PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 10224161-9 1999 When mixed films were formed by successive spreading of DPPC/SP-A/cholesterol, rat SP-A, SP-Ahyp, or SP-ADeltaG8-P80 blocked the interaction of cholesterol with DPPC; SP-Ahyp,E195Q,R197D could not impede the interaction; SP-Ahyp,C6S or SP-Ahyp,DeltaN1-A7 only partially blocked the interaction, and cholesterol appeared to stabilize SP-Ahyp,C6S-DPPC association. 1,2-Dipalmitoylphosphatidylcholine 161-165 surfactant protein A1 Rattus norvegicus 83-87 10828943-3 2000 Recombinant rat SP-A, containing a deletion of the collagen-like domain, was incubated with dipalmitoylphosphatidylcholine:egg phosphatidylcholine (1:1, wt/wt) lipid monolayers in the presence of calcium, negatively stained, and examined by transmission electron microscopy. 1,2-Dipalmitoylphosphatidylcholine 92-122 surfactant protein A1 Rattus norvegicus 16-20 10653651-2 2000 SP-A binds dipalmitoylphosphatidylcholine (DPPC) and galactosylceramide (GalCer), induces liposome aggregation, and regulates the uptake and secretion of surfactant lipids by alveolar type II cells in vitro. 1,2-Dipalmitoylphosphatidylcholine 11-41 surfactant protein A1 Rattus norvegicus 0-4 10653651-2 2000 SP-A binds dipalmitoylphosphatidylcholine (DPPC) and galactosylceramide (GalCer), induces liposome aggregation, and regulates the uptake and secretion of surfactant lipids by alveolar type II cells in vitro. 1,2-Dipalmitoylphosphatidylcholine 43-47 surfactant protein A1 Rattus norvegicus 0-4 10224161-0 1999 Interactions of pulmonary surfactant protein SP-A with monolayers of dipalmitoylphosphatidylcholine and cholesterol: roles of SP-A domains. 1,2-Dipalmitoylphosphatidylcholine 69-99 surfactant protein A1 Rattus norvegicus 45-49 10224161-1 1999 Pulmonary surfactant protein A (SP-A) is an oligomeric glycoprotein that binds dipalmitoylphosphatidylcholine (DPPC). 1,2-Dipalmitoylphosphatidylcholine 79-109 surfactant protein A1 Rattus norvegicus 32-36 10224161-1 1999 Pulmonary surfactant protein A (SP-A) is an oligomeric glycoprotein that binds dipalmitoylphosphatidylcholine (DPPC). 1,2-Dipalmitoylphosphatidylcholine 111-115 surfactant protein A1 Rattus norvegicus 32-36 10224161-2 1999 Interactions of rat SP-A and recombinant SP-As with pure and binary monolayers of DPPC and cholesterol were studied using a rhomboid surface balance at 37 degrees C. A marked inflection at equilibrium surface tension (23 mN/m) in surface tension-area isotherm of a pure DPPC film was abolished by rat SP-A. 1,2-Dipalmitoylphosphatidylcholine 82-86 surfactant protein A1 Rattus norvegicus 41-45 10224161-4 1999 Both rat SP-A and SP-Ahyp decreased surface area reduction required for pure DPPC films to reach near zero surface tension from 30 to 25%. 1,2-Dipalmitoylphosphatidylcholine 77-81 surfactant protein A1 Rattus norvegicus 9-13 10224161-4 1999 Both rat SP-A and SP-Ahyp decreased surface area reduction required for pure DPPC films to reach near zero surface tension from 30 to 25%. 1,2-Dipalmitoylphosphatidylcholine 77-81 surfactant protein A1 Rattus norvegicus 18-25 10224161-5 1999 SP-Ahyp, E195Q,R197D, mutated in carbohydrate recognition domain (CRD) known to be essential for SP-A-vesicle interactions, conveyed a detrimental effect on DPPC surface activity. 1,2-Dipalmitoylphosphatidylcholine 157-161 surfactant protein A1 Rattus norvegicus 0-7 10224161-5 1999 SP-Ahyp, E195Q,R197D, mutated in carbohydrate recognition domain (CRD) known to be essential for SP-A-vesicle interactions, conveyed a detrimental effect on DPPC surface activity. 1,2-Dipalmitoylphosphatidylcholine 157-161 surfactant protein A1 Rattus norvegicus 0-4 10224161-9 1999 When mixed films were formed by successive spreading of DPPC/SP-A/cholesterol, rat SP-A, SP-Ahyp, or SP-ADeltaG8-P80 blocked the interaction of cholesterol with DPPC; SP-Ahyp,E195Q,R197D could not impede the interaction; SP-Ahyp,C6S or SP-Ahyp,DeltaN1-A7 only partially blocked the interaction, and cholesterol appeared to stabilize SP-Ahyp,C6S-DPPC association. 