Evidence map›Paper›PMID 28258219›Full record

ArticleThe Journal of biological chemistry2017

Resolving the cofactor-binding site in the proline biosynthetic enzyme human pyrroline-5-carboxylate reductase 1.

Emily M Christensen, Sagar M Patel, David A Korasick, Ashley C Campbell, Kurt L Krause, Donald F Becker, John J Tanner

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers.

0numbers the graph read from it
0cells of the map it votes in
41citing papers in PubMed
2.6field-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

41 citing papers in PubMed, 59 citations in OpenAlex.

  1. Article
  2. [Research Progress on the Role and Mechanisms of PYCR1 
in Tumorigenesis and Progression].Zhongguo fei ai za zhi = Chinese journal of lung cancer · 2026
    Review
  3. The Substrate Versatility of ΔMolecules (Basel, Switzerland) · 2026
    Article
  4. Inactivation of ornithine aminotransferase by (1Medicinal chemistry research : an international journal for rapid communications on design and mechanisms of action of biologically active agents · 2026
    Article
  5. Review
  6. Review
  7. Review
  8. Review
  9. Review
  10. Article
  11. Article
  12. Article
  13. Novel Fragment Inhibitors of PYCR1 from Docking-Guided X-ray Crystallography.Journal of chemical information and modeling · 2024
    Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Expression and kinetic characterization of PYCR3.Archives of biochemistry and biophysics · 2023
    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

7 authors at 3 institutions in 2 countries.

Emily M ChristensenFrom the Departments of Chemistry and.
Sagar M Patelthe Department of Biochemistry and Redox Biology Center, University of Nebraska, Lincoln, Nebraska 68588.
David A KorasickBiochemistry University of Missouri, Columbia, Missouri 65211.
Ashley C CampbellBiochemistry University of Missouri, Columbia, Missouri 65211.
Kurt L Krausethe Department of Biochemistry, University of Otago, Dunedin 9054, New Zealand, and.
Donald F Beckerthe Department of Biochemistry and Redox Biology Center, University of Nebraska, Lincoln, Nebraska 68588.
John J TannerFrom the Departments of Chemistry and tannerjj@missouri.edu.
University of Missouri · USUniversity of Nebraska–Lincoln · USUniversity of Otago · NZ

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
NIGMS NIH HHS R01 GM065546
6 · The paper itself

Abstract

Pyrroline-5-carboxylate reductase (PYCR) is the final enzyme in proline biosynthesis, catalyzing the NAD(P)H-dependent reduction of Δ

Indexed as

Binding SitesCatalytic DomainCrystallography, X-Raydelta-1-Pyrroline-5-Carboxylate ReductaseHumansKineticsLigandsMutationNADPProlineProtein BindingProtein MultimerizationProtein Structure, QuaternaryProtein Structure, TertiaryPyrroline Carboxylate ReductasesSubstrate Specificitydelta-1-Pyrroline-5-Carboxylate ReductaseLigandsNADPProlinePyrroline Carboxylate Reductasesanalytical ultracentrifugationenzyme kineticsNAD(P)H-dependent reductasenicotinamide adenine dinucleotide (NADH)reductaseRossmann foldsite-directed mutagenesissubstrate specificityX-ray crystallography

Identifiers

PMID28258219
PMCPMC5409489
OpenAlexW2593392007

What Socratic 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 Socratic graph.