Evidence map›Paper›PMID 31351986›Full record

ReviewThe American journal of pathology2019

Mechanisms of Receptor Tyrosine-Protein Kinase ErbB-3 (ERBB3) Action in Human Neoplasia.

Laurel E Black, Jody F Longo, Steven L Carroll

Open access · bronzeAbstract readReview
In one paragraph

Review in The American journal of pathology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 43 papers.

0numbers the graph read from it
0cells of the map it votes in
43citing papers in PubMed
2.9field-weighted citation impact, top 8% 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

43 citing papers in PubMed, 71 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

3 authors at 1 institution in 1 country.

Laurel E BlackDepartment of Pathology and Laboratory Medicine, Medical University of South Carolina, Charleston, South Carolina.
Jody F LongoDepartment of Pathology and Laboratory Medicine, Medical University of South Carolina, Charleston, South Carolina.
Steven L CarrollDepartment of Pathology and Laboratory Medicine, Medical University of South Carolina, Charleston, South Carolina. Electronic address: carrolst@musc.edu.
Medical University of South Carolina · US

Funding

South Carolina Cancer Disparities Research Center (SC CADRE)U54CA210962 · NCI · MEDICAL UNIVERSITY OF SOUTH CAROLINA · PI TURNER, DAVID PAUL · 2017 to 2023
$6.7M
South Carolina Cancer Disparities Research Center (SC CaDRe)U54CA210963 · NCI · SOUTH CAROLINA STATE UNIVERSITY · PI FORD, MARVELLA ELIZABETH, SALLEY, JUDITH · 2017 to 2023
$6.1M
Novel Treatment of NF-1 Associated Malignant Peripheral Nerve Sheath TumorsR01CA122804 · NCI · UNIVERSITY OF ALABAMA AT BIRMINGHAM · PI CARROLL, STEVEN L. · 2008 to 2012
$1.5M
Role of Neuregulin-1 in Schwann Cell NeoplasiaR01NS048353 · NINDS · UNIVERSITY OF ALABAMA AT BIRMINGHAM · PI CARROLL, STEVEN L. · 2004 to 2008
$1.3M
NCI NIH HHS R01 CA122804NCI NIH HHS U54 CA210962NCI NIH HHS U54 CA210963NINDS NIH HHS R01 NS048353
6 · The paper itself

Abstract

It is well established that the epidermal growth factor (EGF) receptor, receptor tyrosine-protein kinase erbB-2 (ERBB2)/human EGF receptor 2 (HER2), and, to a lesser extent, ERBB4/HER4, promote the pathogenesis of many types of human cancers. In contrast, the role that ERBB3/HER3, the fourth member of the ERBB family of receptor tyrosine kinases, plays in these diseases is poorly understood and, until recently, underappreciated. In large part, this was because early structural and functional studies suggested that ERBB3 had little, if any, intrinsic tyrosine kinase activity and, thus, was unlikely to be an important therapeutic target. Since then, however, numerous publications have demonstrated an important role for ERBB3 in carcinogenesis, metastasis, and acquired drug resistance. Furthermore, somatic ERBB3 mutations are frequently encountered in many types of human cancers. Dysregulation of ERBB3 trafficking as well as cooperation with other receptor tyrosine kinases further enhance ERBB3's role in tumorigenesis and drug resistance. As a result of these advances in our understanding of the structure and biochemistry of ERBB3, and a growing focus on the development of precision and combinatorial therapeutic regimens, ERBB3 is increasingly considered to be an important therapeutic target in human cancers. In this review, we discuss the unique structural and functional features of ERBB3 and how this information is being used to develop effective new therapeutic agents that target ERBB3 in human cancers.

Indexed as

CarcinogenesisHumansNeoplasmsPhosphorylationReceptor, ErbB-3Signal TransductionERBB3 protein, humanReceptor, ErbB-3

Identifiers

PMID31351986
PMCPMC6892224
OpenAlexW2965987470

What OpenQuestion holds

Textmetadata
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.