PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 25818314-1 2015 CD59 encodes a 77 amino acid glycosylphosphatidylinositol (GPI)-anchored cell surface glycoprotein that inhibits the final step of membrane attack complex (MAC) formation. Glycosylphosphatidylinositols 59-62 CD59 molecule (CD59 blood group) Homo sapiens 0-4 28330937-5 2017 Single fluorescent molecule tracking in the live-cell PM revealed that they indirectly interact with each other in cholesterol- and sphingosine backbone-dependent manners, and that, for ~10-50 ms, they undergo transient colocalization-codiffusion with a glycosylphosphatidylinositol (GPI)-anchored protein, CD59 (in monomers, transient-dimer rafts, and clusters), in CD59-oligomer size-, cholesterol-, and GPI anchoring-dependent manners. Glycosylphosphatidylinositols 254-282 CD59 molecule (CD59 blood group) Homo sapiens 307-311 28330937-5 2017 Single fluorescent molecule tracking in the live-cell PM revealed that they indirectly interact with each other in cholesterol- and sphingosine backbone-dependent manners, and that, for ~10-50 ms, they undergo transient colocalization-codiffusion with a glycosylphosphatidylinositol (GPI)-anchored protein, CD59 (in monomers, transient-dimer rafts, and clusters), in CD59-oligomer size-, cholesterol-, and GPI anchoring-dependent manners. Glycosylphosphatidylinositols 254-282 CD59 molecule (CD59 blood group) Homo sapiens 367-371 28330937-5 2017 Single fluorescent molecule tracking in the live-cell PM revealed that they indirectly interact with each other in cholesterol- and sphingosine backbone-dependent manners, and that, for ~10-50 ms, they undergo transient colocalization-codiffusion with a glycosylphosphatidylinositol (GPI)-anchored protein, CD59 (in monomers, transient-dimer rafts, and clusters), in CD59-oligomer size-, cholesterol-, and GPI anchoring-dependent manners. Glycosylphosphatidylinositols 284-287 CD59 molecule (CD59 blood group) Homo sapiens 307-311 28330937-5 2017 Single fluorescent molecule tracking in the live-cell PM revealed that they indirectly interact with each other in cholesterol- and sphingosine backbone-dependent manners, and that, for ~10-50 ms, they undergo transient colocalization-codiffusion with a glycosylphosphatidylinositol (GPI)-anchored protein, CD59 (in monomers, transient-dimer rafts, and clusters), in CD59-oligomer size-, cholesterol-, and GPI anchoring-dependent manners. Glycosylphosphatidylinositols 284-287 CD59 molecule (CD59 blood group) Homo sapiens 367-371 28330937-5 2017 Single fluorescent molecule tracking in the live-cell PM revealed that they indirectly interact with each other in cholesterol- and sphingosine backbone-dependent manners, and that, for ~10-50 ms, they undergo transient colocalization-codiffusion with a glycosylphosphatidylinositol (GPI)-anchored protein, CD59 (in monomers, transient-dimer rafts, and clusters), in CD59-oligomer size-, cholesterol-, and GPI anchoring-dependent manners. Glycosylphosphatidylinositols 406-409 CD59 molecule (CD59 blood group) Homo sapiens 307-311 28330937-5 2017 Single fluorescent molecule tracking in the live-cell PM revealed that they indirectly interact with each other in cholesterol- and sphingosine backbone-dependent manners, and that, for ~10-50 ms, they undergo transient colocalization-codiffusion with a glycosylphosphatidylinositol (GPI)-anchored protein, CD59 (in monomers, transient-dimer rafts, and clusters), in CD59-oligomer size-, cholesterol-, and GPI anchoring-dependent manners. Glycosylphosphatidylinositols 406-409 CD59 molecule (CD59 blood group) Homo sapiens 367-371 28516949-3 2017 The gene product of PIGA is required for the biosynthesis of glycosylphosphatidylinositol (GPI) anchors; thus, PIGA mutations lead to a deficiency of GPI-anchored proteins, such as complement decay-accelerating factor (also known as CD55) and CD59 glycoprotein (CD59), which are both complement inhibitors. Glycosylphosphatidylinositols 61-89 CD59 molecule (CD59 blood group) Homo sapiens 243-260 28516949-3 2017 The gene product of PIGA is required for the biosynthesis of glycosylphosphatidylinositol (GPI) anchors; thus, PIGA mutations lead to a deficiency of GPI-anchored proteins, such as complement decay-accelerating factor (also known as CD55) and CD59 glycoprotein (CD59), which are both complement inhibitors. Glycosylphosphatidylinositols 61-89 CD59 molecule (CD59 blood group) Homo sapiens 243-247 28516949-3 2017 The gene product of PIGA is required for the biosynthesis of glycosylphosphatidylinositol (GPI) anchors; thus, PIGA mutations lead to a deficiency of GPI-anchored proteins, such as complement decay-accelerating factor (also known as CD55) and CD59 glycoprotein (CD59), which are both complement inhibitors. Glycosylphosphatidylinositols 91-94 CD59 molecule (CD59 blood group) Homo sapiens 243-260 28516949-3 2017 The gene product of PIGA is required for the biosynthesis of glycosylphosphatidylinositol (GPI) anchors; thus, PIGA mutations lead to a deficiency of GPI-anchored proteins, such as complement decay-accelerating factor (also known as CD55) and CD59 glycoprotein (CD59), which are both complement inhibitors. Glycosylphosphatidylinositols 91-94 CD59 molecule (CD59 blood group) Homo sapiens 243-247 26033571-1 2015 The glycolipid glycosylphosphatidylinositol anchor (GPI-A) plays an important role in lipid raft formation, which is required for proper expression on the cell surface of two inhibitors of the complement cascade, CD55 and CD59. Glycosylphosphatidylinositols 15-43 CD59 molecule (CD59 blood group) Homo sapiens 222-226 27187193-5 2015 CD59 is inserted into the membrane by a glycosylphosphatidylinositol (GPI) anchor. Glycosylphosphatidylinositols 40-68 CD59 molecule (CD59 blood group) Homo sapiens 0-4 26271970-0 2015 [Mutation of palmitoylation site of linker for activation of T cells inhibits signal transduction mediated by glycosyl phosphatidyl inositol-anchored CD59 in T cells]. Glycosylphosphatidylinositols 110-140 CD59 molecule (CD59 blood group) Homo sapiens 150-154 27187193-5 2015 CD59 is inserted into the membrane by a glycosylphosphatidylinositol (GPI) anchor. Glycosylphosphatidylinositols 70-73 CD59 molecule (CD59 blood group) Homo sapiens 0-4 24454946-1 2014 The glycosylphosphatidylinositol (GPI)-anchored molecule CD59 has been implicated in the modulation of T cell responses, but the underlying molecular mechanism of CD59 influencing T cell signaling remained unclear. Glycosylphosphatidylinositols 4-32 CD59 molecule (CD59 blood group) Homo sapiens 57-61 25237200-2 2014 The absence of two glycosylphosphatidylinositol (GPI)-anchored proteins, CD55 and CD59, leads to uncontrolled complement activation that accounts for hemolysis and other PNH manifestations. Glycosylphosphatidylinositols 19-47 CD59 molecule (CD59 blood group) Homo sapiens 82-86 25237200-2 2014 The absence of two glycosylphosphatidylinositol (GPI)-anchored proteins, CD55 and CD59, leads to uncontrolled complement activation that accounts for hemolysis and other PNH manifestations. Glycosylphosphatidylinositols 49-52 CD59 molecule (CD59 blood group) Homo sapiens 82-86 25161188-1 2014 UNLABELLED: A subgroup of the cholesterol-dependent cytolysin (CDC) family of pore-forming toxins (PFTs) has an unusually narrow host range due to a requirement for binding