ReviewJournal of cellular physiology1999
The histidine triad superfamily of nucleotide-binding proteins.
Review in Journal of cellular physiology, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 papers.
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.
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.
Who cites it
40 citing papers in PubMed, 122 citations in OpenAlex.
- Liquid-liquid phase separation and the formation of amyloid fibrils from DcpS scavenger enzymes.Scientific reports · 2026Article
- A repurposed AMP binding domain reveals mitochondrial protein AMPylation as a regulator of cellular metabolism.Nature communications · 2025Article
- Histidine Triad Nucleotide-Binding Protein 1 Improves Critical Limb Ischemia by Regulating Mitochondrial Homeostasis.Nutrients · 2023Article
- Mycobacteriophage Rita: a cluster F1 phage discovered in North Easton, Massachusetts.Microbiology resource announcements · 2023Article
- Protective effect of HINT2 on mitochondrial function via repressing MCU complex activation attenuates cardiac microvascular ischemia-reperfusion injury.Basic research in cardiology · 2021Article
- Comparative Proteomic Study Shows the Expression of Hint-1 in Pituitary Adenomas.Diagnostics (Basel, Switzerland) · 2021Article
- Loss of fragile histidine triad (Fhit) protein expression alters the translation of cancer-associated mRNAs.BMC research notes · 2018Article
- FHIT promoter DNA methylation and expression analysis in childhood acute lymphoblastic leukemia.Oncology letters · 2017Article
- Errors in Crystal structure of HINT from Helicobacter pylori.Acta crystallographica. Section F, Structural biology communications · 2016Article
- Crystal structure of HINT from Helicobacter pylori.Acta crystallographica. Section F, Structural biology communications · 2016Article
- A 24-48 h fed Amblyomma americanum tick saliva immuno-proteome.BMC genomics · 2014Article
- A knockdown with smoke model reveals FHIT as a repressor of Heme oxygenase 1.Cell cycle (Georgetown, Tex.) · 2014Article
- Kinetic mechanism of human histidine triad nucleotide binding protein 1.Biochemistry · 2013Article
- Side chain independent recognition of aminoacyl adenylates by the Hint1 transcription suppressor.The journal of physical chemistry. B · 2012Article
- Hits, Fhits and Nits: beyond enzymatic function.Advances in enzyme regulation · 2011Review
- Article
- An interaction-motif-based scoring function for protein-ligand docking.BMC bioinformatics · 2010Article
- Exploring the biochemical mechanisms of cytotoxic gold compounds: a proteomic study.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2010Article
- CK2 phosphorylation-dependent interaction between aprataxin and MDC1 in the DNA damage response.Nucleic acids research · 2010Article
- Fragile histidine triad protein: structure, function, and its association with tumorogenesis.Journal of cancer research and clinical oncology · 2010Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Histidine triad (HIT) proteins were until recently a superfamily of proteins that shared only sequence motifs. Crystal structures of nucleotide-bound forms of histidine triad nucleotide-binding protein (Hint) demonstrated that the conserved residues in HIT proteins are responsible for their distinctive, dimeric, 10-stranded half-barrel structures that form two identical purine nucleotide-binding sites. Hint-related proteins, found in all forms of life, and fragile histidine triad (Fhit)-related proteins, found in animals and fungi, represent the two main branches of the HIT superfamily. Hint homologs are intracellular receptors for purine mononucleotides whose cellular function remains elusive. Fhit homologs bind and cleave diadenosine polyphosphates (Ap(n)A) such as ApppA and AppppA. Fhit-Ap(n)A complexes appear to function in a proapoptotic tumor suppression pathway in epithelial tissues. In invertebrates, Fhit homologs are encoded as fusion proteins with proteins related to plant and bacterial nitrilases that are candidate signaling partners in tumor suppression.
Indexed as
Identifiers
10497298PMC2556047W2134961408What OpenQuestion holds
Registered trials
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.