Results 61 to 70 of about 10,823 (192)
Epigenetic Regulation in the Pathogenesis of Renal Inflammation: Insights and Therapeutic Potentials
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 +5 more
wiley +1 more source
Adss1–HDAC3 Interaction: A Novel Mechanism for Epigenetic Regulation of Metabolism in Adipose Tissue
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 +3 more
wiley +1 more source
Defining the Human Deubiquitinating Enzyme Interaction Landscape [PDF]
Deubiquitinating enzymes (Dubs) function to remove covalently attached ubiquitin from proteins, thereby controlling substrate activity and/or abundance. For most Dubs, their functions, targets, and regulation are poorly understood. To systematically investigate Dub function, we initiated a global proteomic analysis of Dubs and their associated protein ...
Sowa, Mathew E. +3 more
openaire +2 more sources
N6‐Methyladenosine (m6A) in Liver Disease: Pathogenic Mechanisms and Therapeutic Potential
ABSTRACT Accumulating evidence highlights the critical role of epigenetic modifications, particularly N6‐methyladenosine (m6A), in liver disease. As the most abundant RNA modification in eukaryotic cells, m6A is dynamically regulated by multicomponent m6A methyltransferases (e.g., METTL3 and METTL14), demethylases (FTO and ALKBH5), and m6A‐binding ...
Yingfen Chen +6 more
wiley +1 more source
Role of Deubiquitinating Enzymes in DNA Repair [PDF]
Both proteolytic and nonproteolytic functions of ubiquitination are essential regulatory mechanisms for promoting DNA repair and the DNA damage response in mammalian cells. Deubiquitinating enzymes (DUBs) have emerged as key players in the maintenance of genome stability. In this minireview, we discuss the recent findings on human DUBs that participate
Kee, Younghoon, Huang, Tony T.
openaire +3 more sources
ABSTRACT Sepsis is typified by organ failure due to an unchecked host reaction to infection. This study aims to explore the mechanism of ubiquitin‐specific peptidase 7 (USP7) in sepsis with the involvement of intercellular adhesion molecule‐1 (ICAM‐1).
Hui Xu +4 more
wiley +1 more source
Polyubiquitin Binding and Disassembly By Deubiquitinating Enzymes [PDF]
Ubiquitin (Ub) is a highly conserved protein of 76 amino acids that is covalently linked to target proteins altering their localization, function, or stability 1-3. Proteins can be modified with a large number of different isoforms of ubiquitin and these different ubiquitins are thought to signal different outcomes.
Francisca E, Reyes-Turcu +1 more
openaire +2 more sources
The Role and Mechanism of Deubiquitinase USP7 in Tumor-Associated Inflammation
Deubiquitinating enzymes are a class of proteases that remove ubiquitin tags from proteins, thereby controlling protein stability and function. Tumor inflammation arises from interactions between tumor cells and their microenvironment, which trigger an ...
Luhong Wang +3 more
doaj +1 more source
ABSTRACT Osteoarthritis (OA) is a common degenerative joint disease characterized by chondrocyte dysfunction. In this study, we explored the function and mechanism of ubiquitin‐specific protease 7 (USP7) in chondrocyte ferroptosis in OA. The USP7, TRPV1, collagen II, and GPX4 levels in knee joint tissue were detected using immunohistochemistry ...
Jun Li, Ding Chen, Wei‐Ye Zhong
wiley +1 more source
Abstract Background Spinocerebellar ataxia type 3 (SCA3) is a polyglutamine (polyQ) neurogenerative disorder that results from CAG trinucleotide repeat expansions in the ATXN3 gene, leading to toxic protein aggregate formation and cellular pathway dysfunction.
Tiago Moreira‐Gomes +9 more
wiley +1 more source

