Cargando…

Redox regulation of the proteasome via S-glutathionylation()

The proteasome is a multimeric and multicatalytic intracellular protease responsible for the degradation of proteins involved in cell cycle control, various signaling processes, antigen presentation, and control of protein synthesis. The central catalytic complex of the proteasome is called the 20S...

Descripción completa

Detalles Bibliográficos
Autores principales:	Demasi, Marilene, Netto, Luis E.S., Silva, Gustavo M., Hand, Adrian, de Oliveira, Cristiano L.P., Bicev, Renata N., Gozzo, Fabio, Barros, Mario H., Leme, Janaina M.M., Ohara, Erina
Formato:	Online Artículo Texto
Lenguaje:	English
Publicado:	Elsevier 2013
Materias:	Review Article
Acceso en línea:	https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3881202/ https://www.ncbi.nlm.nih.gov/pubmed/24396728 http://dx.doi.org/10.1016/j.redox.2013.12.003

Ejemplares similares

Glucose restriction in Saccharomyces cerevisiae modulates the phosphorylation pattern of the 20S proteasome and increases its activity
por: Bicev, Renata Naporano, et al.
Publicado: (2023)

Glutathione in Protein Redox Modulation through S-Glutathionylation and S-Nitrosylation
por: Kalinina, Elena, et al.
Publicado: (2021)

Development of ‘Redox Arrays’ for identifying novel glutathionylated proteins in the secretome
por: Mullen, Lisa, et al.
Publicado: (2015)

Cysteine Glutathionylation Acts as a Redox Switch in Endothelial Cells
por: Lermant, Agathe, et al.
Publicado: (2019)

Plasticity in plastid redox networks: evolution of glutathione-dependent redox cascades and glutathionylation sites
por: Müller-Schüssele, Stefanie J., et al.
Publicado: (2021)

Redox amplification of apoptosis by caspase-dependent cleavage of glutaredoxin 1 and S-glutathionylation of Fas
por: Anathy, Vikas, et al.
Publicado: (2009)

S-Glutathionylation of an Auxiliary Subunit Confers Redox Sensitivity to Kv4 Channel Inactivation
por: Jerng, Henry H., et al.
Publicado: (2014)

Redox Regulation by Protein S-Glutathionylation: From Molecular Mechanisms to Implications in Health and Disease
por: Musaogullari, Aysenur, et al.
Publicado: (2020)

Identification of DUOX1-dependent redox signaling through protein S-glutathionylation in airway epithelial cells()
por: Hristova, Milena, et al.
Publicado: (2014)

The redox mechanism for vascular barrier dysfunction associated with metabolic disorders: Glutathionylation of Rac1 in endothelial cells
por: Han, Jingyan, et al.
Publicado: (2016)

Integrated Redox Sensor and Effector Functions for Tetrahydrobiopterin- and Glutathionylation-dependent Endothelial Nitric-oxide Synthase Uncoupling
por: Crabtree, Mark J., et al.
Publicado: (2013)

Basal Glutathionylation of Na,K-ATPase α-Subunit Depends on Redox Status of Cells during the Enzyme Biosynthesis
por: Mitkevich, Vladimir A., et al.
Publicado: (2016)

The Cysteine-Rich Protein Thimet Oligopeptidase as a Model of the Structural Requirements for S-glutathiolation and Oxidative Oligomerization
por: Malvezzi, Alberto, et al.
Publicado: (2012)

The promoter of filamentation (POF1) protein from Saccharomyces cerevisiae is an ATPase involved in the protein quality control process
por: Costa, Iris M, et al.
Publicado: (2011)

Protein Glutathionylation in Cardiovascular Diseases
por: Pastore, Anna, et al.
Publicado: (2013)

Role of Glutathionylation in Infection and Inflammation
por: Checconi, Paola, et al.
Publicado: (2019)

Measurement of S-glutathionylated proteins by HPLC
por: Giustarini, Daniela, et al.
Publicado: (2021)