to human CD59 (hCD59), a glycosylphosphatidylinositol (GPI)-linked complement regulatory molecule. Glycosylphosphatidylinositols 198-226 CD59 molecule (CD59 blood group) Homo sapiens 182-186 25161188-1 2014 UNLABELLED: A subgroup of the cholesterol-dependent cytolysin (CDC) family of pore-forming toxins (PFTs) has an unusually narrow host range due to a requirement for binding to human CD59 (hCD59), a glycosylphosphatidylinositol (GPI)-linked complement regulatory molecule. Glycosylphosphatidylinositols 198-226 CD59 molecule (CD59 blood group) Homo sapiens 188-193 25161188-1 2014 UNLABELLED: A subgroup of the cholesterol-dependent cytolysin (CDC) family of pore-forming toxins (PFTs) has an unusually narrow host range due to a requirement for binding to human CD59 (hCD59), a glycosylphosphatidylinositol (GPI)-linked complement regulatory molecule. Glycosylphosphatidylinositols 228-231 CD59 molecule (CD59 blood group) Homo sapiens 182-186 25161188-1 2014 UNLABELLED: A subgroup of the cholesterol-dependent cytolysin (CDC) family of pore-forming toxins (PFTs) has an unusually narrow host range due to a requirement for binding to human CD59 (hCD59), a glycosylphosphatidylinositol (GPI)-linked complement regulatory molecule. Glycosylphosphatidylinositols 228-231 CD59 molecule (CD59 blood group) Homo sapiens 188-193 24454946-1 2014 The glycosylphosphatidylinositol (GPI)-anchored molecule CD59 has been implicated in the modulation of T cell responses, but the underlying molecular mechanism of CD59 influencing T cell signaling remained unclear. Glycosylphosphatidylinositols 34-37 CD59 molecule (CD59 blood group) Homo sapiens 57-61 24454946-1 2014 The glycosylphosphatidylinositol (GPI)-anchored molecule CD59 has been implicated in the modulation of T cell responses, but the underlying molecular mechanism of CD59 influencing T cell signaling remained unclear. Glycosylphosphatidylinositols 34-37 CD59 molecule (CD59 blood group) Homo sapiens 163-167 23694781-4 2013 Overexpression of PIGV, which encodes GPI mannosyltransferase II, restored the surface expression of CD59 and normalized the accumulation of GPI intermediates in the mutant cells. Glycosylphosphatidylinositols 38-41 CD59 molecule (CD59 blood group) Homo sapiens 101-105 22539359-3 2012 The determination of glycosylphosphatidylinositol (GPI) deficient cells on the erythroid lineage was made with a two-color FCM assay of CD71 and CD59, evaluating the PNH clone on i-RET. Glycosylphosphatidylinositols 51-54 CD59 molecule (CD59 blood group) Homo sapiens 145-149 23746236-1 2013 OBJECTIVE: To investigate the distributions of GPI-anchored protein CD59 and C-terminal Src kinase-binding protein (Cbp) in cell membrane of T lymphocytes and the roles in cell activation and proliferation. Glycosylphosphatidylinositols 47-50 CD59 molecule (CD59 blood group) Homo sapiens 68-72 16493049-0 2006 Expression of glycosylphosphatidylinositol-anchored CD59 on target cells enhances human NK cell-mediated cytotoxicity. Glycosylphosphatidylinositols 14-42 CD59 molecule (CD59 blood group) Homo sapiens 52-56 22188591-13 2011 PERLD1 is involved in the modification of the glycosylphosphatidylinositol anchors for cell surface markers such as CD48 and CD59 which are known to play multiple roles in T-cell activation and proliferation. Glycosylphosphatidylinositols 46-74 CD59 molecule (CD59 blood group) Homo sapiens 125-129 19463836-7 2009 Interestingly, about 60% of the CD59 negative clones were actually GPI mutants determined by staining with the GPI specific fluorescently labeled bacterial toxin aerolysin (FLAER). Glycosylphosphatidylinositols 67-70 CD59 molecule (CD59 blood group) Homo sapiens 32-36 18428041-15 2008 Glycosyl phosphatidylinositol-anchored CD59 was identified as a mobile "echinophilic" but "raftophobic(GM1)" protein. Glycosylphosphatidylinositols 0-29 CD59 molecule (CD59 blood group) Homo sapiens 39-43 17289551-2 2007 Two of these regulators in humans, CD55 and CD59, are glycosylphosphatidylinositol-anchored, type I cell surface proteins, which inhibit formation of the C3 convertases and prevent the terminal polymerization of the membrane attack complex, respectively. Glycosylphosphatidylinositols 54-82 CD59 molecule (CD59 blood group) Homo sapiens 44-48 21183681-8 2011 The increased cellular levels of Dol-P-Man and possibly the decreased cholesterol levels in zaragozic acid A-treated cells also led to increased availability of the glycosylphosphatidylinositol anchor as shown by the elevated cell-surface expression of the CD59 protein. Glycosylphosphatidylinositols 165-193 CD59 molecule (CD59 blood group) Homo sapiens 257-261 21315037-1 2011 AIM: To study the enhancement effect of glycosylphosphatidyl inositol (GPI)-anchored protein CD59 on CD55-mediated T cell signal transduction. Glycosylphosphatidylinositols 40-69 CD59 molecule (CD59 blood group) Homo sapiens 93-97 21315037-1 2011 AIM: To study the enhancement effect of glycosylphosphatidyl inositol (GPI)-anchored protein CD59 on CD55-mediated T cell signal transduction. Glycosylphosphatidylinositols 71-74 CD59 molecule (CD59 blood group) Homo sapiens 93-97 17989688-2 2007 In the rare hemolytic disease paroxysmal nocturnal hemoglobinuria (PNH), somatic mutations result in a deficiency of glycosylphosphatidylinositol-linked surface proteins, including the terminal complement inhibitor CD59, on hematopoietic stem cells. Glycosylphosphatidylinositols 117-145 CD59 molecule (CD59 blood group) Homo sapiens 215-219 16827894-2 2006 CD55 & CD59, two glycosylphosphatidylinositol (GPI)-anchored proteins, have been detected previously in some studies also in the acrosomal region of chemically fixed spermatozoa but never demonstrated at this site on unfixed spermatozoa. Glycosylphosphatidylinositols 21-49 CD59 molecule (CD59 blood group) Homo sapiens 11-15 16827894-2 2006 CD55 & CD59, two glycosylphosphatidylinositol (GPI)-anchored proteins, have been detected previously in some studies also in the acrosomal region of chemically fixed spermatozoa but never demonstrated at this site on unfixed spermatozoa. Glycosylphosphatidylinositols 51-54 CD59 molecule (CD59 blood group) Homo sapiens 11-15 16827894-7 2006 Both CD55 & CD59 were released from the IAM by PI-PLC, demonstrating them to be GPI-anchored. Glycosylphosphatidylinositols 84-87 CD59 molecule (CD59 blood group) Homo sapiens 16-20 16493049-10 2006 GPI-anchored CD59, with or without glycosylation, mediated activation events, whereas CD59 forms lacking the GPI anchor did not. Glycosylphosphatidylinositols 0-3 CD59 molecule (CD59 blood group) Homo sapiens 13-17 16493049-11 2006 The data show that the increased susceptibility of target cells expressing CD59 to NK cytotoxicity requires GPI anchor-mediating signaling events, likely mediated by interactions between GPI-anchored CD59 on targets and NK receptors. Glycosylphosphatidylinositols 108-111 CD59 molecule (CD59 blood group) Homo sapiens 75-79 16493049-11 2006 The data show that the increased susceptibility of target cells expressing CD59 to NK cytotoxicity requires GPI anchor-mediating signaling events, likely mediated by interactions between GPI-anchored CD59 on targets and NK receptors. Glycosylphosphatidylinositols 108-111 CD59 molecule (CD59 blood group) Homo sapiens 200-204 16091585-5 2005 As expected, caveolin and