WebThe antiphospholipid syndrome is an autoimmune disorder of hypercoagulability characterized by the presence of autoantibodies to various phospholipids or phospholipid … WebSep 8, 2024 · A plasmid platform according to the present invention comprises a nucleic acid sequence encoding a modified protein from which an intracellular domain, an extracellular domain, or a combination thereof of lysosome-associated membrane glycoprotein 2B (LAMP-2B) has been removed, and is based on the discovery that …
Cellular and Molecular Mechanisms of Anti-Phospholipid Syndrome
WebDec 23, 2024 · In contrast, the C-terminal domain contains the primary protein-binding site with SNX9 and N-WASP (Hua et al., 2024a) (Figure 1A). It remains unknown which domain acts in the binding to ANXA6. ... ANXA6 is a Calcium/Calmodulin-dependent phospholipid-binding protein and is implicated in various cellular processes (Grewal et al., 2024). WebThe P ho x homology ( PX) domain is a phospholipid-binding domain consisting of ~120 amino acids. The PX domain is found in more than 250 proteins, including the p40 phox … small bursts
A C2-domain phospholipid-binding protein MdCAIP1 positively
WebMar 1, 2013 · Phosphatidylcholine (PtdCho) is the major glycerophospholipid (GPL) in the brain where it is synthesized by the CDP-choline pathway. The rate-limiting step in this pathway is catalyzed by two isoforms of CTP:phosphocholine cytidylyltransferase: CTα and CTβ2, of which the latter is the dominant form in brain [2]. WebApr 2, 2024 · Phospholipid Binding of MdCAIP1 in a Ca 2+ -dependent manner. a Diagram of the predicted structure of the MdCAIP1 protein. The locations of the N and C termini and the eight β-strands in MdCAIP1 are indicated. b Amino acid sequences comparison of C2-domain in MdCAIP1 and representative C2-domain proteins in animal. Webinvolved in phospholipid synthesis in the yeast Saccha-romyces cerevisiae. The phosphorylation of Opi1p by protein kinase A (cAMP-dependent protein kinase) was examined in this work. Using a maltose-binding protein-Opi1p fusion protein as a substrate, protein kinase A activity was time- and dose-dependent and dependent small burst blood vessel in eye