1,2-Dipalmitoylphosphatidylcholine 56-60 surfactant protein A1 Rattus norvegicus 83-87 10224161-9 1999 When mixed films were formed by successive spreading of DPPC/SP-A/cholesterol, rat SP-A, SP-Ahyp, or SP-ADeltaG8-P80 blocked the interaction of cholesterol with DPPC; SP-Ahyp,E195Q,R197D could not impede the interaction; SP-Ahyp,C6S or SP-Ahyp,DeltaN1-A7 only partially blocked the interaction, and cholesterol appeared to stabilize SP-Ahyp,C6S-DPPC association. 1,2-Dipalmitoylphosphatidylcholine 161-165 surfactant protein A1 Rattus norvegicus 89-96 9436177-10 1998 On the other hand, SP-A significantly enhanced binding of dipalmitoyl phosphatidylcholine to plasma membranes (two- to threefold) and uptake into lamellar bodies (threefold) of 19-day fetal cells. 1,2-Dipalmitoylphosphatidylcholine 58-89 surfactant protein A1 Rattus norvegicus 19-23 9748660-1 1998 Surfactant protein A (SP-A) binds to dipalmitoylphosphatidylcholine (DPPC) and induces phospholipid vesicle aggregation. 1,2-Dipalmitoylphosphatidylcholine 37-67 surfactant protein A1 Rattus norvegicus 0-20 9748660-1 1998 Surfactant protein A (SP-A) binds to dipalmitoylphosphatidylcholine (DPPC) and induces phospholipid vesicle aggregation. 1,2-Dipalmitoylphosphatidylcholine 37-67 surfactant protein A1 Rattus norvegicus 22-26 9748660-1 1998 Surfactant protein A (SP-A) binds to dipalmitoylphosphatidylcholine (DPPC) and induces phospholipid vesicle aggregation. 1,2-Dipalmitoylphosphatidylcholine 69-73 surfactant protein A1 Rattus norvegicus 0-20 9748660-1 1998 Surfactant protein A (SP-A) binds to dipalmitoylphosphatidylcholine (DPPC) and induces phospholipid vesicle aggregation. 1,2-Dipalmitoylphosphatidylcholine 69-73 surfactant protein A1 Rattus norvegicus 22-26 9468543-2 1998 SP-A binds to dipalmitoylphosphatidylcholine and galactosylceramide, and it regulates the uptake and secretion of surfactant lipids by alveolar type II cells. 1,2-Dipalmitoylphosphatidylcholine 14-44 surfactant protein A1 Rattus norvegicus 0-4 8843792-4 1996 With 5 micrograms/ml SP-A, type II cells actively take up liposomes (244 pmol dipalmitoylphosphatidylcholine.h-1.10(6) cells-1). 1,2-Dipalmitoylphosphatidylcholine 78-108 surfactant protein A1 Rattus norvegicus 21-25 7961971-3 1994 SP-A specifically binds to dipalmitoylphosphatidylcholine, the major lipid component of surfactant, and can regulate the secretion and recycling of this lipid by alveolar type II cells. 1,2-Dipalmitoylphosphatidylcholine 27-57 surfactant protein A1 Rattus norvegicus 0-4 9188718-1 1997 Pulmonary surfactant protein A (SP-A) is a C-type lectin that regulates the uptake and secretion of surfactant lipids by alveolar type II cells and binds dipalmitoylphosphatidylcholine (DPPC) and galactosylceramide (GalCer). 1,2-Dipalmitoylphosphatidylcholine 154-184 surfactant protein A1 Rattus norvegicus 10-30 9188718-1 1997 Pulmonary surfactant protein A (SP-A) is a C-type lectin that regulates the uptake and secretion of surfactant lipids by alveolar type II cells and binds dipalmitoylphosphatidylcholine (DPPC) and galactosylceramide (GalCer). 1,2-Dipalmitoylphosphatidylcholine 154-184 surfactant protein A1 Rattus norvegicus 32-36 9188718-1 1997 Pulmonary surfactant protein A (SP-A) is a C-type lectin that regulates the uptake and secretion of surfactant lipids by alveolar type II cells and binds dipalmitoylphosphatidylcholine (DPPC) and galactosylceramide (GalCer). 1,2-Dipalmitoylphosphatidylcholine 186-190 surfactant protein A1 Rattus norvegicus 10-30 9188718-1 1997 Pulmonary surfactant protein A (SP-A) is a C-type lectin that regulates the uptake and secretion of surfactant lipids by alveolar type II cells and binds dipalmitoylphosphatidylcholine (DPPC) and galactosylceramide (GalCer). 1,2-Dipalmitoylphosphatidylcholine 186-190 surfactant protein A1 Rattus norvegicus 32-36 7943260-7 1994 Binding assay showed binding of 125I-labeled SP-A to DPPC but not to POPC, indicating that removal of substrate was not the mechanism for inhibition of the enzyme by SP-A. 1,2-Dipalmitoylphosphatidylcholine 53-57 surfactant protein A1 Rattus norvegicus 45-49 7943260-10 1994 The presence of SP-A in liposomes stimulated the uptake of DPPC by isolated granular pneumocytes in primary culture but significantly inhibited its degradation. 1,2-Dipalmitoylphosphatidylcholine 59-63 surfactant protein A1 Rattus norvegicus 16-20