PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 20858460-3 2010 In echinocytes, stomatin, sorcin, and synexin showed a similar curvature-dependent lateral distribution as GM1 patches by accumulating to spiculae induced by ionophore A23187 plus calcium. Calcium 180-187 annexin A7 Homo sapiens 38-45 20890130-7 2010 Importantly, we found that ANXA7 was essential for autophagy induction via modulating the intracellular calcium concentration ([Ca2+]i) in HUVEC s. In summary, our work introduced two distinct autophagy enhancers and highlighted the critical role of ANXA7 in endothelial autophagy. Calcium 104-111 annexin A7 Homo sapiens 27-32 21432772-1 2011 Annexin A7 is a member of the family of annexins, which are thought to function in the regulation of calcium homeostasis and the fusion of vesicles. Calcium 101-108 annexin A7 Homo sapiens 0-10 9078249-0 1997 Calcium-dependence of synexin binding may determine aggregation and fusion of lamellar bodies. Calcium 0-7 annexin A7 Homo sapiens 22-29 16785211-4 2006 Stomatin and the cytosolic proteins synexin and sorcin were enriched in spiculae when induced by cytosolic calcium, but not in spiculae induced by amphiphiles. Calcium 107-114 annexin A7 Homo sapiens 36-43 11994295-0 2002 Protein kinase C and guanosine triphosphate combine to potentiate calcium-dependent membrane fusion driven by annexin 7. Calcium 66-73 annexin A7 Homo sapiens 110-119 11994295-1 2002 Exocytotic secretion is promoted by the concerted action of calcium, guanine nucleotide, and protein kinase C. We now show that the calcium-dependent membrane fusion activity of annexin 7 in vitro is further potentiated by the combined addition of guanine nucleotide and protein kinase C. The observed increment involves the simultaneous activation of annexin 7 by these two effectors. Calcium 60-67 annexin A7 Homo sapiens 178-187 11994295-1 2002 Exocytotic secretion is promoted by the concerted action of calcium, guanine nucleotide, and protein kinase C. We now show that the calcium-dependent membrane fusion activity of annexin 7 in vitro is further potentiated by the combined addition of guanine nucleotide and protein kinase C. The observed increment involves the simultaneous activation of annexin 7 by these two effectors. Calcium 132-139 annexin A7 Homo sapiens 178-187 11994295-1 2002 Exocytotic secretion is promoted by the concerted action of calcium, guanine nucleotide, and protein kinase C. We now show that the calcium-dependent membrane fusion activity of annexin 7 in vitro is further potentiated by the combined addition of guanine nucleotide and protein kinase C. The observed increment involves the simultaneous activation of annexin 7 by these two effectors. Calcium 132-139 annexin A7 Homo sapiens 352-361 11994295-6 2002 These results thus lead us to hypothesize that annexin 7 may serve as a common site of action for calcium, guanine nucleotide, and protein kinase C in the exocytotic membrane fusion process in chromaffin cells. Calcium 98-105 annexin A7 Homo sapiens 47-56 20093729-1 2009 The N-terminal regions of annexins A7 (synexin) and A11 consist of an extended series of short sequence repeats rich in tyrosine, proline, and glycine that provide binding sites for other proteins that may be recruited to membranes by the annexins and that may modulate the calcium and membrane binding activities of the annexin core domains. Calcium 274-281 annexin A7 Homo sapiens 39-46 11278415-3 2001 In vitro, annexin 7 is quantitatively phosphorylated by protein kinase C to a mole ratio of 2.0, and phosphorylation is extraordinarily sensitive to variables such as pH, calcium, phospholipid, phorbol ester, and annexin 7 concentration. Calcium 171-178 annexin A7 Homo sapiens 10-19 11278415-4 2001 Phosphorylation of annexin 7 by protein kinase C significantly potentiates the ability of the protein to fuse phospholipid vesicles and lowers the half-maximal concentration of calcium needed for this fusion process. Calcium 177-184 annexin A7 Homo sapiens 19-28 10767422-0 2000 The sorcin-annexin VII calcium-dependent interaction requires the sorcin N-terminal domain. Calcium 23-30 annexin A7 Homo sapiens 11-22 10767422-1 2000 Surface plasmon resonance experiments show that at neutral pH the stability of the complex between sorcin and annexin VII (synexin) increases dramatically between 3 and 6 microM calcium; at the latter cation concentration the K(D) value is 0.63 microM. Calcium 178-185 annexin A7 Homo sapiens 123-130 9268363-0 1997 Calcium-dependent binding of sorcin to the N-terminal domain of synexin (annexin VII). Calcium 0-7 annexin A7 Homo sapiens 64-71 9268363-0 1997 Calcium-dependent binding of sorcin to the N-terminal domain of synexin (annexin VII). Calcium 0-7 annexin A7 Homo sapiens 73-84 9078249-1 1997 Synexin (annexin VII) is a member of the annexin family