GPI-bound proteins CD55, CD59 and GPI-bound form of CD58 were preferentially localized in detergent-resistant membrane domains (DRMs). Glycosylphosphatidylinositols 26-29 CD59 molecule (CD59 blood group) Homo sapiens 51-55 15907827-10 2005 CONCLUSION: The decreased GPI-PLD expression may reduce the release of GPI-anchored CD55 and CD59 in leukemia cells and finally decrease complement mediated killing of these cells in chronic phase of CML. Glycosylphosphatidylinositols 26-29 CD59 molecule (CD59 blood group) Homo sapiens 93-97 15389819-2 2005 They express the glycosylphosphatidylinositol (GPI)-anchored complement regulatory protein CD59, which has been shown to be transferred to spermatozoa and erythrocytes. Glycosylphosphatidylinositols 17-45 CD59 molecule (CD59 blood group) Homo sapiens 91-95 15389819-2 2005 They express the glycosylphosphatidylinositol (GPI)-anchored complement regulatory protein CD59, which has been shown to be transferred to spermatozoa and erythrocytes. Glycosylphosphatidylinositols 47-50 CD59 molecule (CD59 blood group) Homo sapiens 91-95 15543155-3 2004 We show here that ILY, via its domain 4 structure, binds to the glycosyl-phosphatidylinositol-linked membrane protein human CD59 (huCD59). Glycosylphosphatidylinositols 64-93 CD59 molecule (CD59 blood group) Homo sapiens 124-128 14687727-0 2003 Determination of CD59 protein in normal human serum by enzyme immunoassay, using octyl-glucoside detergent to release glycosyl-phosphatidylinositol-CD59 from lipid complex. Glycosylphosphatidylinositols 118-147 CD59 molecule (CD59 blood group) Homo sapiens 17-21 15325283-3 2004 Confocal microscopic colocalization experiments with GM(1) gangliosides and the GPI-anchored CD59 molecules showed enrichment of HLA I, HLA-DR, and ICAM-1 molecules in specific membrane domains (lipid rafts) excluding the transferrin receptor. Glycosylphosphatidylinositols 80-83 CD59 molecule (CD59 blood group) Homo sapiens 93-97 14687727-0 2003 Determination of CD59 protein in normal human serum by enzyme immunoassay, using octyl-glucoside detergent to release glycosyl-phosphatidylinositol-CD59 from lipid complex. Glycosylphosphatidylinositols 118-147 CD59 molecule (CD59 blood group) Homo sapiens 148-152 14687727-2 2003 The glycosyl-phosphatidylinositol (GPI)-linked form of CD59 is known to complex with serum high-density lipoprotein. Glycosylphosphatidylinositols 4-33 CD59 molecule (CD59 blood group) Homo sapiens 55-59 14687727-2 2003 The glycosyl-phosphatidylinositol (GPI)-linked form of CD59 is known to complex with serum high-density lipoprotein. Glycosylphosphatidylinositols 35-38 CD59 molecule (CD59 blood group) Homo sapiens 55-59 12747280-0 2003 Impaired expression of erythrocyte glycosyl-phosphatidylinositol-anchored membrane CD59 in patients with psoriatic arthritis. Glycosylphosphatidylinositols 35-64 CD59 molecule (CD59 blood group) Homo sapiens 83-87 12902469-3 2003 Triggering CD147 induces a displacement of the GPI-anchored coreceptors CD48 and CD59 from microdomains in human T lymphocytes. Glycosylphosphatidylinositols 47-50 CD59 molecule (CD59 blood group) Homo sapiens 81-85 12645951-5 2003 Exosomes express the glycosylphosphatidylinositol (GPI)-anchored regulators CD55 and CD59, but not the transmembrane protein CD46. Glycosylphosphatidylinositols 21-49 CD59 molecule (CD59 blood group) Homo sapiens 85-89 12645951-5 2003 Exosomes express the glycosylphosphatidylinositol (GPI)-anchored regulators CD55 and CD59, but not the transmembrane protein CD46. Glycosylphosphatidylinositols 51-54 CD59 molecule (CD59 blood group) Homo sapiens 85-89 12370246-6 2002 Depletion of endogenous MAL2 drastically blocked transcytotic transport of exogenous polymeric immunoglobulin receptor and endogenous glycosylphosphatidylinositol-anchored protein CD59 to the apical membrane. Glycosylphosphatidylinositols 134-162 CD59 molecule (CD59 blood group) Homo sapiens 180-184 12453906-5 2002 The diabetic donors showed a prominent reduction in the retinal levels of CD55 and CD59, the two complement inhibitors linked to the plasma membrane by glycosylphosphatidylinositol anchors, but not in the levels of transmembrane CD46. Glycosylphosphatidylinositols 152-180 CD59 molecule (CD59 blood group) Homo sapiens 83-87 12385028-6 2002 By contrast, in the same conditions, Ca2+ signaling via the glycosylphosphatidylinositol (GPI)-anchored protein CD59 is totally abolished. Glycosylphosphatidylinositols 60-88 CD59 molecule (CD59 blood group) Homo sapiens 112-116 12385028-6 2002 By contrast, in the same conditions, Ca2+ signaling via the glycosylphosphatidylinositol (GPI)-anchored protein CD59 is totally abolished. Glycosylphosphatidylinositols 90-93 CD59 molecule (CD59 blood group) Homo sapiens 112-116 12239154-2 2002 PRV-1 is a member of the uPAR/CD59/Ly6 family of cell surface receptors, which share a common cysteine-rich domain and are tethered to the cell surface via a glycosylphosphatidylinositol (GPI) link. Glycosylphosphatidylinositols 158-186 CD59 molecule (CD59 blood group) Homo sapiens 30-34 12239154-2 2002 PRV-1 is a member of the uPAR/CD59/Ly6 family of cell surface receptors, which share a common cysteine-rich domain and are tethered to the cell surface via a glycosylphosphatidylinositol (GPI) link. Glycosylphosphatidylinositols 188-191 CD59 molecule (CD59 blood group) Homo sapiens 30-34 12054528-3 2002 Here we report the construction and expression of a fluorescent GPI anchor on the surface of CHO, EL4, and U937 cells by fusing green fluorescent protein (GFP) to the GPI-attachment site of CD59. Glycosylphosphatidylinositols 167-170 CD59 molecule (CD59 blood group) Homo sapiens 190-194 12054528-3 2002 Here we report the construction and expression of a fluorescent GPI anchor on the surface of CHO, EL4, and U937 cells by fusing green fluorescent protein (GFP) to the GPI-attachment site of CD59. Glycosylphosphatidylinositols 64-67 CD59 molecule (CD59 blood group) Homo sapiens 190-194 12042249-2 2002 N-Linked glycans were released with peptide-N-glycosidase F (PNGase F) within gel from SDS-PAGE-isolated soluble and glycosylphosphatidylinositol (GPI)-anchored human CD59 expressed in CHO cells. Glycosylphosphatidylinositols 117-145 CD59 molecule (CD59 blood group) Homo sapiens 167-171 12042249-2 2002 N-Linked glycans were released with peptide-N-glycosidase F (PNGase F) within gel from SDS-PAGE-isolated soluble and glycosylphosphatidylinositol (GPI)-anchored human CD59 expressed in CHO cells. Glycosylphosphatidylinositols 147-150 CD59 molecule (CD59 blood group) Homo sapiens 167-171 12186694-1 2002 CD55 and CD59 are complement regulatory proteins that are linked to the cell membrane via a glycosyl-phosphatidylinositol anchor. Glycosylphosphatidylinositols 92-121 CD59 molecule (CD59 blood group) Homo sapiens 9-13 11056001-2 2000 Protectin (CD59) is a glycosylphosphatidylinositol (GPI)-anchored cell membrane glycoprotein, acting as terminal regulator of C cascade, which is heterogeneously expressed in melanomas and represents the main restriction factor of C-mediated lysis of melanoma cells. Glycosylphosphatidylinositols 22-50 CD59 molecule (CD59 blood group) Homo sapiens 0-9 12069204-1 2002 PROBLEM: Prostasomes isolated from human seminal plasma have complement regulatory properties because of their content of CD59, a glycosylphosphatidylinositol (GPI)-anchored protein. Glycosylphosphatidylinositols 130-158 CD59 molecule (CD59 blood group) Homo sapiens 122-126 12069204-1 2002 PROBLEM: Prostasomes isolated from human seminal plasma have complement regulatory properties because of their content of CD59, a glycosylphosphatidylinositol (GPI)-anchored protein. Glycosylphosphatidylinositols 160-163 CD59 molecule (CD59 blood group) Homo sapiens 122-126 11807824-1 2002 Protectin (CD59) is a glycosylphosphatidylinositol (GPI)-anchored cell membrane glycoprotein, broadly expressed on melanocytic cells, that represents the main restriction factor of complement (C)-mediated lysis of human melanoma cells. Glycosylphosphatidylinositols 22-50 CD59 molecule (CD59 blood group) Homo sapiens 11-15 11807824-1 2002 Protectin (CD59) is a glycosylphosphatidylinositol (GPI)-anchored cell membrane glycoprotein, broadly expressed on melanocytic cells, that represents the main restriction factor of complement (C)-mediated lysis of human melanoma cells. Glycosylphosphatidylinositols 52-55 CD59 molecule (CD59 blood group) Homo sapiens 11-15 11180111-1 2001 The glycosylphosphatidylinositol (GPI)-anchored protein CD59 and the ganglioside GM1 are present on lipid rafts that can be isolated in a detergent-insoluble membrane (DIM) fraction. Glycosylphosphatidylinositols 4-32 CD59 molecule (CD59 blood group) Homo sapiens 56-60 11180111-1 2001 The glycosylphosphatidylinositol (GPI)-anchored protein CD59 and the ganglioside GM1 are present on lipid rafts that can be isolated in a detergent-insoluble membrane (DIM) fraction. Glycosylphosphatidylinositols 34-37 CD59 molecule (CD59 blood group) Homo sapiens 56-60 11262607-1 2000 PURPOSE: The decay accelerating factor (DAF or CD55) and the membrane inhibitor of reactive lysis (MIRL or CD59), two complement regulatory proteins that protect self cells from autologous complement-mediated injury, are attached to corneal and cqonjunctival epithelial cells by glycosylphos-phatidylinositol (GPI) anchors. Glycosylphosphatidylinositols 279-308 CD59 molecule (CD59 blood group) Homo sapiens 61-97 11262607-1 2000 PURPOSE: The decay accelerating factor (DAF or CD55) and the membrane inhibitor of reactive lysis (MIRL or CD59), two complement regulatory proteins that protect self cells from autologous complement-mediated injury, are attached to corneal and cqonjunctival epithelial cells by glycosylphos-phatidylinositol (GPI) anchors. Glycosylphosphatidylinositols 279-308 CD59 molecule (CD59 blood group) Homo sapiens 99-103 11262607-1 2000 PURPOSE: The decay accelerating factor (DAF or CD55) and the membrane inhibitor of reactive lysis (MIRL or CD59), two complement regulatory proteins that protect self cells from autologous complement-mediated injury, are attached to corneal and cqonjunctival epithelial cells by glycosylphos-phatidylinositol (GPI) anchors. Glycosylphosphatidylinositols 279-308 CD59 molecule (CD59 blood group) Homo sapiens 107-111 11262607-1 2000 PURPOSE: The decay accelerating factor (DAF or CD55) and the membrane inhibitor of reactive lysis (MIRL or CD59), two complement regulatory proteins that protect self cells from autologous complement-mediated injury, are attached to corneal and cqonjunctival epithelial cells by glycosylphos-phatidylinositol (GPI) anchors. Glycosylphosphatidylinositols 310-313 CD59 molecule (CD59 blood group) Homo sapiens 61-97 11262607-1 2000 PURPOSE: The decay accelerating factor (DAF or CD55) and the membrane inhibitor of reactive lysis (MIRL or CD59), two complement regulatory proteins that protect self cells from autologous complement-mediated injury, are attached to corneal and cqonjunctival epithelial cells by glycosylphos-phatidylinositol (GPI) anchors. Glycosylphosphatidylinositols 310-313 CD59 molecule (CD59 blood group) Homo sapiens 99-103 11262607-1 2000 PURPOSE: The decay accelerating factor (DAF or CD55) and the membrane inhibitor of reactive lysis (MIRL or CD59), two complement regulatory proteins that protect self cells from autologous complement-mediated injury, are attached to corneal and cqonjunctival epithelial cells by glycosylphos-phatidylinositol (GPI) anchors. Glycosylphosphatidylinositols 310-313 CD59 molecule (CD59 blood group) Homo sapiens 107-111 11056001-2 2000 Protectin (CD59) is a glycosylphosphatidylinositol (GPI)-anchored cell membrane glycoprotein, acting as terminal regulator of C cascade, which is heterogeneously expressed in melanomas and represents the main restriction factor of C-mediated lysis of melanoma cells. Glycosylphosphatidylinositols 22-50 CD59 molecule (CD59 blood group) Homo sapiens 11-15 11056001-2 2000 Protectin (CD59) is a glycosylphosphatidylinositol (GPI)-anchored cell membrane glycoprotein, acting as terminal regulator of C cascade, which is heterogeneously expressed in melanomas and represents the main restriction factor of C-mediated lysis of melanoma cells. Glycosylphosphatidylinositols 52-55 CD59 molecule (CD59 blood group) Homo sapiens 0-9 11056001-2 2000 Protectin (CD59) is a glycosylphosphatidylinositol (GPI)-anchored cell membrane glycoprotein, acting as terminal regulator of C cascade, which is heterogeneously expressed in melanomas and represents the main restriction factor of C-mediated lysis of melanoma cells. Glycosylphosphatidylinositols 52-55 CD59 molecule (CD59 blood group) Homo sapiens 11-15 10708443-2 2000 These domains can be viewed as floating rafts composed of sphingolipids and cholesterol which sequester glycosylphosphatidylinositol (GPI)-linked proteins, such as Thy-1 and CD59. Glycosylphosphatidylinositols 104-132 CD59 molecule (CD59 blood group) Homo sapiens 174-178 11013013-2 2000 Our earlier immunohistochemical studies have shown that the deposition of the membrane attack complex (MAC) of complement is associated with the loss of protectin (CD59), a glycosyl-phosphatidylinositol (GPI)-anchored sarcolemmal regulator of MAC, from the human and rat infarcted myocardium. Glycosylphosphatidylinositols 173-202 CD59 molecule (CD59 blood group) Homo sapiens 153-162 11013013-2 2000 Our earlier immunohistochemical studies have shown that the deposition of the membrane attack complex (MAC) of complement is associated with the loss of protectin (CD59), a glycosyl-phosphatidylinositol (GPI)-anchored sarcolemmal regulator of MAC, from the human and rat infarcted myocardium. Glycosylphosphatidylinositols 173-202 CD59 molecule (CD59 blood group) Homo sapiens 164-168 10950945-1 2000 To detect a small population of blood cells with a deficiency of glycosyl phosphatidylinositol (GPI)-anchored protein, we evaluated the expression of CD59 by flow cytometry on one million erythrocytes, which is about 100 times more than the number of erythrocytes tested by our standard immunoassay. Glycosylphosphatidylinositols 96-99 CD59 molecule (CD59 blood group) Homo sapiens 150-154 10950945-8 2000 The CD59 assay used in this study is easy to perform and enabled us to detect less than 1% GPI-deficient cells. Glycosylphosphatidylinositols 91-94 CD59 molecule (CD59 blood group) Homo sapiens 4-8 10801333-1 2000 Formation of the membrane attack complex (MAC) of complement on host cells is inhibited by the glycosylphosphatidylinositol- (GPI-) anchored glycoprotein CD59. Glycosylphosphatidylinositols 95-123 CD59 molecule (CD59 blood group) Homo sapiens 