Evidence map›Paper›PMID 28712849›Full record

ReviewArchives of biochemistry and biophysics2017

Structure, function, and mechanism of proline utilization A (PutA).

Li-Kai Liu, Donald F Becker, John J Tanner

Abstract readReview
In one paragraph

Review in Archives of biochemistry and biophysics, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 48 papers.

0numbers the graph read from it
0cells of the map it votes in
48citing papers in PubMed
3.9field-weighted citation impact, top 5% 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

48 citing papers in PubMed, 80 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Review
  6. Article
  7. Article
  8. Review
  9. Review
  10. Article
  11. The Proline Dehydrogenase GeneInternational journal of molecular sciences · 2025
    Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Review
  20. Review
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 2 institutions in 1 country.

Li-Kai LiuDepartment of Biochemistry, University of Missouri, Columbia, MO, 65211, United States.
Donald F BeckerDepartment of Biochemistry and Redox Biology Center, University of Nebraska-Lincoln, Lincoln, NE, 68588-0664, United States. Electronic address: dbecker3@unl.edu.
John J TannerDepartment of Biochemistry, University of Missouri, Columbia, MO, 65211, United States; Department of Chemistry, University of Missouri, Columbia, MO, 65211, United States. Electronic address: tannerjj@missouri.edu.
University of Missouri · USUniversity of Nebraska–Lincoln · US

Funding

Substrate Channeling and Communication in Proline Metabolic EnzymesR01GM065546 · NIGMS · UNIVERSITY OF MISSOURI-COLUMBIA · PI Donald F Becker, JOHN J TANNER · 2002 to 2026
$5.0M
Redox Biology CenterP30GM103335 · NIGMS · UNIVERSITY OF NEBRASKA LINCOLN · PI BECKER, DONALD F · 2012 to 2016
$4.3M
Spectroelectrochemistry of the Novel PutA FlavoproteinR01GM061068 · NIGMS · UNIVERSITY OF NEBRASKA LINCOLN · PI BECKER, DONALD F · 2001 to 2015
$3.7M
NIGMS NIH HHS P30 GM103335NIGMS NIH HHS R01 GM061068NIGMS NIH HHS R01 GM065546
6 · The paper itself

Abstract

Proline has important roles in multiple biological processes such as cellular bioenergetics, cell growth, oxidative and osmotic stress response, protein folding and stability, and redox signaling. The proline catabolic pathway, which forms glutamate, enables organisms to utilize proline as a carbon, nitrogen, and energy source. FAD-dependent proline dehydrogenase (PRODH) and NAD

Indexed as

1-Pyrroline-5-Carboxylate DehydrogenaseAmino Acid Metabolism, Inborn ErrorsAnimalsBacterial ProteinsFlavin-Adenine DinucleotideFlavoproteinsGram-Negative BacteriaHumansMembrane ProteinsProlineProline Oxidase1-Pyrroline-5-Carboxylate DehydrogenaseBacterial ProteinsFlavin-Adenine DinucleotideFlavoproteinsMembrane ProteinsProlineProline OxidasePutA protein, BacteriaAldehyde dehydrogenaseEnzyme hysteresisFlavin-dependent reactionFlavoproteinMultifunctional enzymesproline catabolismProtein structureSubstrate channeling

Identifiers

PMID28712849
PMCPMC5650515
OpenAlexW2735686411

What OpenQuestion holds

Textmetadata
LicenceTDM
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.