Evidence map›Paper›PMID 22069326›Full record

ReviewThe Journal of biological chemistry2012

Divergent evolution in enolase superfamily: strategies for assigning functions.

John A Gerlt, Patricia C Babbitt, Matthew P Jacobson, Steven C Almo

Abstract readReview
In one paragraph

Review in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 63 papers.

0numbers the graph read from it
0cells of the map it votes in
63citing 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

63 citing papers in PubMed.

  1. Article
  2. Article
  3. Impact of Enolase in Allergic Disease.Current allergy and asthma reports · 2024
    Review
  4. Article
  5. Article
  6. Article
  7. Review
  8. The structure of Synechococcus elongatus enolase reveals key aspects of phosphoenolpyruvate binding.Acta crystallographica. Section F, Structural biology communications · 2022
    Article
  9. Article
  10. Article
  11. Setting the stage for evolution of a new enzyme.Current opinion in structural biology · 2021
    Review
  12. NADPJournal of microbiology and biotechnology · 2021
    Article
  13. Article
  14. Review
  15. Article
  16. Article
  17. Article
  18. Article
  19. Review
  20. Article

3 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

4 authors.

John A GerltDepartments of Biochemistry and Chemistry and The Institute for Genomic Biology, University of Illinois, Urbana, Illinois 61801. Electronic address: j-gerlt@uiuc.edu.
Patricia C BabbittDepartment of Bioengineering and Therapeutic Sciences, University of California, San Francisco, California, 94143.
Matthew P JacobsonPharmaceutical Chemistry, School of Pharmacy, University of California, San Francisco, California 94143.
Steven C AlmoDepartment of Biochemistry, Albert Einstein College of Medicine, Yeshiva University, Bronx, New York 10461.

Funding

Core H: MicrobiologyU54GM093342 · NIGMS · UNIVERSITY OF ILLINOIS AT URBANA-CHAMPAIGN · PI GERLT, JOHN A · 2010 to 2015
$34.6M
XRAY CRYSTALLOGRAPHIC STRUCTURE ANALYSIS: PROTEIN SORTINGP41RR001081 · NCRR · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI FERRIN, THOMAS E · 1985 to 2011
$17.6M
Theoretical and Computational ApproachesP01GM071790 · NIGMS · UNIVERSITY OF ILLINOIS URBANA-CHAMPAIGN · PI RAUSHEL, FRANK M. · 2004 to 2013
$15.5M
Laying the Foundation of Genomic EnzymologyR01GM060595 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI BABBITT, PATRICIA CLEMENT · 2000 to 2018
$5.4M
NCRR NIH HHS P41 RR001081NIGMS NIH HHS P01 GM071790NIGMS NIH HHS P01GM071790-07NIGMS NIH HHS R01 GM060595NIGMS NIH HHS U54 GM093342NIGMS NIH HHS U54GM093342NIGMS NIH HHS U54GM093342-01
6 · The paper itself

Abstract

Nature's strategies for evolving catalytic functions can be deciphered from the information contained in the rapidly expanding protein sequence databases. However, the functions of many proteins in the protein sequence and structure databases are either uncertain (too divergent to assign function based on homology) or unknown (no homologs), thereby limiting the utility of the databases. The mechanistically diverse enolase superfamily is a paradigm for understanding the structural bases for evolution of enzymatic function. We describe strategies for assigning functions to members of the enolase superfamily that should be applicable to other superfamilies.

Indexed as

Evolution, MolecularComputational BiologyDrug Evaluation, PreclinicalHumansPhosphopyruvate HydrataseSmall Molecule LibrariesStructure-Activity RelationshipPhosphopyruvate HydrataseSmall Molecule Libraries

Identifiers

PMID22069326
PMCPMC3249080

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.