Results 61 to 70 of about 11,198 (208)

THE STRESS RESPONSE ROLE OF SIRT2 IN CANCER AND IMMUNOLOGY [PDF]

open access: yes, 2020
150 pagesSIRT2 is one of the mammalian NAD+-dependent lysine deacylase. It has attracted growing research interest due to the broad deacylation substrate scope and diverse cellular functions.
Wang, Miao
core   +1 more source

Salmonella escapes adaptive immune response via SIRT2 mediated modulation of innate immune response in dendritic cells.

open access: yesPLoS Pathogens, 2018
Salmonella being a successful pathogen, employs a plethora of immune evasion mechanisms. This contributes to pathogenesis, persistence and also limits the efficacy of available treatment.
Mayuri Gogoi   +5 more
doaj   +1 more source

SIRT2 Contributes to the Regulation of Intestinal Cell Proliferation and DifferentiationSummary

open access: yesCellular and Molecular Gastroenterology and Hepatology, 2020
Background and Aims: Intestinal mucosa undergoes a continual process of proliferation, differentiation, and apoptosis. Disruption of this homeostasis is associated with disorders such as inflammatory bowel disease (IBD).
Chang Li   +8 more
doaj   +1 more source

Chronobiology of Cancer: How Aging Fuels Oncogenesis at the Molecular Level

open access: yesAging and Cancer, EarlyView.
This graphical abstract illustrates the key biological pathways linking aging with cancer development and progression. In the upper left, cumulative exposure to ultraviolet radiation, toxins, and reactive oxygen species (ROS) causes DNA damage and genomic instability, whereas age‐related decline in repair mechanisms, such as ATM/ATR, BER, and NER ...
Anu Singh, Aroonima Misra, Sufian Zaheer
wiley   +1 more source

SIRT2 in age-related neurodegenerative disorders

open access: yesAging, 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   +2 more
openaire   +4 more sources

Activation of GSK3β by Sirt2 is required for early lineage commitment of mouse embryonic stem cell. [PDF]

open access: yesPLoS ONE, 2013
Sirt2, a member of the NAD(+)-dependent protein deacetylase family, is increasingly recognized as a critical regulator of the cell cycle, cellular necrosis and cytoskeleton organization.
Xiaoxing Si   +6 more
doaj   +1 more source

Miro1 Protects Against Acute Kidney Injury Through Modulating Mitochondrial Homeostasis via Interaction With Sirt6

open access: yesAdvanced Science, EarlyView.
Ischemia‐reperfusion reduces Sirt6 activity, thereby increasing Miro1 acetylation. Hyperacetylated Miro1 exhibits perinuclear distribution and degradation, thereby inducing mitochondrial dysfunction and promoting apoptosis in renal tubular epithelial cells. This pathway reveals a mechanistic link between Sirt6‐mediated deacetylation and Miro1 stability
Lin Wu   +12 more
wiley   +1 more source

SIRT2 promotes murine melanoma progression through natural killer cell inhibition

open access: yesScientific Reports, 2021
SIRT2, an NAD+-dependent histone deacetylase, has been shown to play a pivotal role in various physiological processes, however, its role in cancer is currently controversial.
Manchao Zhang   +8 more
doaj   +1 more source

SIRT7‐Mediated H2BK120 Succinylation Drives Aberrant Mitophagy in Sepsis‐Associated Cognitive Dysfunction

open access: yesAdvanced Science, EarlyView.
Sepsis triggers hippocampal SIRT7 loss, promoting histone H2B succinylation and activation of the PD‐1/PD‐L1–PINK1 axis. This metabolic‐epigenetic cascade drives aberrant mitophagy and neuronal injury, ultimately causing cognitive deficits. Targeting SIRT7‐dependent succinylation offers a potential strategy to protect brain function during sepsis ...
Na Meng   +12 more
wiley   +1 more source

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

open access: yesCytoskeleton, 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   +6 more
wiley   +1 more source

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