HHS R01 GM041239NIGMS NIH HHS R01 GM060595NIGMS NIH HHS T32 GM067547NIH HHS S10 OD021832
6 · The paper itself

Abstract

The tautomerase superfamily (TSF) consists of more than 11,000 nonredundant sequences present throughout the biosphere. Characterized members have attracted much attention because of the unusual and key catalytic role of an N-terminal proline. These few characterized members catalyze a diverse range of chemical reactions, but the full scale of their chemical capabilities and biological functions remains unknown. To gain new insight into TSF structure-function relationships, we performed a global analysis of similarities across the entire superfamily and computed a sequence similarity network to guide classification into distinct subgroups. Our results indicate that TSF members are found in all domains of life, with most being present in bacteria. The eukaryotic members of the

Indexed as

Multigene FamilyAmino Acid SequenceAnimalsBinding SitesCrystallography, X-RayEnzymesEukaryotaEvolution, MolecularHumansKineticsMolecular Sequence DataPhylogenyPlantsSequence AlignmentEnzymesenzyme structureenzyme superfamilyevolutionprotein evolutionprotein sequenceprotein structurestructure-functionstructure–function relationshipstautomerase superfamily

Identifiers

PMID29184004
PMCPMC5818174

What OpenQuestion holds

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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.