Results 51 to 60 of about 6,150 (181)

Innovations in Obesity Treatment: Beyond Adipose Tissue Dysfunction

Obesity Reviews, EarlyView.
Obesity drives chronic inflammation, insulin resistance, type 2 diabetes, and cancer development through adipocyte dysfunction. Addressing this multisystemic disorder requires integrated strategies beyond diet and exercise, such as thermogenesis activation via menthol or capsinoids and appetite control through GLP‐1/GIP agonists and neuromodulation to ...
Jesica Martínez‐Godfrey, Irene Pomares‐Bri, Paula de Juan‐Maciá, Mariló Olivares‐Vicente, Enrique Barrajón‐Catalán, Vicente Micol, Enrique Roche, María Herranz‐López   +7 more
wiley   +1 more source

Research progress on the correlation between islet amyloid peptides and type 2 diabetes mellitus

Open Medicine
Type 2 diabetes mellitus (T2DM) is a chronic metabolic disorder characterized by insulin resistance and β-cell dysfunction. A hallmark of T2DM pathology is the accumulation of toxic amyloid polypeptides in and around pancreatic islet cells, leading to ...
Li GuangZhi, Zhang Dongmei
doaj   +1 more source

Antiglycation of Insulin by Selected Six Bioactive Peanut Sprout Stilbenoids and Demonstration of Methylglyoxal‐Mediated Biphasic Insulin Glycation by O‐Phenylenediamine Derivatization

Food Science &Nutrition, Volume 14, Issue 8, August 2026.
Graphical abstract demonstrates 6 peanut sprout containing stilbenoids exhibiting varied structure‐activity potency in protection of insulin integrity from glycation mediated by methylglyoxal (MG), glucose and fructose. Meanwhile, MG‐mediated biphasic insulin glycation was evidenced in Tricine SDS‐PAGE analysis and supported by O‐phenylenediamine (OPD)
Po‐Chang Chiu, Shu‐Mei Lin, Yu‐Jang Li, Chih‐Yu Lo, Robin Y.‐Y. Chiou   +4 more
wiley   +1 more source

Role of Aromatic Interactions in Amyloid Formation by Islet Amyloid Polypeptide [PDF]

Biochemistry, 2012
Aromatic-aromatic and aromatic-hydrophobic interactions have been proposed to play a role in amyloid formation by a range of polypeptides, including islet amyloid polypeptide (IAPP or amylin). IAPP is responsible for amyloid formation in patients with type 2 diabetes. The polypeptide is 37 residues long and contains three aromatic residues, Phe-15, Phe-
Tu, Ling-Hsien, Raleigh, Daniel P
openaire   +4 more sources

Molecular Mechanisms of Amylin Turnover, Misfolding and Toxicity in the Pancreas

Molecules, 2022
Amyloidosis is a common pathological event in which proteins self-assemble into misfolded soluble and insoluble molecular forms, oligomers and fibrils that are often toxic to cells.
Diti Chatterjee Bhowmick, Zhanar Kudaibergenova, Lydia Burnett, Aleksandar M. Jeremic   +3 more
doaj   +1 more source

Type 2 Diabetes Mellitus: Molecular Pathogenesis and Therapeutic Interventions

MedComm, Volume 7, Issue 8, August 2026.
This graphical summary illustrates the multiorgan therapeutic landscape for Type 2 diabetes mellitus (T2D), integrating molecular pathogenesis with modern treatment strategies. It depicts how current interventions, including SGLT2 inhibitors, GLP‐1 receptor agonists, and insulin secretagogues, target key organs—kidney, pancreas, gastrointestinal tract,
Shinuan Fei, Xiyue Xiong, Lu Zhang, Jian Zhang, Lawrence W. C. Chan, Hong Jiang, Qingqing Xiong, Changtao Hu, Jie Chen, Sijun Yang   +9 more
wiley   +1 more source

Beyond Sequence: Posttranslational Remodeling of Antigens in Autoimmunity

Immunological Reviews, Volume 341, Issue 1, August 2026.
ABSTRACT Autoimmune responses are often attributed to failed tolerance to self‐proteins, yet protein expression alone cannot explain why certain antigens dominate disease, why autoreactivity emerges under stress, or why specific HLA alleles shape risk.
Cynthiya Shrestha, Holly M. Weisfelder, Thanh D. Do   +2 more
wiley   +1 more source

Matrix Metalloproteinase-9 Reduces Islet Amyloid Formation by Degrading Islet Amyloid Polypeptide [PDF]

Journal of Biological Chemistry, 2013
Deposition of islet amyloid polypeptide (IAPP) as amyloid is a pathological hallmark of the islet in type 2 diabetes, which is toxic to β-cells. We previously showed that the enzyme neprilysin reduces islet amyloid deposition and thereby reduces β-cell apoptosis, by inhibiting fibril formation.
Kathryn, Aston-Mourney, Sakeneh, Zraika, Jayalakshmi, Udayasankar, Shoba L, Subramanian, Pattie S, Green, Steven E, Kahn, Rebecca L, Hull   +6 more
openaire   +2 more sources

QBP1 Peptide as a Potential Anti‐Amyloidogenic Therapy for Type 2 Diabetes: An In Vitro Study

Advanced Science, Volume 13, Issue 37, 3 July 2026.
The anti‐amyloidogenic peptide QBP1 effectively halts human islet amyloid polypeptide (hIAPP) aggregation, preventing the formation of toxic β‐structured intermediates. Through a combination of biophysical assays, molecular dynamics, and cell‐based studies, QBP1 is shown to preserve β‐cell viability and metabolic homeostasis, positioning it as a ...
María M. Tejero‐Ojeda, Ada Bernaus Vives, Michał Wojciechowski, Dinh Quoc Huy Pham, Mateusz Chwastyk, Mario Vallejo, Anna Novials, Douglas V. Laurents, Mariano Carrión‐Vázquez   +8 more
wiley   +1 more source

Islet amyloid polypeptide in the islets of Langerhans: friend or foe? [PDF]

Diabetologia, 2000
Islet amyloid polypeptide (IAPP), or amylin, was originally discovered as the constituent peptide in amyloid occurring in human insulinomas and in pancreatic islets in human subjects with Type II (non-insulin-dependent) diabetes mellitus. Its normal expression in beta cells and its co-secretion with insulin in response to nutrient stimuli, suggest a ...
S, Gebre-Medhin, C, Olofsson, H, Mulder
openaire   +2 more sources