PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 33861586-3 2021 Annexins A1 and A2 (ANXA1 and ANXA2, respectively) are structurally similar and bind to negatively charged phosphatidylserine (PS) to induce membrane cross-linking and to promote fusion, which are both essential processes that occur during membrane repair. Phosphatidylserines 107-125 annexin A2 Homo sapiens 30-35 33861586-3 2021 Annexins A1 and A2 (ANXA1 and ANXA2, respectively) are structurally similar and bind to negatively charged phosphatidylserine (PS) to induce membrane cross-linking and to promote fusion, which are both essential processes that occur during membrane repair. Phosphatidylserines 127-129 annexin A2 Homo sapiens 30-35 12627981-4 2003 In the experimental setup chosen, the annexin A2t binding is strictly Ca2+-dependent and only affected by the amount of phosphatidylserine (PS) in the membrane and the Ca2+ concentration in solution. Phosphatidylserines 120-138 annexin A2 Homo sapiens 38-48 25418092-4 2014 Here, we performed a quantitative analysis of the binding of AnxA2 to solid supported membranes containing the annexin binding lipids phosphatidylinositol-4,5-bisphosphate and phosphatidylserine in different compositions. Phosphatidylserines 176-194 annexin A2 Homo sapiens 61-66 25418092-9 2014 Together our results reveal for the first time, to our knowledge, that AnxA2 and its derivatives bind cooperatively to membranes containing cholesterol, phosphatidylserine, and/or phosphatidylinositol-4,5-bisphosphate, thus providing a mechanistic model for the lipid clustering activity of AnxA2. Phosphatidylserines 153-171 annexin A2 Homo sapiens 71-76 15545357-3 2004 Based on the recent identification of human cell membrane phosphatidylserine (PS) in the outer coat of HIV-1, we define a novel role for annexin II, a PS-binding moiety, as a cellular cofactor supporting macrophage HIV-1 infection. Phosphatidylserines 78-80 annexin A2 Homo sapiens 137-147 12627981-4 2003 In the experimental setup chosen, the annexin A2t binding is strictly Ca2+-dependent and only affected by the amount of phosphatidylserine (PS) in the membrane and the Ca2+ concentration in solution. Phosphatidylserines 140-142 annexin A2 Homo sapiens 38-48 34699769-2 2022 However, the principal molecular partners of AnxA2 are negatively charged phospholipids such as phosphatidylserine and phosphatidyl-inositol-(4,5)-phosphate. Phosphatidylserines 96-114 annexin A2 Homo sapiens 45-50 11342144-8 2001 Consistent with this observation, liposomes containing phosphatidylserine and cholesterol were aggregated by the tetrameric form of annexin 2 at submicromolar Ca(2+) concentrations. Phosphatidylserines 55-73 annexin A2 Homo sapiens 132-141 10956650-4 2000 In this study, we demonstrate that annexin II, V, or VI mediate Ca(2+) influx into phosphatidylserine (PS)-enriched liposomes, liposomes containing lipids extracted from authentic MV, and intact authentic MV. Phosphatidylserines 83-101 annexin A2 Homo sapiens 35-45 10956650-4 2000 In this study, we demonstrate that annexin II, V, or VI mediate Ca(2+) influx into phosphatidylserine (PS)-enriched liposomes, liposomes containing lipids extracted from authentic MV, and intact authentic MV. Phosphatidylserines 103-105 annexin A2 Homo sapiens 35-45 2138016-5 1990 Both calpactin I heavy chain and lipocortin I promoted aggregation of phosphatidylserine- or phosphatidylinositol-containing vesicles in the presence of less than 10 microM-Ca2+. Phosphatidylserines 70-88 annexin A2 Homo sapiens 5-28