Evidence map›Paper›PMID 38791967›Full record

ReviewCancers2024

"Oh, Dear We Are in Tribble": An Overview of the Oncogenic Functions of Tribbles 1.

Karnika Singh, Christian A Showalter, Heather R Manring, Saikh Jaharul Haque, Arnab Chakravarti

Abstract readReview
In one paragraph

Review in Cancers, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
–field-weighted citation impact
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

2 citing papers in PubMed.

  1. Review
  2. 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.

Karnika SinghDepartment of Radiation Oncology, The Ohio State University Comprehensive Cancer Center, Columbus, OH 43210, USA.ORCID 0000-0002-2108-6523
Christian A ShowalterDepartment of Radiation Oncology, The Ohio State University Comprehensive Cancer Center, Columbus, OH 43210, USA.ORCID 0000-0002-8187-7773
Heather R ManringDepartment of Radiation Oncology, The Ohio State University Comprehensive Cancer Center, Columbus, OH 43210, USA.
Saikh Jaharul HaqueDepartment of Radiation Oncology, The Ohio State University Comprehensive Cancer Center, Columbus, OH 43210, USA.
Arnab ChakravartiDepartment of Radiation Oncology, The Ohio State University Comprehensive Cancer Center, Columbus, OH 43210, USA.ORCID 0000-0002-5392-8721

Funding

Genetic evolution of glioblastomas during radiation and temozolomide therapyR01CA188228 · NCI · DANA-FARBER CANCER INST · PI BEROUKHIM, RAMEEN, CHAKRAVARTI, ARNAB · 2015 to 2025
$6.9M
OSU as Network Lead Academic Participating Site for the NCI NCTNU10CA180850 · NCI · OHIO STATE UNIVERSITY · PI BLUM, KRISTIE A, CHAKRAVARTI, ARNAB · 2014 to 2018
$6.8M
Signal Transduction Pathways in GlioblastomaR01CA108633 · NCI · OHIO STATE UNIVERSITY · PI CHAKRAVARTI, ARNAB · 2005 to 2009
$2.3M
TOWARDS A REFINED MOLECULAR RECURSIVE PARTITIONING ANALYSIS MODEL FOR GLIOBLASTOMRC2CA148190 · NCI · AMERICAN COLLEGE OF RADIOLOGY · PI ALDAPE, KENNETH D, CHAKRAVARTI, ARNAB · 2009 to 2010
$2.1M
Therapeutic Exploitation of Mutant BRAF for AstrocytomaR01CA169368 · NCI · UNIVERSITY OF TEXAS HLTH SCIENCE CENTER · PI HOUGHTON, PETER J · 2013 to 2017
$1.6M
A Brain Tumor Funders Collaborative Grant NANCI NIH HHS 1RC2CA148190NCI NIH HHS R01 CA108633NCI NIH HHS R01CA108633NCI NIH HHS R01CA1145128NCI NIH HHS R01CA11522358NCI NIH HHS R01 CA169368NCI NIH HHS R01CA169368NCI NIH HHS R01 CA188228NCI NIH HHS R01CA188228NCI NIH HHS RC2 CA148190NCI NIH HHS U10 CA180850NCI NIH HHS U10CA180850-01The Ohio State University Comprehensive Cancer Center - Arthur G. James Cancer Hospital and Richard J. Solove Research Institute NA
6 · The paper itself

Abstract

Pseudokinases are catalytically inactive proteins in the human genome that lack the ability to transfer phosphate from ATP to their substrates. The Tribbles family of pseudokinases contains three members: Tribbles 1, 2, and 3. Tribbles 1 has recently gained importance because of its involvement in various diseases, including cancer. It acts as a scaffolding protein that brings about the degradation of its substrate proteins, such as C/EBPα/β, MLXIPL, and RAR/RXRα, among others, via the ubiquitin proteasome system. It also serves as an adapter protein, which sequesters different protein molecules and activates their downstream signaling, leading to processes, such as cell survival, cell proliferation, and lipid metabolism. It has been implicated in cancers such as AML, prostate cancer, breast cancer, CRC, HCC, and glioma, where it activates oncogenic signaling pathways such as PI3K-AKT and MAPK and inhibits the anti-tumor function of p53. TRIB1 also causes treatment resistance in cancers such as NSCLC, breast cancer, glioma, and promyelocytic leukemia. All these effects make TRIB1 a potential drug target. However, the lack of a catalytic domain renders TRIB1 "undruggable", but knowledge about its structure, conformational changes during substrate binding, and substrate binding sites provides an opportunity to design small-molecule inhibitors against specific TRIB1 interactions.

Indexed as

cancerdrug targetinglipid metabolismoncogenic signalingpseudokinasetreatment resistancetribbles 1

Identifiers

PMID38791967
PMCPMC11120034

What OpenQuestion holds

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LicenceCC BY
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.