Results 121 to 130 of about 55,883 (307)

ATRIP Deacetylation by SIRT2 Drives ATR Checkpoint Activation by Promoting Binding to RPA-ssDNA

Cell Reports, 2016
The ataxia telangiectasia-mutated and Rad3-related (ATR) kinase checkpoint pathway maintains genome integrity; however, the role of the sirtuin 2 (SIRT2) acetylome in regulating this pathway is not clear.
Hui Zhang, PamelaSara E. Head, Waaqo Daddacha, Seong-Hoon Park, Xingzhe Li, Yunfeng Pan, Matthew Z. Madden, Duc M. Duong, Maohua Xie, Bing Yu, Matthew D. Warren, Elaine A. Liu, Vishal R. Dhere, Chunyang Li, Ivan Pradilla, Mylin A. Torres, Ya Wang, William S. Dynan, Paul W. Doetsch, Xingming Deng, Nicholas T. Seyfried, David Gius, David S. Yu   +22 more
doaj   +1 more source

Sirtuins and their influence on autophagy

Journal of Cellular Biochemistry, 2023
AbstractSirtuins and autophagy are well‐characterized agents that can promote longevity and protect individual organisms from age‐associated diseases like neurodegenerative disorders. In recent years, more and more data has been obtained that discerned potential overlaps and crosstalk between Sirtuin proteins and autophagic activity.
openaire   +2 more sources

Menopause hormone therapy in women with cardiovascular risk factors or established ischemic heart disease: A joint FIGO and WHF position paper

International Journal of Gynecology &Obstetrics, EarlyView.
Integrated approach to menopausal hormone therapy in women with cardiovascular risk factors or established ischemic heart disease, from early treatment initiation and risk stratification to individualized therapy, multidisciplinary follow‐up, and health‐system recommendations.
Chiara Benedetto, Martha Gulati, Suvarna S. Khadilkar, Angela H. E. M. Maas, Federica Frezet, Gláucia Maria Moraes de Oliveira, Andrea R. Genazzani, Hema Divakar, Athena Poppas, on behalf of the World Heart Federation (WHF) and the International Federation of Gynecology and Obstetrics (FIGO)   +9 more
wiley   +1 more source

The sirtuins in the pathogenesis of cancer

Clinical Epigenetics, 2010
Abstract Aging is the natural trace that time leaves behind on life during blossom and maturation, culminating in senescence and death. This process is accompanied by a decline in the healthy function of multiple organ systems, leading to increased incidence and mortality from diseases such as diabetes, cancer, cardiovascular disease, and ...
Voelter-Mahlknecht, Susanne, Mahlknecht, Ulrich   +1 more
openaire   +2 more sources

Epigenetic Regulation in the Pathogenesis of Renal Inflammation: Insights and Therapeutic Potentials

iNew Medicine, EarlyView.
ABSTRACT Renal inflammation is a common pathological process in various kidney diseases, often initiated by factors such as toxins, ischemia, or autoimmune reactions. This inflammatory response can result in structural damage and a rapid decline in renal function.
Yu‐Hang Dong, Xiao‐Yu Shen, Han‐Cheng Jin, Xiang‐Yu Li, Hao He, Xiao‐Ming Meng   +5 more
wiley   +1 more source

Adss1–HDAC3 Interaction: A Novel Mechanism for Epigenetic Regulation of Metabolism in Adipose Tissue

iNew Medicine, EarlyView.
ABSTRACT Obesity and its related metabolic disorders have emerged as global public health challenges with underlying mechanisms involving an imbalance between energy storage and expenditure in the adipose tissue. In recent years, with the deepening research on adipose tissue metabolism, the cross talk between metabolic enzymes and epigenetic regulation
Jiarui Zhao, Jingjing Sun, Yan Lu, Ying Yang   +3 more
wiley   +1 more source

Research Progress of Berberine in Kidney Disease: Targeting Mitochondria and Ferroptosis

iNew Medicine, EarlyView.
This figure illustrates the model‐specific renoprotective mechanisms of berberine (BBR) across three major kidney diseases. From left to right, the diagram shows that BBR targets distinct core pathways depending on the pathological context: in diabetic nephropathy (DN), BBR activates AMPK to improve mitochondrial energy metabolism; in acute kidney ...
Liuqing Wang, Rongyu Guo, Xiaojun Feng, Liqin Tang   +3 more
wiley   +1 more source

A pharmaco‐epistasis strategy reveals a new cell size controlling pathway in yeast

Molecular Systems Biology, 2013
Cell size is a complex quantitative trait resulting from interactions between intricate genetic networks and environmental conditions. Here, taking advantage of previous studies that uncovered hundreds of genes affecting budding yeast cell size ...
Fabien Moretto, Isabelle Sagot, Bertrand Daignan‐Fornier, Benoît Pinson   +3 more
doaj   +1 more source

The mechanism of sirtuin 2-mediated exacerbation of alpha-synuclein toxicity in models of Parkinson disease. [PDF]

