Evidence map›Paper›PMID 23416973›Full record

ArticleOncogene2014

Engineering a single ubiquitin ligase for the selective degradation of all activated ErbB receptor tyrosine kinases.

F Kong, J Zhang, Y Li, X Hao, X Ren, H Li, P Zhou

Abstract read
In one paragraph

Article in Oncogene, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.

0numbers the graph read from it
0cells of the map it votes in
9citing 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

9 citing papers in PubMed.

  1. Article
  2. Article
  3. The emerging role for Cullin 4 family of E3 ligases in tumorigenesis.Biochimica et biophysica acta. Reviews on cancer · 2019
    Review
  4. Review
  5. Article
  6. Article
  7. Article
  8. Article
  9. Review
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

7 authors.

F Kong1] Department of Pathology and Laboratory Medicine, Weill Cornell Medical College, New York, NY, USA [2] Key Laboratory of Cancer Prevention and Therapy, Department of Biotherapy, Tianjin Medical University Cancer Institute and Hospital, Tianjin, China.
J ZhangDepartment of Pathology and Laboratory Medicine, Weill Cornell Medical College, New York, NY, USA.
Y LiDepartment of Pathology and Laboratory Medicine, Weill Cornell Medical College, New York, NY, USA.
X HaoKey Laboratory of Cancer Prevention and Therapy, Department of Biotherapy, Tianjin Medical University Cancer Institute and Hospital, Tianjin, China.
X RenKey Laboratory of Cancer Prevention and Therapy, Department of Biotherapy, Tianjin Medical University Cancer Institute and Hospital, Tianjin, China.
H LiKey Laboratory of Cancer Prevention and Therapy, Department of Biotherapy, Tianjin Medical University Cancer Institute and Hospital, Tianjin, China.
P ZhouDepartment of Pathology and Laboratory Medicine, Weill Cornell Medical College, New York, NY, USA.

Funding

Regulation of Nucleotide Excision Repair by ProteolysisR01CA098210 · NCI · WEILL MEDICAL COLL OF CORNELL UNIV · PI ZHOU, PENGBO · 2003 to 2013
$3.3M
Tumorigenic Role of the CUL4A Ubiquitin LigaseR01CA159925 · NCI · WEILL MEDICAL COLL OF CORNELL UNIV · PI SHIN, SANDRA, ZHOU, PENGBO · 2011 to 2015
$2.0M
Protein Knockout Technology/Molecular Analysis of CancerR33CA092792 · NCI · WEILL MEDICAL COLLEGE OF CORNELL UNIV · PI ZHOU, PENGBO · 2002 to 2004
$1.0M
Protein Knockout Technology/Molecular Analysis of CancerR21CA092792 · NCI · WEILL MEDICAL COLLEGE OF CORNELL UNIV · PI ZHOU, PENGBO · 2001 to 2001
$170k
NCI NIH HHS CA92792NCI NIH HHS R01 CA098210NCI NIH HHS R01 CA159925NCI NIH HHS R21 CA092792NCI NIH HHS R33 CA092792
6 · The paper itself

Abstract

Interrogating specific cellular activities often entails the dissection of posttranslational modifications or functional redundancy conferred by protein families, which demands more sophisticated research tools than simply eliminating a specific gene product by gene targeting or RNA interference. We have developed a novel methodology that involves engineering a single SCF(βTrCP)-based ubiquitin ligase that is capable of not only simultaneously targeting the entire family of ErbB receptor tyrosine kinases for ubiquitination and degradation, but also selectively recruiting only activated ErbBs. The engineered SCF(βTrCP) ubiquitin ligase effectively blocked ErbB signaling and attenuated oncogenicity in breast cancer cells, yet had little effect on the survival and growth of non-cancerous breast epithelial cells. Therefore, engineering ubiquitin ligases offers a simple research tool to dissect the specific traits of tumorigenic protein families, and provides a rapid and feasible means to expand the dimensionality of drug discovery by assessing protein families or posttranslational modifications as potential drug targets.

Indexed as

Breast NeoplasmsCell CycleCell Line, TumorFemaleHumansMitogen-Activated Protein KinasesPhosphatidylinositol 3-KinasesProtein EngineeringProteolysisReceptor Protein-Tyrosine KinasesSignal TransductionUbiquitin-Protein LigasesMitogen-Activated Protein KinasesPhosphatidylinositol 3-KinasesReceptor Protein-Tyrosine KinasesUbiquitin-Protein Ligases

Identifiers

PMID23416973
PMCPMC3930622

What OpenQuestion holds

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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.