PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
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	
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	120-138	annexin A2	Homo sapiens	38-48	
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	
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	103-105	annexin A2	Homo sapiens	35-45	
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	
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	
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	
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	
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