Evidence map›Paper›PMID 9164465›Full record

ArticleNature structural biology1997

Crystal structures of HINT demonstrate that histidine triad proteins are GalT-related nucleotide-binding proteins.

C Brenner, P Garrison, J Gilmour, D Peisach, D Ringe, G A Petsko, J M Lowenstein

Open access · greenAbstract read
In one paragraph

Article in Nature structural biology, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 52 papers.

0numbers the graph read from it
0cells of the map it votes in
52citing papers in PubMed
6.2field-weighted citation impact, top 3% 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

52 citing papers in PubMed, 133 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. International journal of molecular sciences · 2024
    Article
  5. Article
  6. The Many Faces of Histidine Triad Nucleotide Binding Protein 1 (HINT1).ACS pharmacology & translational science · 2023
    Review
  7. Article
  8. Article
  9. Axonal neuropathy with neuromyotonia: there is a HINT.Brain : a journal of neurology · 2017
    Review
  10. Review
  11. Errors in Crystal structure of HINT from Helicobacter pylori.Acta crystallographica. Section F, Structural biology communications · 2016
    Article
  12. Structures of a histidine triad family protein from Entamoeba histolytica bound to sulfate, AMP and GMP.Acta crystallographica. Section F, Structural biology communications · 2015
    Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  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

7 authors at 2 institutions in 1 country.

C BrennerDepartment of Biochemistry, Brandeis University, Waltham, Massachusetts 02254, USA. brenner@dada.jci.tju.edu
P Garrison
J Gilmour
D Peisach
D Ringe
G A Petsko
J M Lowenstein
Brandeis University · USThe University of Texas Health Science Center at San Antonio · US

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 R01 CA075954
6 · The paper itself

Abstract

Histidine triad nucleotide-binding protein (HINT), a dimeric purine nucleotide-binding protein from rabbit heart, is a member of the HIT (histidine triad) superfamily which includes HINT homologues and FHIT (HIT protein encoded at the chromosome 3 fragile site) homologues. Crystal structures of HINT-nucleotide complexes demonstrate that the most conserved residues in the superfamily mediate nucleotide binding and that the HIT motif forms part of the phosphate binding loop. Galactose-1-phosphate uridylyltransferase, whose deficiency causes galactosemia, contains tandem HINT domains with the same fold and mode of nucleotide binding as HINT despite having no overall sequence similarity. Features of FHIT, a diadenosine polyphosphate hydrolase and candidate tumour suppressor, are predicted from HINT-nucleotide structures.

Indexed as

HydrolasesModels, StructuralProtein Structure, SecondaryAmino Acid SequenceAnimalsBinding SitesBiological EvolutionChromosome MappingComputer SimulationCrystallography, X-RayDimerizationHistidineHumansModels, MolecularMolecular Sequence DataMyocardiumHistidinehistidine triad proteinHydrolasesNucleosidesNucleotidesProteinsRecombinant ProteinsUTP-Hexose-1-Phosphate Uridylyltransferase

Identifiers

PMID9164465
PMCPMC2571075
OpenAlexW1984201743

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.