التفاصيل البيبلوغرافية
العنوان:
Serum amyloid A sequesters diverse phospholipids and their hydrolytic products, hampering fibril formation and proteolysis in a lipid-dependent manner
المؤلفون:
Olga Gursky , Christian Haupt , Shobini Jayaraman , Marcus Fändrich , Donald L. Gantz
المصدر:
Chemical communications (Cambridge, England) . 54(28)
سنة النشر:
2018
مصطلحات موضوعية:
0301 basic medicine , Dependent manner , Proteolysis , animal diseases , Catalysis , Article , 03 medical and health sciences , Hydrolysis , Immune system , Phospholipase A2 , hemic and lymphatic diseases , Materials Chemistry , medicine , Serum amyloid A , Phospholipids , Serum Amyloid A Protein , medicine.diagnostic_test , biology , Chemistry , Amyloidosis , Metals and Alloys , Fibrillogenesis , Esters , General Chemistry , medicine.disease , Surfaces, Coatings and Films , Electronic, Optical and Magnetic Materials , stomatognathic diseases , 030104 developmental biology , Biochemistry , Ceramics and Composites , biology.protein , lipids (amino acids, peptides, and proteins)
الوصف:
Serum amyloid A action in immune response and deposition in inflammation-linked amyloidosis involve SAA-lipid interactions. We show that SAA sequesters neutral and anionic phospholipids and their hydrolytic products to form nanoparticles, suggesting a synergy with phospholipase A(2). The lipid charge and shape affect SAA protection from proteolysis, aggregation and fibrillogenesis.
تدمد:
1364-548X
الوصول الحر:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::fe862c479289f11eccf01453178ac30fTest https://pubmed.ncbi.nlm.nih.gov/29565436Test
حقوق:
OPEN
رقم الانضمام:
edsair.doi.dedup.....fe862c479289f11eccf01453178ac30f
قاعدة البيانات:
OpenAIRE
