Endothelial SIRT1 prevents adverse arterial remodeling by facilitating HERC2-mediated degradation of acetylated LKB1

10.18632/oncotarget.9687

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Main Authors:	Bai, B, Man, A.W.C, Kangmin Yang, State Key Laboratory of Pharmaceutical Biotechnology, Department of Pharmacology and Pharmacy, The University of Hong Kong, Hong Kong, Yumeng Guo, State Key Laboratory of Pharmaceutical Biotechnology, Department of Pharmacology and Pharmacy, The University of Hong Kong, Hong Kong, Cheng Xu, State Key Laboratory of Pharmaceutical Biotechnology, Department of Pharmacology and Pharmacy, The University of Hong Kong, Hong Kong, Tse, H.-F, Han, W, Bloksgaard, M, De Mey, J.G.R, Vanhoutte, P.M, Xu, A, Wang, Y
Other Authors:	DUKE-NUS MEDICAL SCHOOL
Format:	Article
Published:	Impact Journals LLC 2020
Subjects:	endothelial nitric oxide synthase HECT and RLD domain containing E3 ubiquitin protein ligase 2 protein kinase protein kinase LKB1 sirtuin 1 transforming growth factor beta1 unclassified drug guanine nucleotide exchange factor HERC2 protein, human protein serine threonine kinase SIRT1 protein, human STK11 protein, human ubiquitin aging animal cell Article binding affinity binding site bioaccumulation cell aging cell proliferation chromatin immunoprecipitation complex formation controlled study down regulation gene gene function gene identification HECT and RLD domain containing E3 ubiquitin protein ligase 2 gene human human cell in vitro study molecular dynamics mouse nonhuman polymerase chain reaction protein binding protein determination protein function protein protein interaction quantitative analysis sirtuin 1 gene site directed mutagenesis vascular aging vascular remodeling vascular smooth muscle cell 3T3-L1 cell line acetylation animal artery carotid artery chemistry endothelium cell genetics homeostasis metabolism pathology protein processing transgenic mouse tumor cell line vascular endothelium vascular smooth muscle 3T3-L1 Cells Acetylation Animals Arteries Carotid Arteries Cell Line, Tumor Endothelial Cells Endothelium, Vascular Guanine Nucleotide Exchange Factors Homeostasis Humans Mice Mice, Transgenic Muscle, Smooth, Vascular Mutagenesis, Site-Directed Nitric Oxide Synthase Type III Protein Processing, Post-Translational Protein-Serine-Threonine Kinases Sirtuin 1 Ubiquitin Vascular Remodeling
Online Access:	https://scholarbank.nus.edu.sg/handle/10635/180387
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Institution:	National University of Singapore

