Results 71 to 80 of about 10,461 (217)

SIRT6‐Mediated Deacetylation of ATF3 Promotes Silica‐Induced Lung Fibrosis by Enhancing its Nuclear Import via Binding to Importin α

Advanced Science, EarlyView.
SIRT6‐mediated ATF3 acetylation drives MGARP transcription and mitochondrial dysfunction in macrophages, promoting macrophage senescence and pulmonary fibrosis. Mechanistically, HSP70/Importin α competitively binds to ATF3, modulating its nuclear translocation.
Demin Cheng, Wenxia Bu, Fengxu Wang, Yueyuan Jin, Rongzhu Liu, Rui Zhao, Xuehai Wang, Mengna Jiang, Jinping Shen, Xinhang Cheng, Zuming Chen, Li Zhu, Jinlong Li, Zhenzhong Ge, Shichen Miao, Haotian Xu, Xiaoyu Zhou, Dongming Wang, Xinyuan Zhao   +18 more
wiley   +1 more source

SIRT1 and SIRT2: emerging targets in neurodegeneration

EMBO Molecular Medicine, 2013
Abstract Sirtuins are NAD‐dependent protein deacetylases known to have protective effects against age‐related diseases such as cancer, diabetes, cardiovascular and neurodegenerative diseases. In mammals, there are seven sirtuins (SIRT1‐7), which display diversity in subcellular localization and function.
Donmez G, Outeiro TF
openaire   +5 more sources

Long‐Term Ambient Benzene Exposure and Brain Disorders Among Urban Adults: Effect Modification by Genetic Susceptibility and Potential Mediation by Plasma Proteins

Advanced Science, EarlyView.
Low‐level ambient benzene exposure is associated with increased risks of multiple brain disorders in urban adults. Genetic susceptibility modifies these associations, while plasma proteomics points to potential biological pathways linking benzene exposure to adverse brain health.
Jianhui Guo, Xia Zhong, Petros Koutrakis, Carolina L. Zilli Vieira, Feifei Si, Yaqi Wang, Xinyao Lian, Yi Fan, Zhaokun Wang, Shaodan Huang, Jing Li   +10 more
wiley   +1 more source

NAD+ Metabolism Licenses Zygotic Genome Activation via PARP7‐Mediated ADP‐Ribosylation of UHRF1 in Mouse Early Embryos

Advanced Science, EarlyView.
This study uncovers a metabolic‐epigenetic axis licensing zygotic genome activation (ZGA) in mouse embryos. A developmental decline in NAD+ levels activates PARP7, which mono‐ADP‐ribosylates and stabilizes UHRF1. This modification promotes the establishment of permissive histone acetylation marks, thereby facilitating timely ZGA.
Guangyi Cao, Ziqi Zhang, Anqi Chen, Yanbo Liu, Yuling Lin, Lina Yu, Ruixin Shi, Aolei Guo, Yan Mao, Ganggui Lou, Chaojun Li, Luhong Wen, Guijun Yan, Haixiang Sun   +13 more
wiley   +1 more source

Colocalization of SIRT2 with the centrosome. [PDF]

, 2013
(A) U2OS cells expressing SIRT2-HA were stained for HA (green) and for γ-tubulin (red) and analyzed by confocal microscopy. (B) HeLa cells were stained with antisera for endogenous SIRT2 (green) and Aurora A (red) and analyzed by confocal microscopy. (C)
Brian J. North (78353), Eric Verdin (3608)   +1 more
core   +1 more source

Recombinant Monoclonal Antibodies for Detecting the Tubulin Post‐Translational Modifications Glutamylation and Lysine‐40 Acetylation

Cytoskeleton, EarlyView.
ABSTRACT Post‐translational modifications (PTMs) to tubulin subunits in microtubule filaments are thought to comprise a component of the tubulin code that specifies microtubule functions in cell physiology and animal development. Acetylation of Lysine‐40 (K40) on α‐tubulin (αTub‐K40ac) and glutamylation of both α‐ and β‐tubulin are two tubulin PTMs of ...
Lynne Blasius, Ezekiel C. Thomas, Erik H. Collet, Erin Jenson, Chad G. Pearson, Ryoma Ohi, Kristen J. Verhey   +6 more
wiley   +1 more source

SIRT2 stops cells

The Journal of Cell Biology, 2008
Recent work from [Pandithage et al.][1] reveals a new pathway for controlling cell movement that involves a cancer enabler and a member of a protein family best known for boosting longevity. The researchers chanced on the discovery while investigating the oncogene Myc, which is overactive in ...
openaire   +2 more sources

SIRT2 in age-related neurodegenerative disorders

Aging, 2018
Sirtuin 2 (SIRT2) is one of seven members of the NAD+-dependent histone deacetylases (HDAC) family of proteins. Sirtuins play diverse roles in cellular metabolism and the aging process. SIRT2 is located in the nucleus, cytoplasm, and mitochondria, is highly expressed in the central nervous system (CNS), and has been reported to regulate a variety of ...
Fourcade, Stéphane, Outeiro, Tiago F., Pujol Onofre, Aurora   +2 more
openaire   +4 more sources

Microglial SIRT2 deficiency aggravates cognitive decline and amyloid pathology in Alzheimer's disease [PDF]

Sirtuin 2 (SIRT2), a NAD+-dependent deacetylase, has been implicated in aging and neurodegenerative diseases such as Alzheimer's disease (AD). While global SIRT2 inhibition has shown promise in reducing amyloid-beta pathology and cognitive deficits in ...
Fernández-Irigoyen, Joaquín, Guruceaga, Elisabeth, Mera-Delgado, MCarmen, Puerta, Elena, Sola-Sevilla, Noemi, Tordera, Rosa M, García-Carracedo, Lucía, Garmendia-Berges, Maider, Anaya-Cubero, Elena, Expósito, Sara, Santamaria, Enrique, Martin, Eduardo D, Solas, Maite, Aleixo, Mikel   +13 more
core   +1 more source

Mutational analysis of SIRT2 NES sequence. [PDF]

, 2013
(A) HeLa cells were transfected with GFP-SIRT2 wild-type or single and double point mutants of the proposed NES sequence. (B) Subcellular distribution results of all single and double mutants of SIRT2 NES analyzed in (A).
Brian J. North (78353), Eric Verdin (3608)   +1 more
core   +1 more source