Evidence map›Paper›PMID 29455667›Full record

ReviewMolecular cancer2018

Role of Non Receptor Tyrosine Kinases in Hematological Malignances and its Targeting by Natural Products.

Kodappully S Siveen, Kirti S Prabhu, Iman W Achkar, Shilpa Kuttikrishnan, Sunitha Shyam, Abdul Q Khan, Maysaloun Merhi, Said Dermime, Shahab Uddin

Open access · goldAbstract readReview
In one paragraph

Review in Molecular cancer, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 70 papers.

0numbers the graph read from it
0cells of the map it votes in
70citing papers in PubMed
6.7field-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

70 citing papers in PubMed, 126 citations in OpenAlex.

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  16. Molecular biology of the novel anticancer medications: a focus on kinases inhibitors, biologics and CAR T-cell therapy.Inflammation research : official journal of the European Histamine Research Society ... [et al.] · 2025
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10 more citing papers are in PubMed but not listed here.

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

9 authors at 2 institutions in 1 country.

Kodappully S SiveenTranslational Research Institute, Academic Health System, Hamad Medical Corporation, PO Box 3050, Doha, State of Qatar.
Kirti S PrabhuTranslational Research Institute, Academic Health System, Hamad Medical Corporation, PO Box 3050, Doha, State of Qatar.
Iman W AchkarTranslational Research Institute, Academic Health System, Hamad Medical Corporation, PO Box 3050, Doha, State of Qatar.
Shilpa KuttikrishnanTranslational Research Institute, Academic Health System, Hamad Medical Corporation, PO Box 3050, Doha, State of Qatar.
Sunitha ShyamMedical Research Center, Hamad Medical Corporation, Doha, State of Qatar.
Abdul Q KhanTranslational Research Institute, Academic Health System, Hamad Medical Corporation, PO Box 3050, Doha, State of Qatar.
Maysaloun MerhiTranslational Cancer Research Facility, National Center for Cancer Care and Research, Hamad Medical Corporation, Doha, State of Qatar.
Said DermimeTranslational Cancer Research Facility, National Center for Cancer Care and Research, Hamad Medical Corporation, Doha, State of Qatar.
Shahab UddinTranslational Research Institute, Academic Health System, Hamad Medical Corporation, PO Box 3050, Doha, State of Qatar. Skhan34@hamad.qa.ORCID 0000-0003-1886-6710
Hamad Medical Corporation · QANational Center for Cancer Care and Research · QA

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Tyrosine kinases belong to a family of enzymes that mediate the movement of the phosphate group to tyrosine residues of target protein, thus transmitting signals from the cell surface to cytoplasmic proteins and the nucleus to regulate physiological processes. Non-receptor tyrosine kinases (NRTK) are a sub-group of tyrosine kinases, which can relay intracellular signals originating from extracellular receptor. NRTKs can regulate a huge array of cellular functions such as cell survival, division/propagation and adhesion, gene expression, immune response, etc. NRTKs exhibit considerable variability in their structural make up, having a shared kinase domain and commonly possessing many other domains such as SH2, SH3 which are protein-protein interacting domains. Recent studies show that NRTKs are mutated in several hematological malignancies, including lymphomas, leukemias and myelomas, leading to aberrant activation. It can be due to point mutations which are intragenic changes or by fusion of genes leading to chromosome translocation. Mutations that lead to constitutive kinase activity result in the formation of oncogenes, such as Abl, Fes, Src, etc. Therefore, specific kinase inhibitors have been sought after to target mutated kinases. A number of compounds have since been discovered, which have shown to inhibit the activity of NRTKs, which are remarkably well tolerated. This review covers the role of various NRTKs in the development of hematological cancers, including their deregulation, genetic alterations, aberrant activation and associated mutations. In addition, it also looks at the recent advances in the development of novel natural compounds that can target NRTKs and perhaps in combination with other forms of therapy can show great promise for the treatment of hematological malignancies.

Indexed as

AnimalsBiological ProductsHematologic NeoplasmsHumansProtein-Tyrosine KinasesSignal TransductionBiological ProductsProtein-Tyrosine Kinaseshematological malignancynatural productsNon receptor tyrosine kinasessignaling pathways

Identifiers

PMID29455667
PMCPMC5817858
OpenAlexW2797623003

What OpenQuestion holds

Textmetadata
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.