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spelling	sg-nus-scholar.10635-1803872023-11-01T08:19:44Z Endothelial SIRT1 prevents adverse arterial remodeling by facilitating HERC2-mediated degradation of acetylated LKB1 Bai, B Man, A.W.C Kangmin Yang, State Key Laboratory of Pharmaceutical Biotechnology, Department of Pharmacology and Pharmacy, The University of Hong Kong, Hong Kong Yumeng Guo, State Key Laboratory of Pharmaceutical Biotechnology, Department of Pharmacology and Pharmacy, The University of Hong Kong, Hong Kong Cheng Xu, State Key Laboratory of Pharmaceutical Biotechnology, Department of Pharmacology and Pharmacy, The University of Hong Kong, Hong Kong Tse, H.-F Han, W Bloksgaard, M De Mey, J.G.R Vanhoutte, P.M Xu, A Wang, Y DUKE-NUS MEDICAL SCHOOL endothelial nitric oxide synthase HECT and RLD domain containing E3 ubiquitin protein ligase 2 protein kinase protein kinase LKB1 sirtuin 1 transforming growth factor beta1 unclassified drug endothelial nitric oxide synthase guanine nucleotide exchange factor HERC2 protein, human protein serine threonine kinase SIRT1 protein, human sirtuin 1 STK11 protein, human ubiquitin aging animal cell Article binding affinity binding site bioaccumulation cell aging cell proliferation chromatin immunoprecipitation complex formation controlled study down regulation gene gene function gene identification HECT and RLD domain containing E3 ubiquitin protein ligase 2 gene human human cell in vitro study molecular dynamics mouse nonhuman polymerase chain reaction protein binding protein determination protein function protein protein interaction quantitative analysis sirtuin 1 gene site directed mutagenesis vascular aging vascular remodeling vascular smooth muscle cell 3T3-L1 cell line acetylation animal artery carotid artery chemistry endothelium cell genetics homeostasis metabolism pathology protein processing transgenic mouse tumor cell line vascular endothelium vascular remodeling vascular smooth muscle 3T3-L1 Cells Acetylation Animals Arteries Carotid Arteries Cell Line, Tumor Endothelial Cells Endothelium, Vascular Guanine Nucleotide Exchange Factors Homeostasis Humans Mice Mice, Transgenic Muscle, Smooth, Vascular Mutagenesis, Site-Directed Nitric Oxide Synthase Type III Protein Processing, Post-Translational Protein-Serine-Threonine Kinases Sirtuin 1 Ubiquitin Vascular Remodeling 10.18632/oncotarget.9687 Oncotarget 7 26 39065-39081 2020-10-26T08:45:19Z 2020-10-26T08:45:19Z 2016 Article Bai, B, Man, A.W.C, Kangmin Yang, State Key Laboratory of Pharmaceutical Biotechnology, Department of Pharmacology and Pharmacy, The University of Hong Kong, Hong Kong, Yumeng Guo, State Key Laboratory of Pharmaceutical Biotechnology, Department of Pharmacology and Pharmacy, The University of Hong Kong, Hong Kong, Cheng Xu, State Key Laboratory of Pharmaceutical Biotechnology, Department of Pharmacology and Pharmacy, The University of Hong Kong, Hong Kong, Tse, H.-F, Han, W, Bloksgaard, M, De Mey, J.G.R, Vanhoutte, P.M, Xu, A, Wang, Y (2016). Endothelial SIRT1 prevents adverse arterial remodeling by facilitating HERC2-mediated degradation of acetylated LKB1. Oncotarget 7 (26) : 39065-39081. ScholarBank@NUS Repository. https://doi.org/10.18632/oncotarget.9687 1949-2553 https://scholarbank.nus.edu.sg/handle/10635/180387 Attribution 4.0 International http://creativecommons.org/licenses/by/4.0/ Impact Journals LLC Unpaywall 20201031
institution	National University of Singapore
building	NUS Library
continent	Asia
country	Singapore Singapore
content_provider	NUS Library
collection	ScholarBank@NUS
topic	endothelial nitric oxide synthase HECT and RLD domain containing E3 ubiquitin protein ligase 2 protein kinase protein kinase LKB1 sirtuin 1 transforming growth factor beta1 unclassified drug endothelial nitric oxide synthase guanine nucleotide exchange factor HERC2 protein, human protein serine threonine kinase SIRT1 protein, human sirtuin 1 STK11 protein, human ubiquitin aging animal cell Article binding affinity binding site bioaccumulation cell aging cell proliferation chromatin immunoprecipitation complex formation controlled study down regulation gene gene function gene identification HECT and RLD domain containing E3 ubiquitin protein ligase 2 gene human human cell in vitro study molecular dynamics mouse nonhuman polymerase chain reaction protein binding protein determination protein function protein protein interaction quantitative analysis sirtuin 1 gene site directed mutagenesis vascular aging vascular remodeling vascular smooth muscle cell 3T3-L1 cell line acetylation animal artery carotid artery chemistry endothelium cell genetics homeostasis metabolism pathology protein processing transgenic mouse tumor cell line vascular endothelium vascular remodeling vascular smooth muscle 3T3-L1 Cells Acetylation Animals Arteries Carotid Arteries Cell Line, Tumor Endothelial Cells Endothelium, Vascular Guanine Nucleotide Exchange Factors Homeostasis Humans Mice Mice, Transgenic Muscle, Smooth, Vascular Mutagenesis, Site-Directed Nitric Oxide Synthase Type III Protein Processing, Post-Translational Protein-Serine-Threonine Kinases Sirtuin 1 Ubiquitin Vascular Remodeling