154-158 10760796-3 2000 We show here that the glycosylphosphatidylinositol linked CD59 molecule is expressed at the surface of Jurkat and J.RT3.T3.5 cells, and when cross-linked by specific antibodies can induce cell death. Glycosylphosphatidylinositols 22-50 CD59 molecule (CD59 blood group) Homo sapiens 58-62 10708443-2 2000 These domains can be viewed as floating rafts composed of sphingolipids and cholesterol which sequester glycosylphosphatidylinositol (GPI)-linked proteins, such as Thy-1 and CD59. Glycosylphosphatidylinositols 134-137 CD59 molecule (CD59 blood group) Homo sapiens 174-178 9834251-2 1998 Intravascular red blood cell (RBC) destruction is caused by increased sensitivity of the abnormal erythrocyte to complement-mediated lysis, due to the GPI absence of a membrane-bound glycosylphosphatidylinositol (GPI)-linked protein, which functions as an inhibitor of reactive lysis (CD59). Glycosylphosphatidylinositols 183-211 CD59 molecule (CD59 blood group) Homo sapiens 285-289 10571018-2 1999 A considerable part of erythrocytes in patient blood is susceptible to autologous complement activation because of the deficiency of CD59, which is a glycosylphosphatidylinositol (GPI)-anchored protein and inhibits the formation of the membrane attack complex (MAC) of complement. Glycosylphosphatidylinositols 150-178 CD59 molecule (CD59 blood group) Homo sapiens 133-137 10571018-2 1999 A considerable part of erythrocytes in patient blood is susceptible to autologous complement activation because of the deficiency of CD59, which is a glycosylphosphatidylinositol (GPI)-anchored protein and inhibits the formation of the membrane attack complex (MAC) of complement. Glycosylphosphatidylinositols 180-183 CD59 molecule (CD59 blood group) Homo sapiens 133-137 10064071-5 1999 We found that raft patches formed by GPI-anchored CD59 protein and the ganglioside GM1 accumulate filamentous actin. Glycosylphosphatidylinositols 37-40 CD59 molecule (CD59 blood group) Homo sapiens 50-54 9842910-6 1998 Co-immunoprecipitation experiments with antibodies to the MAL molecule or to the GPI-anchored CD59 antigen indicated specific association of MAL with GPI-anchored proteins and Src-like tyrosine kinases. Glycosylphosphatidylinositols 81-84 CD59 molecule (CD59 blood group) Homo sapiens 94-98 9813086-4 1998 Jurkat T cells cultured in PUFA-supplemented medium showed a markedly diminished calcium response when stimulated via the transmembrane CD3 complex or glycosyl phosphatidylinositol (GPI)- anchored CD59. Glycosylphosphatidylinositols 151-180 CD59 molecule (CD59 blood group) Homo sapiens 197-201 9813086-4 1998 Jurkat T cells cultured in PUFA-supplemented medium showed a markedly diminished calcium response when stimulated via the transmembrane CD3 complex or glycosyl phosphatidylinositol (GPI)- anchored CD59. Glycosylphosphatidylinositols 182-185 CD59 molecule (CD59 blood group) Homo sapiens 197-201 9761744-5 1998 From endothelial cells, MBCD released GPI-anchored CD59, and CD44, but only a negligible amount of caveolin. Glycosylphosphatidylinositols 38-41 CD59 molecule (CD59 blood group) Homo sapiens 51-55 9538246-1 1998 Human glycosyl phosphatidylinositol-anchored protein CD59 was solubilized in detergent-insoluble complexes (DICs) and in post-nuclear pellets by a two-step solubilization procedure using Triton X-100 and octylglucoside. Glycosylphosphatidylinositols 6-35 CD59 molecule (CD59 blood group) Homo sapiens 53-57 9737993-1 1998 CD59 is a glycosylphosphatidylinositol-anchored cell surface glycoprotein involved in protecting cells from host-mediated complement attack. Glycosylphosphatidylinositols 10-38 CD59 molecule (CD59 blood group) Homo sapiens 0-4 27405407-4 1997 The abnormal sensitivity is explained by a lack of complement regulatory membrane proteins such as decay-accelerating factor (DAF, CD55) and membrane inhibitor of reactive lysis (MIRL, CD59), which are covalently linked to the erythrocyte membrane through a glycosylphosphatidylinositol (GPI) anchor. Glycosylphosphatidylinositols 258-286 CD59 molecule (CD59 blood group) Homo sapiens 141-177 9371784-7 1997 Highly mobile membrane components, phosphatidylethanolamine- and glycosylphosphatidylinositol-linked CD59 with no specific skeletal association were enriched in the vesicle. Glycosylphosphatidylinositols 65-93 CD59 molecule (CD59 blood group) Homo sapiens 101-105 9276743-1 1997 Protectin (CD59), a glycosylphosphatidylinositol-anchored cell membrane glycoprotein, is differentially expressed on melanocytic cells and represents the main restriction factor of C-mediated lysis of melanoma cells. Glycosylphosphatidylinositols 20-48 CD59 molecule (CD59 blood group) Homo sapiens 0-9 9276743-1 1997 Protectin (CD59), a glycosylphosphatidylinositol-anchored cell membrane glycoprotein, is differentially expressed on melanocytic cells and represents the main restriction factor of C-mediated lysis of melanoma cells. Glycosylphosphatidylinositols 20-48 CD59 molecule (CD59 blood group) Homo sapiens 11-15 9185710-8 1997 Treatment of DU 145 and PC3 cells with phosphatidylinositol-specific phospholipase C caused a significant decrease of CD59 expression indicating that the CD59 expressed by prostate cancer cells is anchored to the cell membrane via a glycosylphosphatidylinositol (GPI) linkage. Glycosylphosphatidylinositols 233-261 CD59 molecule (CD59 blood group) Homo sapiens 154-158 9185710-8 1997 Treatment of DU 145 and PC3 cells with phosphatidylinositol-specific phospholipase C caused a significant decrease of CD59 expression indicating that the CD59 expressed by prostate cancer cells is anchored to the cell membrane via a glycosylphosphatidylinositol (GPI) linkage. Glycosylphosphatidylinositols 263-266 CD59 molecule (CD59 blood group) Homo sapiens 154-158 9185710-10 1997 We conclude that malignant and benign human prostate cells express CD59 that is GPI-linked to the cell surface and that CD59 may regulate the immunological response to cancerous prostate cells by protecting the cells from the cytolytic activity of complement. Glycosylphosphatidylinositols 80-83 CD59 molecule (CD59 blood group) Homo sapiens 67-71 9054419-1 1997 Human erythrocyte CD59 contains N- and O-glycans and a glycosylphosphatidylinositol (GPI) anchor, all of which have been analyzed in this study. Glycosylphosphatidylinositols 55-83 CD59 molecule (CD59 blood group) Homo sapiens 18-22 9054419-1 1997 Human erythrocyte CD59 contains N- and O-glycans and a glycosylphosphatidylinositol (GPI) anchor, all of which have been analyzed in this study. Glycosylphosphatidylinositols 85-88 CD59 molecule (CD59 blood group) Homo sapiens 18-22 27405407-4 1997 The abnormal sensitivity is explained by a lack of complement regulatory membrane proteins such as decay-accelerating factor (DAF, CD55) and membrane inhibitor of reactive lysis (MIRL, CD59), which are covalently linked to the erythrocyte membrane through a glycosylphosphatidylinositol (GPI) anchor. Glycosylphosphatidylinositols 258-286 CD59 molecule (CD59 blood group) Homo sapiens 179-183 27405407-4 1997 The abnormal sensitivity is explained by a lack of complement regulatory membrane proteins such as decay-accelerating factor (DAF, CD55) and membrane inhibitor of reactive lysis (MIRL, CD59), which are covalently linked to the erythrocyte membrane through a