Evidence map›Paper›PMID 35191957›Full record

ReviewBiochemical Society transactions2022

IMPDH dysregulation in disease: a mini review.

Anika L Burrell, Justin M Kollman

Open access · bronzeAbstract readReview
In one paragraph

Review in Biochemical Society transactions, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.

0numbers the graph read from it
0cells of the map it votes in
31citing papers in PubMed
3.6field-weighted citation impact, top 6% 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

31 citing papers in PubMed, 47 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Review
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Review
  15. Article
  16. Review
  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

2 authors at 1 institution in 1 country.

Anika L BurrellDepartment of Biochemistry, University of Washington, Seattle, WA, U.S.A.
Justin M KollmanDepartment of Biochemistry, University of Washington, Seattle, WA, U.S.A.ORCID 0000-0001-6943-9570
University of Washington · US

Funding

TRAINING IN MOLECULAR BIOPHYSICST32GM008268 · NIGMS · UNIVERSITY OF WASHINGTON · PI KOLLMAN, JUSTIN M, ZHENG, NING · 1988 to 2023
$8.6M
The Structure and Function of Metabolic FilamentsR01GM118396 · NIGMS · UNIVERSITY OF WASHINGTON · PI KOLLMAN, JUSTIN M · 2016 to 2023
$2.9M
IMPDH structure and function in retinal degenerationR21EY031546 · NEI · UNIVERSITY OF WASHINGTON · PI BROCKERHOFF, SUSAN E, KOLLMAN, JUSTIN M · 2020 to 2021
$479k
IMPDH1 structure and function in the healthy and diseased retinaF31EY030732 · NEI · UNIVERSITY OF WASHINGTON · PI BURRELL, ANIKA LAUREN · 2019 to 2021
$116k
NEI NIH HHS F31 EY030732NEI NIH HHS R21 EY031546NIGMS NIH HHS R01 GM118396NIGMS NIH HHS T32 GM008268
6 · The paper itself

Abstract

Inosine-5'-monophosphate dehydrogenase (IMPDH) is a highly conserved enzyme in purine metabolism that is tightly regulated on multiple levels. IMPDH has a critical role in purine biosynthesis, where it regulates flux at the branch point between adenine and guanine nucleotide synthesis, but it also has a role in transcription regulation and other moonlighting functions have been described. Vertebrates have two isoforms, IMPDH1 and IMPDH2, and point mutations in each are linked to human disease. Mutations in IMPDH2 in humans are associated with neurodevelopmental disease, but the effects of mutations at the enzyme level have not yet been characterized. Mutations in IMPDH1 lead to retinal degeneration in humans, and recent studies have characterized how they cause functional defects in regulation. IMPDH1 is expressed as two unique splice variants in the retina, a tissue with very high and specific demands for purine nucleotides. Recent studies have revealed functional differences among splice variants, demonstrating that retinal variants up-regulate guanine nucleotide synthesis by reducing sensitivity to feedback inhibition by downstream products. A better understanding of the role of IMPDH1 in the retina and the characterization of an animal disease model will be critical for determining the molecular mechanism of IMPDH1-associated blindness.

Indexed as

IMP DehydrogenaseRetinal DegenerationAnimalsMutationProtein IsoformsRetinaIMP DehydrogenaseProtein Isoformsallosteric regulationretinitis pigmentosasplice variants

Identifiers

PMID35191957
PMCPMC9022972
OpenAlexW4213278264

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.