About: Localization of mouse mitochondrial SIRT proteins: shift of SIRT3 to nucleus by co-expression with SIRT5

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rdf:type	Item
description	artículu científicu espublizáu en 2008 (ast) vědecký článek publikovaný v roce 2008 (cs) наукова стаття, опублікована в лютому 2008 (uk) 2008 թուականի Փետրուարին հրատարակուած գիտական յօդուած (hyw) 2008 թվականի փետրվարին հրատարակված գիտական հոդված (hy) مقالة علمية (نشرت في فبراير 2008) (ar) wetenschappelijk artikel (gepubliceerd op 2008/02/01) (nl) vedecký článok (publikovaný 2008/02/01) (sk) article scientifique publié en 2007 (fr) im Februar 2008 veröffentlichter wissenschaftlicher Artikel (de) scientific journal article (en)
publication date	wds:Q28504984-60C9859A-4F93-4826-886E-C5EA9729E279
publication date	2007-12-03 00:00:00Z (xsd:dateTime)
language of work or name	wds:Q28504984-13ACF566-A7BA-432C-A90A-84408F2F937A
language of work or name	English
author name string	wds:Q28504984-3D11669A-C8E5-4DB4-8134-03C8F4668F7D wds:Q28504984-4103A4D1-F279-4286-B4B0-9754E093B5B6 wds:Q28504984-85CA8EA6-B1C1-4392-8E19-F999755307F8
OpenCitations bibliographic resource ID	wds:Q28504984-765A1F96-7756-45E8-804C-7B4D8871F7DE
OpenCitations bibliographic resource ID	https://w3id.org/oc/corpus/br/2015213
author name string	Daisuke Tanaka Masahito Ogura Yasuhiko Nakamura
OpenCitations bibliographic resource ID	2015213
rdfs:label	Localization of mouse mitochondrial SIRT proteins: shift of SIRT3 to nucleus by co-expression with SIRT5 (en) Localization of mouse mitochondrial SIRT proteins: shift of SIRT3 to nucleus by co-expression with SIRT5 (nl) Localization of mouse mitochondrial SIRT proteins: shift of SIRT3 to nucleus by co-expression with SIRT5 (ast)
skos:prefLabel	Localization of mouse mitochondrial SIRT proteins: shift of SIRT3 to nucleus by co-expression with SIRT5 (en) Localization of mouse mitochondrial SIRT proteins: shift of SIRT3 to nucleus by co-expression with SIRT5 (nl) Localization of mouse mitochondrial SIRT proteins: shift of SIRT3 to nucleus by co-expression with SIRT5 (ast)
name	Localization of mouse mitochondrial SIRT proteins: shift of SIRT3 to nucleus by co-expression with SIRT5 (en) Localization of mouse mitochondrial SIRT proteins: shift of SIRT3 to nucleus by co-expression with SIRT5 (nl) Localization of mouse mitochondrial SIRT proteins: shift of SIRT3 to nucleus by co-expression with SIRT5 (ast)
author	wds:Q28504984-DB3F9ADB-4CEC-4A72-9C64-3AA572BD42B8
author	Nobuya Inagaki
title	wds:Q28504984-B80EA173-ABAB-4C68-A919-F7F9CEE9C847
title	Localization of mouse mitochondrial SIRT proteins: shift of SIRT3 to nucleus by co-expression with SIRT5 (en)
page(s)	wds:Q28504984-994F2CB7-569D-45B0-BECB-3626B5CBD1B8
page(s)	174-179
instance of	wds:Q28504984-27035295-A72C-4532-B3A5-C6AD91EF8B08
instance of	scholarly article
main subject	wds:Q28504984-48F4D6C4-D7C5-4CA1-83D4-52145E5F447E wds:Q28504984-98454065-34D7-4B84-8091-A54C70D369A3 wds:Q28504984-C584C80A-B9D8-461E-8DB0-C760BA522AD3 wds:Q28504984-D4D257E7-A8DF-4C6B-AB47-741373AE5A5C
main subject	mitochondrion Sirtuin 5 Sirtuin 3 Sirtuin 4
PubMed ID	wds:Q28504984-AFB66434-5709-49DE-834F-B461D8C481C7
PubMed ID	http://rdf.ncbi.nlm.nih.gov/pubchem/reference/18054327
PubMed ID	18054327
published in	wds:Q28504984-B5B90739-2E60-4AED-AD2B-8EAD81E9F4DF
published in	Biochemical and Biophysical Research Communications
issue	wds:Q28504984-CC101A50-CF0D-4411-8AE0-BFB9D0EF804B
volume	wds:Q28504984-F7BEB8F9-3F36-48FE-9A13-917217869F3F
issue	1
volume	366
DOI	wds:Q28504984-BA31D735-DD5C-4214-A81C-F34E3E9B1865