, 2017
Sirtuin genes have been associated with aging and are known to affect multiple cellular pathways. Sirtuin 2 was previously shown to modulate proteotoxicity associated with age-associated neurodegenerative disorders such as Alzheimer and Parkinson disease
Fonseca L, Moniot, S., Enguita FJ, Francelle L, Hugo Vicente Miranda, Moniot Sébastien, Diana F Lázaro, Vicente Miranda, Hugo, Fonseca, L., Guerreiro P, de Oliveira Rita Machado, Diana F. Lázaro (659832), Éva M Szegö, Sébastien Moniot (685066), Gerhardt, Ellen, Qiang Tong (231446), Zweckstetter, Markus, Szego EM, Lazaro DF, Markus Zweckstetter, Zweckstetter M, Renato Martinho (3812251), Pinho, R., Kugler S, Penque D, Martinho Renato, Pais Teresa Faria, Steegborn C, Lázaro, Diana F, Hugo Vicente Miranda (3812248), Hilal Ahmed Lashuel, Guerreiro, P., Penque, D., Ellen Gerhardt, Fonseca Luis, Marijanovic, Zrinka, Lázaro, Diana F., Szegö Éva M., Gerhardt Ellen, Enguita, F., Pedro Antas, Tong, Qiang, Hilal Ahmed Lashuel (3812239), Francesca Munari, Luis Fonseca, Pinho R, Martinho, R., Outeiro, T.F., Lashuel HA, Lázaro, D.F., de Oliveira RM, Steegborn, Clemens, Gerhardt E, Patrícia Guerreiro, Francisco Javier Enguita (218113), Bruno Fauvet, Szegoe, Eva Monika, Francisco Javier Enguita, Clemens Steegborn (117996), Miranda, H., Guerreiro, Patricia S., Laetitia Francelle, Munari, F., Vicente Miranda Hugo, Sébastien Moniot, Laetitia Francelle (3812245), Kügler Sebastian, Fauvet, Bruno, Antas Pedro, Outeiro TF, Raquel Pinho, Teresa Faria Pais, Enguita, Francisco Javier, Fonseca-Ornelas, Luis, Vicente Miranda H, Fauvet Bruno, Martinho, Renato, Tong Q, Guerreiro, Patrícia, de Oliveira, Rita Machado, Qiang Tong, Moniot S, Machado de Oliveira, R., Lázaro Diana F., Pinho Raquel, Teresa Faria Pais (3812236), Marijanovic Zrinka, Pais, T., Outeiro, T., Lashuel, Hilal Ahmed, Patrícia Guerreiro (659837), Tong Qiang, Sebastian Kügler (75267), Éva M. Szegö, Pais, T.F., Munari, Francesca, Deborah Penque (2365399), Munari Francesca, Rita Machado de Oliveira, Kuegler, Sebastian, Guerreiro Patrícia, Antas P, Éva M. Szegö (3812242), Vicente Miranda, H., Steegborn Clemens, Tiago Fleming Outeiro (199633), Francelle Laetitia, Szegö, É.M., Szegö, E., Martinho R, Renato Martinho, Antas, Pedro, Outeiro, Tiago Fleming, Francelle, L., Zrinka Marijanovic, Pais, Teresa Faria, Lashuel, Hilal, Tong, Q., Enguita, F.J., Penque Deborah, Munari F, Lázaro, D., Becker, Stefan, Diana F. Lázaro, Raquel Pinho (2847800), Rita Machado de Oliveira (199598), Marijanovic, Z., Miranda, Hugo Vicente, Kügler, Sebastian, Outeiro Tiago Fleming, Pinho, Raquel, Pais TF, Kügler, S., Gerhardt, E., Steegborn, C., Penque, Deborah, Lashuel, H., Sebastian Kügler, Zrinka Marijanovic (218099), Bruno Fauvet (133457), de Oliveira, R., Markus Zweckstetter (133481), Deborah Penque, Becker S, Szegö, Éva M, Moniot, Sébastien, Lashuel, H.A., Francelle, Laetitia, Becker, S., Fauvet, B., Clemens Steegborn, Marijanovic Z, Luis Fonseca-Ornelas, Szegö, Éva M., Zweckstetter Markus, Tiago Fleming Outeiro, Stefan Becker (156472), Luis Fonseca (76017), Stefan Becker, Ellen Gerhardt (185546), de Oliveira, R.M., Pedro Antas (561215), Fauvet B, Antas, P., Zweckstetter, M., Enguita Francisco Javier, Becker Stefan, Fonseca, Luis, Francesca Munari (400905), Lashuel Hilal Ahmed   +169 more
core   +2 more sources

Sirtuin chemical mechanisms [PDF]

Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics, 2010
Sirtuins are ancient proteins widely distributed in all lifeforms of earth. These proteins are universally able to bind NAD(+), and activate it to effect ADP-ribosylation of cellular nucleophiles. The most commonly observed sirtuin reaction is the ADP-ribosylation of acetyllysine, which leads to NAD(+)-dependent deacetylation.
openaire   +2 more sources