glycosylphosphatidylinositol (GPI) anchor. Glycosylphosphatidylinositols 258-286 CD59 molecule (CD59 blood group) Homo sapiens 185-189 27405407-4 1997 The abnormal sensitivity is explained by a lack of complement regulatory membrane proteins such as decay-accelerating factor (DAF, CD55) and membrane inhibitor of reactive lysis (MIRL, CD59), which are covalently linked to the erythrocyte membrane through a glycosylphosphatidylinositol (GPI) anchor. Glycosylphosphatidylinositols 288-291 CD59 molecule (CD59 blood group) Homo sapiens 141-177 27405407-4 1997 The abnormal sensitivity is explained by a lack of complement regulatory membrane proteins such as decay-accelerating factor (DAF, CD55) and membrane inhibitor of reactive lysis (MIRL, CD59), which are covalently linked to the erythrocyte membrane through a glycosylphosphatidylinositol (GPI) anchor. Glycosylphosphatidylinositols 288-291 CD59 molecule (CD59 blood group) Homo sapiens 179-183 27405407-4 1997 The abnormal sensitivity is explained by a lack of complement regulatory membrane proteins such as decay-accelerating factor (DAF, CD55) and membrane inhibitor of reactive lysis (MIRL, CD59), which are covalently linked to the erythrocyte membrane through a glycosylphosphatidylinositol (GPI) anchor. Glycosylphosphatidylinositols 288-291 CD59 molecule (CD59 blood group) Homo sapiens 185-189 8890564-1 1996 Decay-accelerating factor (DAF) and CD59 are major complement regulators linked to plasma membrane via glycosylphosphatidylinositol anchor and inhibit C3 activation and the formation of membrane attack complex, respectively. Glycosylphosphatidylinositols 103-131 CD59 molecule (CD59 blood group) Homo sapiens 36-40 8898942-3 1996 On the other hand, there are indications that signaling through T cell surface molecules anchored via glycosylphosphatidylinositol (GPI), such as Thy-1, Ly-6 or CD59, is dependent on the TCR. Glycosylphosphatidylinositols 102-130 CD59 molecule (CD59 blood group) Homo sapiens 161-165 8798614-1 1996 CD59 is a glycosylphosphatidylinositol-anchored membrane glycoprotein that serves as the principle cellular inhibitor of the C5b-9 membrane attack complex (MAC) of human complement. Glycosylphosphatidylinositols 10-38 CD59 molecule (CD59 blood group) Homo sapiens 0-4 8650218-5 1996 When the GPI-anchored proteins CD59, CD48, and Thy-1 were immunoprecipitated from various cell lines or freshly isolated lymphocytes, all were found to be associated with a 41-kDa phosphoprotein that we have identified, by using specific antisera, as a mixture of tyrosine phosphorylated G protein alpha subunits: a small amount of Gialpha1, and substantial amounts of Gialpha2 and Gialpha3. Glycosylphosphatidylinositols 9-12 CD59 molecule (CD59 blood group) Homo sapiens 31-35 8759753-2 1996 Membrane inhibitor of reactive lysis (MIRL, CD59) is an 18-kDa glycosylphosphatidylinositol-anchored protein that regulates formation of the membrane attack complex of complement. Glycosylphosphatidylinositols 63-91 CD59 molecule (CD59 blood group) Homo sapiens 0-36 8759753-2 1996 Membrane inhibitor of reactive lysis (MIRL, CD59) is an 18-kDa glycosylphosphatidylinositol-anchored protein that regulates formation of the membrane attack complex of complement. Glycosylphosphatidylinositols 63-91 CD59 molecule (CD59 blood group) Homo sapiens 38-42 8759753-2 1996 Membrane inhibitor of reactive lysis (MIRL, CD59) is an 18-kDa glycosylphosphatidylinositol-anchored protein that regulates formation of the membrane attack complex of complement. Glycosylphosphatidylinositols 63-91 CD59 molecule (CD59 blood group) Homo sapiens 44-48 8569195-5 1996 CD59 is bound to melanoma cells by a glycosylphosphatidylinositol anchor: treatment of C-resistant melanoma cells Mel 97, by increasing doses of phosphatidylinositol-specific phospholipase C (PI-PLC), progressively decreased cell-surface expression of CD59 and increased C-mediated lysis of cells sensitized with mAb R24. Glycosylphosphatidylinositols 37-65 CD59 molecule (CD59 blood group) Homo sapiens 0-4 8615796-0 1996 Mechanisms by which the surface expression of the glycosyl-phosphatidylinositol-anchored complement regulatory proteins decay-accelerating factor (CD55) and CD59 is lost in human leukaemia cell lines. Glycosylphosphatidylinositols 50-79 CD59 molecule (CD59 blood group) Homo sapiens 157-161 8666664-4 1996 Here, we show that the GPI-anchored CD59 molecule on Jurkat T cells is internalized after cross-linking, a process inhibited by nystatin, a sterol chelating agent. Glycosylphosphatidylinositols 23-26 CD59 molecule (CD59 blood group) Homo sapiens 36-40 8671618-4 1996 In the two patients that were tested, the GPI-anchored surface molecules CD55 and CD59 were also absent on the CD52- cells, although expression of other cell surface transmembrane, proteins (CD3, CD4 and CD2) was unaffected. Glycosylphosphatidylinositols 42-45 CD59 molecule (CD59 blood group) Homo sapiens 82-86 9238677-7 1996 All of the post-testicularly acquired GPI-anchored proteins identified thus far have also been found on cells of the immune system (CD62, CD55, CD59, CD73), and we speculate that they may have a role in protecting spermatozoa from immune attack in the male and female reproductive tracts. Glycosylphosphatidylinositols 38-41 CD59 molecule (CD59 blood group) Homo sapiens 144-148 9238658-2 1996 Both the CD55 and CD59 glycosyl phosphatidylinositol (GPI)-anchored proteins were expressed by the plasma membrane and zona pellucida of oocytes, early embryos and expanded preimplantation blastocysts; in contrast, CD46 was expressed only on the plasma membrane. Glycosylphosphatidylinositols 23-52 CD59 molecule (CD59 blood group) Homo sapiens 18-22 9238658-2 1996 Both the CD55 and CD59 glycosyl phosphatidylinositol (GPI)-anchored proteins were expressed by the plasma membrane and zona pellucida of oocytes, early embryos and expanded preimplantation blastocysts; in contrast, CD46 was expressed only on the plasma membrane. Glycosylphosphatidylinositols 54-57 CD59 molecule (CD59 blood group) Homo sapiens 18-22 7593188-0 1995 Exogenous glycosyl phosphatidylinositol-anchored CD59 associates with kinases in membrane clusters on U937 cells and becomes Ca(2+)-signaling competent. Glycosylphosphatidylinositols 10-39 CD59 molecule (CD59 blood group) Homo sapiens 49-53 8536377-7 1995 Removal of CD59 from the cell surface by phosphatidylinositol-specific phospholipase C (PI-PLC) demonstrated its production as a glycosyl phosphatidylinositol (GPI)-anchored protein. Glycosylphosphatidylinositols 129-158 CD59 molecule (CD59 blood group) Homo sapiens 11-15 8536377-7 1995 Removal of CD59 from the cell surface by phosphatidylinositol-specific phospholipase C (PI-PLC) demonstrated its production as a glycosyl phosphatidylinositol (GPI)-anchored protein. Glycosylphosphatidylinositols 160-163 CD59 molecule (CD59 blood group) Homo sapiens 11-15 7593188-1 1995 CD59, an 18-20-kD complement inhibitor anchored to the membrane via glycosyl phosphatidylinositol (GPI), can induce activation of T cells and neutrophils upon cross-linking with antibody. Glycosylphosphatidylinositols 68-97 CD59 molecule (CD59 blood group) Homo sapiens 0-4 7593188-1 1995 CD59, an 18-20-kD complement inhibitor anchored to the membrane via glycosyl phosphatidylinositol (GPI), can induce activation of T cells