Evidence map›Paper›PMID 11805111›Full record

ArticleThe Journal of biological chemistry2002

Adenosine monophosphoramidase activity of Hint and Hnt1 supports function of Kin28, Ccl1, and Tfb3.

Pawel Bieganowski, Preston N Garrison, Santosh C Hodawadekar, Gerard Faye, Larry D Barnes, Charles Brenner

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2002. 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
4.7field-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, 110 citations in OpenAlex.

  1. Article
  2. Article
  3. The Many Faces of Histidine Triad Nucleotide Binding Protein 1 (HINT1).ACS pharmacology & translational science · 2023
    Review
  4. Article
  5. Intracellular HINT1-Assisted Hydrolysis of Nucleoside 5'-International journal of molecular sciences · 2022
    Article
  6. Nucleoside 5'-Phosphoramidates Control the Phenylpropanoid Pathway inInternational journal of molecular sciences · 2021
    Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Review
  12. Article
  13. Review
  14. Axonal neuropathy with neuromyotonia: there is a HINT.Brain : a journal of neurology · 2017
    Review
  15. Errors in Crystal structure of HINT from Helicobacter pylori.Acta crystallographica. Section F, Structural biology communications · 2016
    Article
  16. Article
  17. Lack of neuropathy-related phenotypes in hint1 knockout mice.Journal of neuropathology and experimental neurology · 2014
    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

6 authors at 3 institutions in 2 countries.

Pawel BieganowskiStructural Biology and Bioinformatics Program, Kimmel Cancer Center, Philadelphia, Pennsylvania 19107, USA.
Preston N Garrison
Santosh C Hodawadekar
Gerard Faye
Larry D Barnes
Charles Brenner
Sidney Kimmel Cancer Center · USThe University of Texas Health Science Center at San Antonio · USCentre National de la Recherche Scientifique · FR

Funding

Mechanism of Dnmt1 Up-regulation by Fhit LossR01CA075954 · NCI · UNIVERSITY OF IOWA · PI BRENNER, CHARLES M · 1997 to 2012
$3.0M
NCI NIH HHS CA75954NCI NIH HHS R01 CA075954
6 · The paper itself

Abstract

The histidine triad superfamily of nucleotide hydrolases and nucleotide transferases consists of a branch of proteins related to Hint and Aprataxin, a branch of Fhit-related hydrolases, and a branch of galactose-1-phosphate uridylyltransferase (GalT)-related transferases. Although substrates of Fhit and GalT are known and consequences of mutations in Aprataxin, Fhit, and GalT are known, good substrates had not been reported for any member of the Hint branch, and mutational consequences were unknown for Hint orthologs, which are the most ancient and widespread proteins in the Hint branch and in the histidine triad superfamily. Here we show that rabbit and yeast Hint hydrolyze the natural product adenosine-5'-monophosphoramidate (AMPNH(2)) in an active-site-dependent manner at second order rates exceeding 1,000,000 m(-1) s(-1). Yeast strains constructed with specific loss of the Hnt1 active site fail to grow on galactose at elevated temperatures. Loss of Hnt1 enzyme activity also leads to hypersensitivity to mutations in Ccl1, Tfb3, and Kin28, which constitute the TFIIK kinase subcomplex of general transcription factor TFIIH and to mutations in Cak1, which phosphorylates Kin28. The target of Hnt1 regulation in this pathway was shown to be downstream of Cak1 and not to affect stability of Kin28 monomers. Functional complementation of all Hnt1 phenotypes was provided by rabbit Hint, which is only 22% identical to yeast Hnt1 but has very similar adenosine monophosphoramidase activity.

Indexed as

Cyclin-Dependent KinasesPlant ProteinsTranscription Factors, TFIIAllelesAnimalsFungal ProteinsHydrolasesMutagenesisPhosphorylationProteinsProtein Serine-Threonine KinasesSaccharomyces cerevisiae ProteinsTranscription Factorsadenosine 5'-phosphoramidate hydrolaseCyclin-Dependent KinasesFungal Proteinshistidine triad proteinHydrolasesKin28 protein kinase, S cerevisiaePlant ProteinsProteinsProtein Serine-Threonine KinasesSaccharomyces cerevisiae ProteinsTFB3 protein, S cerevisiaeTranscription FactorsTranscription Factors, TFII

Identifiers

PMID11805111
PMCPMC2556056
OpenAlexW2159495147

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.