spellingShingle	endothelial nitric oxide synthase HECT and RLD domain containing E3 ubiquitin protein ligase 2 protein kinase protein kinase LKB1 sirtuin 1 transforming growth factor beta1 unclassified drug endothelial nitric oxide synthase guanine nucleotide exchange factor HERC2 protein, human protein serine threonine kinase SIRT1 protein, human sirtuin 1 STK11 protein, human ubiquitin aging animal cell Article binding affinity binding site bioaccumulation cell aging cell proliferation chromatin immunoprecipitation complex formation controlled study down regulation gene gene function gene identification HECT and RLD domain containing E3 ubiquitin protein ligase 2 gene human human cell in vitro study molecular dynamics mouse nonhuman polymerase chain reaction protein binding protein determination protein function protein protein interaction quantitative analysis sirtuin 1 gene site directed mutagenesis vascular aging vascular remodeling vascular smooth muscle cell 3T3-L1 cell line acetylation animal artery carotid artery chemistry endothelium cell genetics homeostasis metabolism pathology protein processing transgenic mouse tumor cell line vascular endothelium vascular remodeling vascular smooth muscle 3T3-L1 Cells Acetylation Animals Arteries Carotid Arteries Cell Line, Tumor Endothelial Cells Endothelium, Vascular Guanine Nucleotide Exchange Factors Homeostasis Humans Mice Mice, Transgenic Muscle, Smooth, Vascular Mutagenesis, Site-Directed Nitric Oxide Synthase Type III Protein Processing, Post-Translational Protein-Serine-Threonine Kinases Sirtuin 1 Ubiquitin Vascular Remodeling Bai, B Man, A.W.C Kangmin Yang, State Key Laboratory of Pharmaceutical Biotechnology, Department of Pharmacology and Pharmacy, The University of Hong Kong, Hong Kong Yumeng Guo, State Key Laboratory of Pharmaceutical Biotechnology, Department of Pharmacology and Pharmacy, The University of Hong Kong, Hong Kong Cheng Xu, State Key Laboratory of Pharmaceutical Biotechnology, Department of Pharmacology and Pharmacy, The University of Hong Kong, Hong Kong Tse, H.-F Han, W Bloksgaard, M De Mey, J.G.R Vanhoutte, P.M Xu, A Wang, Y Endothelial SIRT1 prevents adverse arterial remodeling by facilitating HERC2-mediated degradation of acetylated LKB1
description	10.18632/oncotarget.9687
author2	DUKE-NUS MEDICAL SCHOOL
author_facet	DUKE-NUS MEDICAL SCHOOL Bai, B Man, A.W.C Kangmin Yang, State Key Laboratory of Pharmaceutical Biotechnology, Department of Pharmacology and Pharmacy, The University of Hong Kong, Hong Kong Yumeng Guo, State Key Laboratory of Pharmaceutical Biotechnology, Department of Pharmacology and Pharmacy, The University of Hong Kong, Hong Kong Cheng Xu, State Key Laboratory of Pharmaceutical Biotechnology, Department of Pharmacology and Pharmacy, The University of Hong Kong, Hong Kong Tse, H.-F Han, W Bloksgaard, M De Mey, J.G.R Vanhoutte, P.M Xu, A Wang, Y
format	Article
author	Bai, B Man, A.W.C Kangmin Yang, State Key Laboratory of Pharmaceutical Biotechnology, Department of Pharmacology and Pharmacy, The University of Hong Kong, Hong Kong Yumeng Guo, State Key Laboratory of Pharmaceutical Biotechnology, Department of Pharmacology and Pharmacy, The University of Hong Kong, Hong Kong Cheng Xu, State Key Laboratory of Pharmaceutical Biotechnology, Department of Pharmacology and Pharmacy, The University of Hong Kong, Hong Kong Tse, H.-F Han, W Bloksgaard, M De Mey, J.G.R Vanhoutte, P.M Xu, A Wang, Y
author_sort	Bai, B
title	Endothelial SIRT1 prevents adverse arterial remodeling by facilitating HERC2-mediated degradation of acetylated LKB1
title_short	Endothelial SIRT1 prevents adverse arterial remodeling by facilitating HERC2-mediated degradation of acetylated LKB1
title_full	Endothelial SIRT1 prevents adverse arterial remodeling by facilitating HERC2-mediated degradation of acetylated LKB1
title_fullStr	Endothelial SIRT1 prevents adverse arterial remodeling by facilitating HERC2-mediated degradation of acetylated LKB1
title_full_unstemmed	Endothelial SIRT1 prevents adverse arterial remodeling by facilitating HERC2-mediated degradation of acetylated LKB1
title_sort	endothelial sirt1 prevents adverse arterial remodeling by facilitating herc2-mediated degradation of acetylated lkb1
publisher	Impact Journals LLC
publishDate	2020
url	https://scholarbank.nus.edu.sg/handle/10635/180387
_version_	1781792379106230272

Endothelial SIRT1 prevents adverse arterial remodeling by facilitating HERC2-mediated degradation of acetylated LKB1

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