and neutrophils upon cross-linking with antibody. Glycosylphosphatidylinositols 99-102 CD59 molecule (CD59 blood group) Homo sapiens 0-4 7593188-5 1995 Confocal microscopy revealed an initial diffuse distribution of CD59 that became clustered within 2 h to give a pattern similar to endogenous GPI-anchored molecules. Glycosylphosphatidylinositols 142-145 CD59 molecule (CD59 blood group) Homo sapiens 64-68 7553895-1 1995 CD55 and CD59 are both glycosylphosphatidylinositol (GPI)-anchored complement regulatory proteins found on the surface of most hemopoietic cells. Glycosylphosphatidylinositols 23-51 CD59 molecule (CD59 blood group) Homo sapiens 9-13 7553895-5 1995 Treatment with phosphatidylinositol-specific phospholipase C released both the CD55 and CD59 antigens from the surface of CD56+CD3- cells, indicating that both are GPI-anchored, as they are on other lymphocytes. Glycosylphosphatidylinositols 164-167 CD59 molecule (CD59 blood group) Homo sapiens 88-92 7553895-1 1995 CD55 and CD59 are both glycosylphosphatidylinositol (GPI)-anchored complement regulatory proteins found on the surface of most hemopoietic cells. Glycosylphosphatidylinositols 53-56 CD59 molecule (CD59 blood group) Homo sapiens 9-13 7490134-3 1995 These populations differed in their expression of the glycosyl-phosphatidylinositol (GPI)-anchored inhibitors CD59 and decay-accelerating factor (DAF). Glycosylphosphatidylinositols 54-83 CD59 molecule (CD59 blood group) Homo sapiens 110-114 7490134-3 1995 These populations differed in their expression of the glycosyl-phosphatidylinositol (GPI)-anchored inhibitors CD59 and decay-accelerating factor (DAF). Glycosylphosphatidylinositols 85-88 CD59 molecule (CD59 blood group) Homo sapiens 110-114 7490134-9 1995 As CD48, DAF and CD59 are all GPI-anchored molecules it is likely that a defect in the GPI-anchoring mechanism is responsible for the generation of the second population of cells. Glycosylphosphatidylinositols 30-33 CD59 molecule (CD59 blood group) Homo sapiens 17-21 7490134-9 1995 As CD48, DAF and CD59 are all GPI-anchored molecules it is likely that a defect in the GPI-anchoring mechanism is responsible for the generation of the second population of cells. Glycosylphosphatidylinositols 87-90 CD59 molecule (CD59 blood group) Homo sapiens 17-21 7743216-5 1995 On SH-SY5Y cells, both PCR amplification and immunocytochemistry demonstrated the presence of CD59, a glycosylphosphatidylinositol-anchored protein that restricts homologous complement activation by inhibiting the formation of the membrane attack complex. Glycosylphosphatidylinositols 102-130 CD59 molecule (CD59 blood group) Homo sapiens 94-98 7543140-1 1995 This study investigates whether cell-derived glycosylphosphatidylinositol-linked complement control proteins CD55 and CD59 can be incorporated into HIV-1 virions and contribute to complement resistance. Glycosylphosphatidylinositols 45-73 CD59 molecule (CD59 blood group) Homo sapiens 118-122 7542590-0 1995 The glycosylphosphatidylinositol-anchored CD59 protein stimulates both T cell receptor zeta/ZAP-70-dependent and -independent signaling pathways in T cells. Glycosylphosphatidylinositols 4-32 CD59 molecule (CD59 blood group) Homo sapiens 42-46 7542590-1 1995 The glycosylphosphatidylinositol (GPI)-anchored CD59 protein (human protectin) protects cells against complement-induced lysis, binds to CD2 and also transduces activation signals within T cells. Glycosylphosphatidylinositols 4-32 CD59 molecule (CD59 blood group) Homo sapiens 48-52 7542590-1 1995 The glycosylphosphatidylinositol (GPI)-anchored CD59 protein (human protectin) protects cells against complement-induced lysis, binds to CD2 and also transduces activation signals within T cells. Glycosylphosphatidylinositols 34-37 CD59 molecule (CD59 blood group) Homo sapiens 48-52 7545610-0 1995 Exogenous CD59 incorporated into U937 cells through its glycosyl phosphatidylinositol anchor becomes associated with signalling molecules in a time dependent manner. Glycosylphosphatidylinositols 56-85 CD59 molecule (CD59 blood group) Homo sapiens 10-14 7543447-6 1995 The newly expressed CD59 was functionally active and anchored through glycosyl-phosphatidylinositol (GPI). Glycosylphosphatidylinositols 70-99 CD59 molecule (CD59 blood group) Homo sapiens 20-24 7543447-6 1995 The newly expressed CD59 was functionally active and anchored through glycosyl-phosphatidylinositol (GPI). Glycosylphosphatidylinositols 101-104 CD59 molecule (CD59 blood group) Homo sapiens 20-24 7532041-1 1995 The lack of glycosylphosphatidylinositol (GPI)-anchored membrane proteins such as decay-accelerating factor (DAF) and CD59 on blood cells has a diagnostic value in paroxysmal nocturnal hemoglobinuria (PNH). Glycosylphosphatidylinositols 42-45 CD59 molecule (CD59 blood group) Homo sapiens 118-122 7524752-2 1994 Affected blood cells in PNH lack glycosylphosphatidylinositol (GPI)-anchored membrane proteins such as decay-accelerating factor (DAF) and CD59. Glycosylphosphatidylinositols 63-66 CD59 molecule (CD59 blood group) Homo sapiens 139-143 7528012-10 1994 An N-glycosylation site was identified at Asn-16 and a putative glycosylphosphatidylinositol anchor addition site at Asn-79, indicating that the mature processed protein was two residues longer than human CD59. Glycosylphosphatidylinositols 64-92 CD59 molecule (CD59 blood group) Homo sapiens 205-209 7522441-1 1994 The major glycolipid co-immunopurifying with the glycosylphosphatidylinositol-anchored leucocyte surface glycoprotein CD59 from detergent lysates of human T cell lines HPB ALL, Jurkat and myeloid line HL-60 was identified as the glycosphingolipid GM3. Glycosylphosphatidylinositols 49-77 CD59 molecule (CD59 blood group) Homo sapiens 118-122 7522635-3 1994 Specifically, somatic mutations in the phosphatidylinositol glycan class A gene result in the ability of blood cells to anchor complement-regulatory proteins (CD59 and DAF) to the cell surface via glycosyl phosphatidylinositol (GPI). Glycosylphosphatidylinositols 197-226 CD59 molecule (CD59 blood group) Homo sapiens 159-163 7522635-3 1994 Specifically, somatic mutations in the phosphatidylinositol glycan class A gene result in the ability of blood cells to anchor complement-regulatory proteins (CD59 and DAF) to the cell surface via glycosyl phosphatidylinositol (GPI). Glycosylphosphatidylinositols 228-231 CD59 molecule (CD59 blood group) Homo sapiens 159-163 7530684-6 1994 CD59 in the PNS and CNS was glycosyl-phosphatidylinositol linked and had a molecular weight of 19,000-25,000. Glycosylphosphatidylinositols 28-57 CD59 molecule (CD59 blood group) Homo sapiens 0-4 7514386-0 1994 Structural study on the glycosyl-phosphatidylinositol anchor and the asparagine-linked sugar chain of a soluble form of CD59 in human urine. Glycosylphosphatidylinositols 24-53 CD59 molecule (CD59 blood group) Homo sapiens 120-124 7517877-5 1994 CD59 on HT29 cells was glycosyl-phosphatidylinositol-linked, and had a molecular mass of 19-25 kDa. Glycosylphosphatidylinositols 23-52 CD59 molecule (CD59 blood group) Homo sapiens 0-4 7514386-2 1994 An important structural feature of CD59 is its attachment to the cell surface via a glycosyl-phosphatidylinositol (GPI) anchor. Glycosylphosphatidylinositols 84-113 CD59 molecule (CD59 blood group) Homo sapiens 35-39 7514386-2 1994 