of calcium and phospholipid binding proteins that promote calcium-dependent aggregation and fusion of lipid vesicles or secretory granules. Calcium 59-66 annexin A7 Homo sapiens 0-7 9078249-1 1997 Synexin (annexin VII) is a member of the annexin family of calcium and phospholipid binding proteins that promote calcium-dependent aggregation and fusion of lipid vesicles or secretory granules. Calcium 59-66 annexin A7 Homo sapiens 9-20 9078249-1 1997 Synexin (annexin VII) is a member of the annexin family of calcium and phospholipid binding proteins that promote calcium-dependent aggregation and fusion of lipid vesicles or secretory granules. Calcium 114-121 annexin A7 Homo sapiens 0-7 9078249-1 1997 Synexin (annexin VII) is a member of the annexin family of calcium and phospholipid binding proteins that promote calcium-dependent aggregation and fusion of lipid vesicles or secretory granules. Calcium 114-121 annexin A7 Homo sapiens 9-20 9078249-3 1997 In this study, we characterized calcium-dependency of synexin binding to lamellar bodies and plasma membranes, since such binding is the initial, and, therefore, may be the rate-limiting step in membrane aggregation and fusion. Calcium 32-39 annexin A7 Homo sapiens 54-61 9078249-4 1997 The binding of biotinylated synexin to lamellar bodies and plasma membranes increased in a calcium-dependent manner reaching a maximum at approx. Calcium 91-98 annexin A7 Homo sapiens 28-35 9078249-9 1997 The calcium kinetics were noticeably similar for synexin binding to lamellar bodies and plasma membranes, aggregation of lamellar bodies, and fusion of lamellar bodies with lipid vesicles. Calcium 4-11 annexin A7 Homo sapiens 49-56 9078249-10 1997 At low calcium concentrations, aggregation of lamellar bodies could be increased with increasing synexin concentration, and arachidonic acid increased all three parameters (binding, aggregation, and fusion) in a similar manner. Calcium 7-14 annexin A7 Homo sapiens 97-104 9078249-11 1997 The effects of calcium and arachidonic acid on these three parameters suggest that synexin binding to lamellar bodies may be a rate-determining step for fusion during surfactant secretion. Calcium 15-22 annexin A7 Homo sapiens 83-90 9078249-12 1997 Furthermore, at near physiological calcium levels, the membrane fusion may be enhanced by elevated concentrations of synexin and polyunsaturated fatty acids. Calcium 35-42 annexin A7 Homo sapiens 117-124 2971392-1 1988 The effect of synexin on the calcium-induced fusion of large unilamellar liposomes was studied by using two assays for the mixing of aqueous contents. Calcium 29-36 annexin A7 Homo sapiens 14-21 1835828-0 1991 Immunoelectron microscopy of the calcium-binding protein synexin in isolated adrenal chromaffin granules and chromaffin cells. Calcium 33-40 annexin A7 Homo sapiens 57-64 2184163-5 1990 The annexins comprise a group of calcium-dependent membrane-aggregating proteins, of which synexin is the prototype, which can initiate contacts between secretory vesicle membranes which will then fuse if the membranes are further perturbed by the addition of exogenous free fatty acids. Calcium 33-40 annexin A7 Homo sapiens 91-98 2542947-3 1989 The derived amino acid sequence of synexin reveals strong homology in the C-terminal domain with a previously identified class of calcium-dependent membrane binding proteins. Calcium 130-137 annexin A7 Homo sapiens 35-42 8855260-2 1996 However, the calcium-dependent membrane fusion reaction driven by synexin (annexin VII) is an in vitro model for this process, which we have now found to be further activated by GTP. Calcium 13-20 annexin A7 Homo sapiens 66-73 8855260-2 1996 However, the calcium-dependent membrane fusion reaction driven by synexin (annexin VII) is an in vitro model for this process, which we have now found to be further activated by GTP. Calcium 13-20 annexin A7 Homo sapiens 75-86 8855260-3 1996 The mechanism of fusion activation depends on the unique ability of synexin to bind and hydrolyze GTP in a calcium-dependent manner, both in vitro and in vivo in streptolysin O-permeabilized chromaffin cells. Calcium 107-114 annexin A7 Homo sapiens 68-75 2971392-7 1988 The effect of calcium-induced synexin polymerization was investigated by preincubation of synexin with calcium prior to addition of liposomes. Calcium 14-21 annexin A7 Homo sapiens 30-37 2971392-7 1988 The effect of calcium-induced synexin polymerization was investigated by preincubation of synexin with calcium prior to addition of liposomes. Calcium 14-21 annexin A7 Homo sapiens 90-97 2971392-7 1988 The effect of calcium-induced synexin polymerization was investigated by preincubation of synexin with calcium prior to addition of liposomes. Calcium 103-110 annexin A7 Homo sapiens 30-37 2971392-7 1988 The effect of calcium-induced synexin polymerization