Results 231 to 239 of about 40,878 (239)

TCA cycle off, ATF4 on for metabolic homeostasis

Trends in Biochemical Sciences, 2022
Tricarboxylic acid (TCA) cycle is a major hub for catabolic and anabolic reactions, yet cellular metabolic adaptations following its inhibition are largely unknown. Using multi-tiered omics approaches, Ryan et al. have shown convergent activation of the integrated stress response (ISR) through ATF4-mediated rewiring of cellular amino acid and redox ...
Durga Mahor, Rishikesh Pandey, Vinay Bulusu   +2 more
openaire   +2 more sources

miR-214 targets ATF4 to inhibit bone formation

Nature Medicine, 2012
Emerging evidence indicates that microRNAs (miRNAs) have important roles in regulating osteogenic differentiation and bone formation. Thus far, no study has established the pathophysiological role for miRNAs identified in human osteoporotic bone specimens.
Xiaogang, Wang, Baosheng, Guo, Qi, Li, Jiang, Peng, Zhijun, Yang, Aiyuan, Wang, Dong, Li, Zhibo, Hou, Ke, Lv, Guanghan, Kan, Hongqing, Cao, Heng, Wu, Jinping, Song, Xiaohua, Pan, Qiao, Sun, Shukuan, Ling, Yuheng, Li, Mu, Zhu, Pengfei, Zhang, Songlin, Peng, Xiaoqing, Xie, Tao, Tang, An, Hong, Zhaoxiang, Bian, Yanqiang, Bai, Aiping, Lu, Yinghui, Li, Fuchu, He, Ge, Zhang, Yingxian, Li   +29 more
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ATF4 in cellular stress, ferroptosis, and cancer

Archives of Toxicology
Activating transcription factor 4 (ATF4), a member of the ATF/cAMP response element-binding (CREB) family, plays a critical role as a stress-induced transcription factor. It orchestrates cellular responses, particularly in the management of endoplasmic reticulum stress, amino acid deprivation, and oxidative challenges.
Hu Tang, Rui Kang, Jiao Liu, Daolin Tang
openaire   +2 more sources

ATF4 regulates γ-secretase activity during amino acid imbalance

Biochemical and Biophysical Research Communications, 2007
Accumulation of amyloid-beta (Abeta), which is generated from amyloid precursor protein by gamma-secretase, in cerebral cortex is common and critical incident in Alzheimer disease. Specifically, presenilin is an essential for gamma-secretase activity. However, the regulation of presenilin expression, affecting gamma-secretase activity, remains obscure.
Teruhiko, Mitsuda, Yoshika, Hayakawa, Masanori, Itoh, Kazunori, Ohta, Toshiyuki, Nakagawa   +4 more
openaire   +2 more sources

Phosphorylation-dependent structure of ATF4 peptides derived from a human ATF4 protein, a member of the family of transcription factors

Peptides, 2007
ATF4 plays a crucial role in the cellular response to stress and the F-box protein beta-TrCP, the receptor component of the SCF E3 ubiquitin ligase responsible for ATF4 degradation by the proteasome, binds to ATF4, and controls its stability. Association between the two proteins depends on ATF4 phosphorylation of serine residues 219 and 224 present in ...
Julien, Pons, Nathalie, Evrard-Todeschi, Gildas, Bertho, Josyane, Gharbi-Benarous, Richard, Benarous, Jean-Pierre, Girault   +5 more
openaire   +2 more sources

ATF4: a Novel Potential Therapeutic Target for Alzheimer’s Disease

Molecular Neurobiology, 2014
Activating transcription factor 4 (ATF4) belongs to the activating transcription factor family and its expression is increased upon the stimulation of a diverse array of microenvironmental stresses. ATF4 plays a major role in the development, metabolism, and memory formation.
Na, Wei, Ling-Qiang, Zhu, Dan, Liu
openaire   +2 more sources

Atf4

AfCS-Nature Molecule Pages, 2011
Kurosh Ameri, Adrian Harris, Dean Singleton   +2 more
openaire   +1 more source

ATF4, Hypoxia and Treatment Resistance in Cancer

2019
Oxygen deprivation (hypoxia) is a common feature of tumors that is associated with treatment resistance and poor patient survival. Hypoxia perturbs the oxidative environment within the endoplasmic reticulum (EnR), limiting protein folding capacity.
Dean C. Singleton, Adrian L. Harris
openaire   +1 more source

ATF4: a novel regulator of cell growth

Blood, 2002
Activating transcription factor-4 (ATF4) is a member of the ATF/CREB subfamily of basic region-leucine zipper proteins. ATF4 forms homodimers or heterodimers by interacting with itself or other proteins through its leucine zipper motif. Potential partners of ATF4 include members of the AP-1 and C/
openaire   +1 more source