Evidence map›Paper›PMID 21035495›Full record

ReviewAdvances in enzyme regulation2011

Hits, Fhits and Nits: beyond enzymatic function.

Kay Huebner, Joshua C Saldivar, Jin Sun, Hidetaka Shibata, Teresa Druck

Abstract readReview
In one paragraph

Review in Advances in enzyme regulation, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
1.1field-weighted citation impact, top 24% 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

13 citing papers in PubMed, 37 citations in OpenAlex.

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

5 authors at 2 institutions in 1 country.

Kay HuebnerDepartment of Molecular Virology, Immunology, and Medical Genetics, The Ohio State University Medical Center, Columbus, OH 43210, United States. kay.huebner@osumc.edu
Joshua C Saldivar
Jin Sun
Hidetaka Shibata
Teresa Druck
The Ohio State University Wexner Medical Center · USThe Ohio State University · US

Funding

ROLE OF THE FHIT LOCUS IN ENVIRONMENTAL CARCINOGENESISP01CA077738 · NCI · THOMAS JEFFERSON UNIVERSITY · PI HUEBNER, KAY · 2000 to 2004
$5.6M
Integrative Training in Biomedical SystemsT32GM068412 · NIGMS · OHIO STATE UNIVERSITY · PI PARVIN, JEFFREY D · 2005 to 2020
$2.4M
Wwox as a Critical Signal Mediator in Breast CancerR01CA120516 · NCI · OHIO STATE UNIVERSITY · PI HUEBNER, KAY · 2006 to 2013
$1.3M
Fhit modulation of cell cycle progression and DNA damage responseR01CA132453 · NCI · OHIO STATE UNIVERSITY · PI HUEBNER, KAY · 2007 to 2010
$1.3M
FHIT Gene Therapy in Cancer Prevention and TreatmentR01CA115965 · NCI · OHIO STATE UNIVERSITY · PI CROCE, CARLO M · 2007 to 2011
$1.1M
NCI NIH HHS CA115965NCI NIH HHS CA120516NCI NIH HHS CA132453NCI NIH HHS P01 CA077738NCI NIH HHS R01 CA115965NCI NIH HHS R01 CA120516NCI NIH HHS R01 CA132453NIGMS NIH HHS T32 GM068412NIGMS NIH HHS T32GM068412
6 · The paper itself

Abstract

We have briefly summarized what is known about these proteins, but in closing wish to feature the outstanding questions. Hint1 was discovered mistakenly as an inhibitor of Protein Kinase C and designated Pkci, a designation that still confuses the literature. The other Hint family members were discovered by homology to Hint1. Aprataxin was discovered as a result of the hunt for a gene responsible for AOA1. Fhit was discovered through cloning of a familial chromosome translocation breakpoint on chromosome 3 that interrupts the large FHIT gene within an intron, in the FRA3B chromosome region (Ohta et al., 1996), now known to be the region of the human genome most susceptible to DNA damage due to replication stress (Durkin et al., 2008). The NitFhit fusion genewas discovered during searches for Fhit homologs in flies and worms because the fly/worm Nit polypeptide is fused to the 5'-end of the Fhit gene; the mammalian Nit gene family was discovered because of the NitFhit fusion gene, in searches for homologs to the Nit polypeptide of the NitFhit gene. Each of the Hit family member proteins is reported to have enzymatic activities toward putative substrates involving nucleosides or dinucleosides. Most surprisingly, each of the Hit family proteins discussed has been implicated in important DNA damage response pathways and/or tumor suppression pathways. And for each of them it has been difficult to assign definite substrates, to know if the substrates and catalytic products have biological functions, to know if that function is related to the DNA damage response and suppressor functions, and to precisely define the pathways through which tumor suppression occurs. When the fly Nit sequence was found at the 5'-end of the fly Fhit gene, this gene was hailed as a Rosetta stone gene/protein that would help in discovery of the function of Fhit, because the Nit protein should be in the same signal pathway (Pace et al., 2000). However, the mammalian Nit family proteins have turned out to be at least as mysterious as the Fhit proteins, with the Nit1 substrate still unknown and the surprising finding that Nit proteins also appear to behave as tumor suppressor proteins. Whether the predicted enzymatic functions of these proteins are relevant to the observed biological functions, remain among the outstanding unanswered puzzles and raise the question: have these mammalian proteins evolved beyond the putative original enzymatic purpose, such that the catalytic function is now vestigial and subservient to signal pathways that use the protein-substrate complexes in pathways that signal apoptosis or DNA damage response? Or can these proteins be fulfilling catalytic functions independently but in parallel with signal pathway functions, as perhaps observed for Aprataxin? Or is the catalytic function indeed part of the observed biological functions, such as apoptosis and tumor suppression? Perhaps the recent, post-genomic focus on metabolomics and genome-wide investigations of signal pathway networks will lead to answers to some of these outstanding questions.

Indexed as

Acid Anhydride HydrolasesAmino Acid SequenceAminohydrolasesAnimalsBis(5'-adenosyl)triphosphataseHumansHydrolasesMolecular Sequence DataNeoplasm ProteinsSequence AlignmentAcid Anhydride HydrolasesAminohydrolasesBis(5'-adenosyl)triphosphatasehistidine triad proteinHydrolasesNeoplasm Proteinsnitrilase

Identifiers

PMID21035495
PMCPMC3041834
OpenAlexW2030497633

What OpenQuestion holds

Textmetadata
LicenceTDM
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.