Results 131 to 140 of about 16,783,083 (225)

Identification of activating transcription factor 4 (ATF4) as an Nrf2-interacting protein. Implication for heme oxygenase-1 gene regulation.

open access: yesThe Journal of biological chemistry, 2001
Nrf2 regulates expression of genes encoding enzymes with antioxidant (e.g. heme oxygenase-1 (HO-1)) or xenobiotic detoxification (e.g. NAD(P)H:quinone oxidoreductase, glutathione S-transferase) functions via the stress- or antioxidant-response elements (StRE/ARE).
C H, He   +6 more
openaire   +1 more source

Resolving Endoplasmic Reticulum‐Protein Misfolding Restores Corticosteroid Sensitivity in Experimental Models of Severe Asthma

open access: yesAllergy, EarlyView.
This study investigates the role of ER stress in steroid resistance in severe asthma. Results from advanced 3D models of human bronchial epithelial cells, steroid‐resistant severe asthma mouse models, and human severe asthma sputum samples show that treatment with ICS in combination with the ER stress inhibitor 4‐PBA significantly enhances steroid ...
Prabuddha S. Pathinayake   +8 more
wiley   +1 more source

Thbs1 regulates skeletal muscle mass in a TGFβ-Smad2/3-ATF4-dependent manner

open access: yesCell Reports
Summary: Loss of muscle mass is a feature of chronic illness and aging. Here, we report that skeletal muscle-specific thrombospondin-1 transgenic mice (Thbs1 Tg) have profound muscle atrophy with age-dependent decreases in exercise capacity and premature
Davy Vanhoutte   +10 more
doaj   +1 more source

Histone deacetylase inhibitors as venetoclax‐sensitising partners in acute myeloid leukaemia: Mechanisms, pharmacology and translational perspectives

open access: yesBritish Journal of Pharmacology, EarlyView.
Abstract Venetoclax combined with hypomethylating agents has improved treatment for older or unfit patients with acute myeloid leukaemia (AML), but resistance and relapse remain common. This review analyses the rationale for combining venetoclax with inhibitors of histone deacetylase (HDAC).
Jaebok Lee, Marc Diederich
wiley   +1 more source

YBX1 Promotes Malignant Progression of HNSCC via Stabilizing NSUN2‐m5C Modified ATF4 mRNA

open access: yesCancer Science, EarlyView.
The diagram depicts the core axis and the key finding: “Targeting YBX1/NSUN2 abrogates HNSCC progression”. Within left‐sided HNSCC cells, NSUN2 mediates m5C methylation on the CDS of ATF4 mRNA; YBX1 then specifically recognizes and binds this modified site, augmenting ATF4 mRNA stability, which ultimately promotes cancer cell proliferation, migration ...
Yanwei Li   +3 more
wiley   +1 more source

The p300/CBP-associated factor (PCAF) is a cofactor of ATF4 for amino acid-regulated transcription of CHOP

open access: yes, 2007
When an essential amino acid is limited, a signaling cascade is triggered that leads to increased translation of the 'master regulator', activating transcription factor 4 (ATF4), and resulting in the induction of specific target genes. Binding of ATF4 to
Parry, Laurent   +11 more
core   +1 more source

The Pathological Roles of Cationic Amino Acid Transporters (CATs) in Cancer

open access: yesCancer Science, EarlyView.
CAT family transporters (SLC7A1–SLC7A4) coordinate arginine allocation within the tumor microenvironment, thereby regulating cancer metabolism, mTORC1 signaling, immune responses, and metastatic progression. Emerging evidence supports context‐dependent roles for SLC7A1–SLC7A3, whereas the physiological and pathological functions of SLC7A4 remain poorly
Thant Thant Myo Oo, Yasuhiro Saito
wiley   +1 more source

Targeting NAT10 inhibits osteosarcoma progression via ATF4/ASNS-mediated asparagine biosynthesis

open access: yesCell Reports Medicine
Summary: Despite advances in treatment, the prognosis of patients with osteosarcoma remains unsatisfactory, and searching for potential targets is imperative.
Yutong Zou   +11 more
doaj   +1 more source

ER proteostasis meets mitochondrial function: contact sites as hubs of communication and therapeutic targets

open access: yesThe FEBS Journal, EarlyView.
Proteostasis ensures proper protein folding, modification, and degradation, while its impairment triggers ER stress. Chronic ER stress and maladaptive UPR via the CHOP–ERO1 axis remodel ERMCs, altering calcium signaling and mitochondrial metabolism.
Giorgia Maria Renna   +5 more
wiley   +1 more source

Proteostasis of organelles in aging and disease

open access: yesThe FEBS Journal, EarlyView.
Cells rely on regulated proteostasis mechanisms to keep their internal compartments functioning properly. When these mechanisms fail, damaged proteins accumulate, disrupting organelles, such as the nucleus, mitochondria, endoplasmic reticulum, Golgi, and lysosomes, as well as membraneless organelles, such as stress granules, processing bodies, the ...
Yara Nabawi   +5 more
wiley   +1 more source

Home - About - Disclaimer - Privacy