Evidence map›Paper›PMID 26476077›Full record

ReviewNeoplasia (New York, N.Y.)2015

Inducing Oncoprotein Degradation to Improve Targeted Cancer Therapy.

Dipankar Ray, Kyle C Cuneo, Alnawaz Rehemtulla, Theodore S Lawrence, Mukesh K Nyati

Open access · goldAbstract readReview
In one paragraph

Review in Neoplasia (New York, N.Y.), 2015. 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
0.8field-weighted citation impact, top 28% 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, 22 citations in OpenAlex.

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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 1 institution in 1 country.

Dipankar RayDepartment of Radiation Oncology, University of Michigan, Ann Arbor, MI, 48109.
Kyle C CuneoDepartment of Radiation Oncology, University of Michigan, Ann Arbor, MI, 48109.
Alnawaz RehemtullaDepartment of Radiation Oncology, University of Michigan, Ann Arbor, MI, 48109.
Theodore S LawrenceDepartment of Radiation Oncology, University of Michigan, Ann Arbor, MI, 48109.
Mukesh K NyatiDepartment of Radiation Oncology, University of Michigan, Ann Arbor, MI, 48109. Electronic address: nyati@umich.edu.
University of Michigan–Ann Arbor · US

Funding

QUANTITATION OF HUMAN BRAIN TUMOR THERAPY RESPONSE BY MRP01CA085878 · NCI · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI ROSS, BRIAN D. · 2001 to 2017
$31.9M
Therapeutic Potential and Mechanism of Action of Potent Small Molecule InhibitorsP50CA097248 · NCI · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI WOLF, GREGORY T · 2002 to 2013
$25.3M
Efficacy of PDI inhibitors in glioblastomaR01CA193690 · NCI · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI NEAMATI, NOURI, REHEMTULLA, ALNAWAZ · 2015 to 2019
$2.4M
Integration of EGFR Inhibitors with Radiochemotherapy in Head and Neck CancerR01CA131290 · NCI · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI NYATI, MUKESH K. · 2009 to 2013
$1.5M
Targeting SMURF2 as a novel therapy for EGFR driven tumorsR01CA160981 · NCI · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI RAY, DIPANKAR · 2011 to 2015
$1.4M
NCI NIH HHS P01 CA085878NCI NIH HHS P01CA085878NCI NIH HHS P50 CA097248NCI NIH HHS P50CA097248NCI NIH HHS R01 CA131290NCI NIH HHS R01CA131290NCI NIH HHS R01 CA160981NCI NIH HHS R01CA160981NCI NIH HHS R01 CA193690NCI NIH HHS R01CA193690
6 · The paper itself

Abstract

Over the past decade, inhibition of the kinase activities of oncogenic proteins using small molecules and antibodies has been a mainstay of our anticancer drug development effort, resulting in several Food and Drug Administration-approved cancer therapies. The clinical effectiveness of kinase-targeted agents has been inconsistent, mostly because of the development of resistance. The expression and function of oncoproteins and tumor suppressors are regulated by numerous posttranslational protein modifications including phosphorylation, ubiquitination, and acetylation; hence, targeting specific posttranslational protein modifications provides for an attractive strategy for anticancer drug development. The present review discusses the hypothesis that targeted degradation of an oncoprotein may overcome many of the shortcomings seen with kinase inhibitors and that the approach would enable targeted inhibition of oncogenic proteins previously thought to be undruggable.

Indexed as

AnimalsAntineoplastic AgentsDrug Delivery SystemsHumansMolecular Targeted TherapyNeoplasmsOncogene ProteinsAntineoplastic AgentsOncogene Proteins

Identifiers

PMID26476077
PMCPMC4611070
OpenAlexW2120572950

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.