was investigated by preincubation of synexin with calcium prior to addition of liposomes. Calcium 103-110 annexin A7 Homo sapiens 90-97 2954851-0 1987 Membrane capacity measurements suggest a calcium-dependent insertion of synexin into phosphatidylserine bilayers. Calcium 41-48 annexin A7 Homo sapiens 72-79 2954851-1 1987 The mechanism by which synexin mediates calcium-dependent aggregation of medullary cell chromaffin granules and fusion of granule ghosts involves specific interactions with the lipid component of the membrane. Calcium 40-47 annexin A7 Homo sapiens 23-30 2953727-9 1987 These results suggest that PMN contain a protein similar to, or identical with, synexin that may be involved in calcium-dependent fusion of intracellular membranes. Calcium 112-119 annexin A7 Homo sapiens 80-87 2954851-5 1987 However, addition of calcium (0.1-2.5 mM) in the presence of synexin in the external solution caused a marked increase in the size and time constant of decay of the displacement current. Calcium 21-28 annexin A7 Homo sapiens 61-68 2954851-9 1987 These properties of the extra charge movement support our view that in the presence of calcium the cytosolic protein synexin penetrates into the bilayer. Calcium 87-94 annexin A7 Homo sapiens 117-124 6218998-0 1982 Synhibin: a new calcium-dependent membrane-binding protein that inhibits synexin-induced chromaffin granule aggregation and fusion. Calcium 16-23 annexin A7 Homo sapiens 73-80 6224488-0 1983 Calcium dependence of the binding of synexin to isolated chromaffin granules. Calcium 0-7 annexin A7 Homo sapiens 37-44 6224488-1 1983 The calcium dependence of the binding of synexin to isolated chromaffin granules has been investigated. Calcium 4-11 annexin A7 Homo sapiens 41-48 6220716-0 1983 Identification of a second synexin-like adrenal medullary and liver protein that enhances calcium-induced membrane aggregation. Calcium 90-97 annexin A7 Homo sapiens 27-34 3155695-0 1985 Synexin binds in a calcium-dependent fashion to oriented chromaffin cell plasma membranes. Calcium 19-26 annexin A7 Homo sapiens 0-7 3155695-1 1985 Oriented plasma membrane fragments from chromaffin cells, isolated on polylysine-coated polyacrylamide beads, bind synexin in a calcium dependent manner. Calcium 128-135 annexin A7 Homo sapiens 115-122 3155695-3 1985 Synexin binding to plasma membrane coated beads showed a specific requirement for calcium (K1 2 = 200 microM) and was insensitive to other divalent cations such as magnesium, strontium and barium. Calcium 82-89 annexin A7 Homo sapiens 0-7 762079-0 1979 Self-association of synexin in the presence of calcium. Calcium 47-54 annexin A7 Homo sapiens 20-27 6211522-0 1982 Purification and mode of action of synexin: a protein enhancing calcium-induced membrane aggregation. Calcium 64-71 annexin A7 Homo sapiens 35-42 6452452-2 1981 Synexin, a soluble adrenal medullary and liver protein which causes calcium-dependent aggregation of isolated chromaffin granules, was isolated and purified according to published procedures. Calcium 68-75 annexin A7 Homo sapiens 0-7 632306-0 1978 Identification and purification of an adrenal medullary protein (synexin) that causes calcium-dependent aggregation of isolated chromaffin granules. Calcium 86-93 annexin A7 Homo sapiens 65-72 31975592-7 2020 We then demonstrated that annexin A7 (ANXA7), a calcium-dependent phospholipid-binding protein, can translocate to impaired mitochondria upon CCCP treatment, where it played a pivotal part in the process of Parkin-dependent mitophagy via interacting with BASP1. Calcium 48-55 annexin A7 Homo sapiens 26-36 31975592-7 2020 We then demonstrated that annexin A7 (ANXA7), a calcium-dependent phospholipid-binding protein, can translocate to impaired mitochondria upon CCCP treatment, where it played a pivotal part in the process of Parkin-dependent mitophagy via interacting with BASP1. Calcium 48-55 annexin A7 Homo sapiens 38-43 30321230-1 2018 BACKGROUND: Annexin A7 (ANXA7) is a member of the multifunctional calcium or phospholipid-binding annexin gene family. Calcium 66-73 annexin A7 Homo sapiens 12-22 30321230-1 2018 BACKGROUND: Annexin A7 (ANXA7) is a member of the multifunctional calcium or phospholipid-binding annexin gene family. Calcium 66-73 annexin A7 Homo sapiens 24-29 27807828-4 2017 ANXA7-GTPase contains a calcium binding domain that classifies it as a member of the annexin family. Calcium 24-31 annexin A7 Homo sapiens 0-5 27807828-8 2017 This review focuses on the recent progress in understanding the tumor suppressor functions of ANXA7-GTPase emphasizing the role of this gene in Ca2+ metabolism, and exploring opportunities for function as an example of a calcium binding GTPase acting as a tumor suppressor and opportunities for ANXA7-GTPase gene cancer therapy. Calcium 221-228 annexin A7 Homo sapiens 94-99