Cellular Redox Imbalance and Changes of Protein S-glutathionylation Patterns Are Associated with Senescence Induced by Oncogenic H-Ras
por: Armeni, Tatiana, et al.
Publicado: (2012)

Stress-Induced Protein S-Glutathionylation and S-Trypanothionylation in African Trypanosomes—A Quantitative Redox Proteome and Thiol Analysis
por: Ulrich, Kathrin, et al.
Publicado: (2017)

Role of Glutaredoxin-1 and Glutathionylation in Cardiovascular Diseases
por: Burns, Mannix, et al.
Publicado: (2020)

Redox regulation of proteasome function
por: Lefaki, Maria, et al.
Publicado: (2017)

A novel approach for predicting protein S-glutathionylation
por: Anashkina, Anastasia A., et al.
Publicado: (2020)

S-Glutathionylation in Monocyte and Macrophage (Dys)Function
por: Ullevig, Sarah, et al.
Publicado: (2013)

S-glutathionylation reactions in mitochondrial function and disease
por: Mailloux, Ryan J., et al.
Publicado: (2014)

Protein Glutathionylation in the Pathogenesis of Neurodegenerative Diseases
por: Cha, Sun Joo, et al.
Publicado: (2017)

Effects of an Anticarcinogenic Bowman-Birk Protease Inhibitor on Purified 20S Proteasome and MCF-7 Breast Cancer Cells
por: Souza, Larissa da Costa, et al.
Publicado: (2014)

Stereoselectivity of Aldose Reductase in the Reduction of Glutathionyl-Hydroxynonanal Adduct
por: Balestri, Francesco, et al.
Publicado: (2019)

A novel proteasome inhibitor acting in mitochondrial dysfunction, ER stress and ROS production
por: Maria, Durvanei Augusto, et al.
Publicado: (2012)

Reversible Silencing of CFTR Chloride Channels by Glutathionylation
por: Wang, Wei, et al.
Publicado: (2005)

Prediction of S-Glutathionylation Sites Based on Protein Sequences
por: Sun, Chenglei, et al.
Publicado: (2013)

Immunoprecipitation methods to identify S-glutathionylation in target proteins
por: Butturini, Elena, et al.
Publicado: (2019)

S-glutathionylation, friend or foe in cardiovascular health and disease
por: Rashdan, N.A., et al.
Publicado: (2020)

Protein Glutathionylation and Glutaredoxin: Role in Neurodegenerative Diseases
por: A., Haseena P., et al.
Publicado: (2022)

Changes in Hemoglobin Properties in Complex with Glutathione and after Glutathionylation
por: Kuleshova, Iuliia D., et al.
Publicado: (2023)

Alterations of the Intracellular Peptidome in Response to the Proteasome Inhibitor Bortezomib
por: Gelman, Julia S., et al.
Publicado: (2013)

S-glutathionylation activates STIM1 and alters mitochondrial homeostasis
por: Hawkins, Brian J., et al.
Publicado: (2010)

The proteasome and the degradation of oxidized proteins: Part III—Redox regulation of the proteasomal system
por: Höhn, Tobias Jung Annika, et al.
Publicado: (2014)

S-glutathionylation of buccal cell proteins as biomarkers of exposure to hydrogen peroxide
por: Grek, Christina L., et al.
Publicado: (2014)

The siRNA suppressor RTL1 is redox-regulated through glutathionylation of a conserved cysteine in the double-stranded-RNA-binding domain
por: Charbonnel, Cyril, et al.
Publicado: (2017)

GSTP1-mediated S-glutathionylation of Pik3r1 is a redox hub that inhibits osteoclastogenesis through regulating autophagic flux
por: Ji, Xiaoxiao, et al.
Publicado: (2023)

Cannot write session to /tmp/vufind_sessions/sess_p3epo1novlo4brskmhtlcbp8ft