DOI	http://dx.doi.org/10.1016/J.BBRC.2007.11.122
DOI	10.1016/J.BBRC.2007.11.122
is about of	https://www.wikidata.org/wiki/Special:EntityData/Q28504984
is cites work of	A large set of estrogen receptor β-interacting proteins identified by tandem affinity purification in hormone-responsive human breast cancer cell nuclei Substrates and regulation mechanisms for the human mitochondrial sirtuins Sirt3 and Sirt5 SIRT5 facilitates cancer cell growth and drug resistance in non-small cell lung cancer. Using mitochondrial sirtuins as drug targets: disease implications and available compounds SIRT5 deacetylates and activates urate oxidase in liver mitochondria of mice SIRT5 Deacetylates carbamoyl phosphate synthetase 1 and regulates the urea cycle Sirtuin inhibitors. Sirtuins, bioageing, and cancer. Regulation of sirtuin function by posttranslational modifications Protective effects and mechanisms of sirtuins in the nervous system Sirtuins as novel players in the pathogenesis of diabetes mellitus Mammalian sirtuins: biological insights and disease relevance SIRT3 interacts with the daf-16 homolog FOXO3a in the mitochondria, as well as increases FOXO3a dependent gene expression Opposing effects of sirtuins on neuronal survival: SIRT1-mediated neuroprotection is independent of its deacetylase activity A new splice variant of the mouse SIRT3 gene encodes the mitochondrial precursor protein Characterization of the murine SIRT3 mitochondrial localization sequence and comparison of mitochondrial enrichment and deacetylase activity of long and short SIRT3 isoforms Where in the cell is SIRT3?--functional localization of an NAD+-dependent protein deacetylase Calorie restriction and the exercise of chromatin The emerging and diverse roles of sirtuins in cancer: a clinical perspective Pathways for ischemic cytoprotection: role of sirtuins in caloric restriction, resveratrol, and ischemic preconditioning The importance of NAD in multiple sclerosis SIRT3 is a stress-responsive deacetylase in cardiomyocytes that protects cells from stress-mediated cell death by deacetylation of Ku70 Function of the SIRT3 mitochondrial deacetylase in cellular physiology, cancer, and neurodegenerative disease SIRT3 and cancer: tumor promoter or suppressor? Sirtuin-3 (SIRT3), a novel potential therapeutic target for oral cancer. SIRT3 functions in the nucleus in the control of stress-related gene expression Mitochondrial SIRT3 and heart disease Sirtinol treatment reduces inflammation in human dermal microvascular endothelial cells Sirtuins: molecular traffic lights in the crossroad of oxidative stress, chromatin remodeling, and transcription The coordination of nuclear and mitochondrial communication during aging and calorie restriction Protein deacetylation by sirtuins: delineating a post-translational regulatory program responsive to nutrient and redox stressors The effect of marathon on mRNA expression of anti-apoptotic and pro-apoptotic proteins and sirtuins family in male recreational long-distance runners Sirtuin 1 in immune regulation and autoimmunity Respected Sir(2): magic target for diabetes Caloric excess or restriction mediated modulation of metabolic enzyme acetylation-proposed effects on cardiac growth and function The emerging characterization of lysine residue deacetylation on the modulation of mitochondrial function and cardiovascular biology Beyond histone and deacetylase: an overview of cytoplasmic histone deacetylases and their nonhistone substrates

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