FBXW7 E3 Ubiquitin Ligase: Degrading, Not Degrading, or Being Degraded

Protein & Cell - Germany
doi 10.1007/s13238-019-0652-x
Full Text
Abstract

Available in full text

Date
Authors
Publisher

Springer Science and Business Media LLC

Related search

Fbxw7 Acts as an E3 Ubiquitin Ligase That Targets C-Myb for Nemo-Like Kinase (NLK)-induced Degradation

Journal of Biological Chemistry
BiochemistryCell BiologyMolecular Biology
2008English

Functional Dissection of a HECT Ubiquitin E3 Ligase

Molecular and Cellular Proteomics
BiochemistryMedicineAnalytical ChemistryMolecular Biology
2007English

Ubiquitin E3 Ligase MARCH7 Promotes Ovarian Tumor Growth

Oncotarget
Oncology
2015English

E3 Ligase FBXW7 Aggravates TMPD-induced Systemic Lupus Erythematosus by Promoting Cell Apoptosis

Cellular and Molecular Immunology
Infectious DiseasesMedicineAllergyImmunology
2018English

CHIP Is a U-Box-Dependent E3 Ubiquitin Ligase

Journal of Biological Chemistry
BiochemistryCell BiologyMolecular Biology
2001English

miR-367 Stimulates WNT Cascade Activation Through Degrading FBXW7 in NSCLC Stem Cells

Cell Cycle
MedicineDevelopmental BiologyCell BiologyMolecular Biology
2017English

Insulin-Induced Gene 1 (INSIG1) Inhibits HIV-1 Production by Degrading Gag via Activity of the Ubiquitin Ligase TRC8

Journal of Biological Chemistry
BiochemistryCell BiologyMolecular Biology
2018English

E3 Ubiquitin Ligase-Mediated Regulation of Bone Formation and Tumorigenesis

Cell Death and Disease
Molecular NeuroscienceImmunologyCell BiologyCancer ResearchCellularMedicine
2013English

The Ubiquitin Ligase FBXW7 Modulates Leukemia-Initiating Cell Activity by Regulating MYC Stability

Cell
BiochemistryGeneticsMolecular Biology
2013English

Amanote Research

Note-taking for researchers

Follow Amanote

© 2024 Amaplex Software S.P.R.L. All rights reserved.

Privacy PolicyRefund Policy