An important structural feature of CD59 is its attachment to the cell surface via a glycosyl-phosphatidylinositol (GPI) anchor. Glycosylphosphatidylinositols 115-118 CD59 molecule (CD59 blood group) Homo sapiens 35-39 7514386-4 1994 The structures of the GPI anchor and the asparagine-linked sugar chain of a soluble form of CD59 in urine, U-CD59, were determined. Glycosylphosphatidylinositols 22-25 CD59 molecule (CD59 blood group) Homo sapiens 92-96 7514386-4 1994 The structures of the GPI anchor and the asparagine-linked sugar chain of a soluble form of CD59 in urine, U-CD59, were determined. Glycosylphosphatidylinositols 22-25 CD59 molecule (CD59 blood group) Homo sapiens 109-113 7514386-7 1994 The peptide containing an asparagine-linked sugar chain and the peptide containing a glycan portion of the GPI anchor were isolated after trypsin digestion of U-CD59. Glycosylphosphatidylinositols 107-110 CD59 molecule (CD59 blood group) Homo sapiens 161-165 7524616-4 1994 Moreover, they lack surface expression of complement regulatory proteins such as DAF (CD55) and CD59, that are the most important glycosylphosphatidylinositol (GPI)-anchored membrane proteins defective in haemopoietic cells of patients with PNH. Glycosylphosphatidylinositols 130-158 CD59 molecule (CD59 blood group) Homo sapiens 96-100 7524616-4 1994 Moreover, they lack surface expression of complement regulatory proteins such as DAF (CD55) and CD59, that are the most important glycosylphosphatidylinositol (GPI)-anchored membrane proteins defective in haemopoietic cells of patients with PNH. Glycosylphosphatidylinositols 160-163 CD59 molecule (CD59 blood group) Homo sapiens 96-100 7507966-10 1994 DAF is a glycosylphosphatidylinositol-linked protein that is released from HUVEC by a phosphatidylinositol-specific phospholipase C. Although HUVEC also contain the glycosylphosphatidylinositol-anchored complement inhibitor CD59, this was not released during a 24-h incubation, suggesting that the shedding of DAF from HUVEC is not caused by PI-PLC but by other enzymes, possibly proteinases. Glycosylphosphatidylinositols 9-37 CD59 molecule (CD59 blood group) Homo sapiens 224-228 7518799-8 1994 CD59 was expressed on the U937 subline at similar levels to that on HL60 and K562 cells, was glycosylphosphatidylinositol (GPI) anchored and could be immunoprecipitated from cell extracts. Glycosylphosphatidylinositols 93-121 CD59 molecule (CD59 blood group) Homo sapiens 0-4 7518799-8 1994 CD59 was expressed on the U937 subline at similar levels to that on HL60 and K562 cells, was glycosylphosphatidylinositol (GPI) anchored and could be immunoprecipitated from cell extracts. Glycosylphosphatidylinositols 123-126 CD59 molecule (CD59 blood group) Homo sapiens 0-4 7520819-3 1994 RESULTS: CD59 was purified from human urine, retaining the N-glycan and at least some of the non-lipid component of the glycosylphosphatidylinositol membrane anchor. Glycosylphosphatidylinositols 120-148 CD59 molecule (CD59 blood group) Homo sapiens 9-13 7687899-1 1993 The membrane inhibitor of reactive lysis (MIRL) is an 18-Kd glycosyl phosphatidylinositol anchored membrane glycoprotein that inhibits the cytolytic activity of complement. Glycosylphosphatidylinositols 60-89 CD59 molecule (CD59 blood group) Homo sapiens 4-40 7694573-0 1993 Expression of the glycosylphosphatidylinositol-linked complement-inhibiting protein CD59 antigen in insect cells using a baculovirus vector. Glycosylphosphatidylinositols 18-46 CD59 molecule (CD59 blood group) Homo sapiens 84-88 7694573-1 1993 CD59 antigen (CD59) is a glycosylphosphatidylinositol (GPI)-linked membrane glycoprotein which protects human cells from complement-mediated lysis. Glycosylphosphatidylinositols 25-53 CD59 molecule (CD59 blood group) Homo sapiens 0-4 7694573-1 1993 CD59 antigen (CD59) is a glycosylphosphatidylinositol (GPI)-linked membrane glycoprotein which protects human cells from complement-mediated lysis. Glycosylphosphatidylinositols 25-53 CD59 molecule (CD59 blood group) Homo sapiens 14-18 7694573-1 1993 CD59 antigen (CD59) is a glycosylphosphatidylinositol (GPI)-linked membrane glycoprotein which protects human cells from complement-mediated lysis. Glycosylphosphatidylinositols 55-58 CD59 molecule (CD59 blood group) Homo sapiens 0-4 7694573-1 1993 CD59 antigen (CD59) is a glycosylphosphatidylinositol (GPI)-linked membrane glycoprotein which protects human cells from complement-mediated lysis. Glycosylphosphatidylinositols 55-58 CD59 molecule (CD59 blood group) Homo sapiens 14-18 8276756-0 1993 Determination of carboxyl-terminal residue and disulfide bonds of MACIF (CD59), a glycosyl-phosphatidylinositol-anchored membrane protein. Glycosylphosphatidylinositols 82-111 CD59 molecule (CD59 blood group) Homo sapiens 66-71 8276756-0 1993 Determination of carboxyl-terminal residue and disulfide bonds of MACIF (CD59), a glycosyl-phosphatidylinositol-anchored membrane protein. Glycosylphosphatidylinositols 82-111 CD59 molecule (CD59 blood group) Homo sapiens 73-77 8276756-1 1993 MACIF (CD59) is a glycosyl-phosphatidylinositol (GPI)-anchored membrane glycoprotein which inhibits the formation of membrane attack complex of human complement. Glycosylphosphatidylinositols 18-47 CD59 molecule (CD59 blood group) Homo sapiens 0-5 8276756-1 1993 MACIF (CD59) is a glycosyl-phosphatidylinositol (GPI)-anchored membrane glycoprotein which inhibits the formation of membrane attack complex of human complement. Glycosylphosphatidylinositols 18-47 CD59 molecule (CD59 blood group) Homo sapiens 7-11 8276756-1 1993 MACIF (CD59) is a glycosyl-phosphatidylinositol (GPI)-anchored membrane glycoprotein which inhibits the formation of membrane attack complex of human complement. Glycosylphosphatidylinositols 49-52 CD59 molecule (CD59 blood group) Homo sapiens 0-5 8276756-1 1993 MACIF (CD59) is a glycosyl-phosphatidylinositol (GPI)-anchored membrane glycoprotein which inhibits the formation of membrane attack complex of human complement. Glycosylphosphatidylinositols 49-52 CD59 molecule (CD59 blood group) Homo sapiens 7-11 7687899-1 1993 The membrane inhibitor of reactive lysis (MIRL) is an 18-Kd glycosyl phosphatidylinositol anchored membrane glycoprotein that inhibits the cytolytic activity of complement. Glycosylphosphatidylinositols 60-89 CD59 molecule (CD59 blood group) Homo sapiens 42-46 7688416-5 1993 Decay accelerating factor (DAF, CD55) and the membrane attack complex (MAC) inhibitor (CD59) are two cell proteins whose sole function is to protect cells from the action of complement, the former affecting the earlier components of the complement cascade, and the latter the terminal ones; both are bound to the cell surface via a glycosylphosphatidylinositol link. Glycosylphosphatidylinositols 345-373 CD59 molecule (CD59 blood group) Homo sapiens 100-104 1382093-1 1992 A significant fraction of human glycosyl-phosphatidylinositol-anchored Ag CD59, CD55, CD48, and CDw52 is present in several cell lines tested (HPB-ALL, Jurkat, HL-60, Raji) in very large noncovalent complexes relatively resistant to dissociation by detergents. Glycosylphosphatidylinositols 32-61 CD59 molecule (CD59 blood group) Homo sapiens 74-78 7683035-3 1993 Like purified E CD59, SP CD59 also possesses a glycosyl phosphatidyl inositol (GPI) anchor and incorporates into the membranes of heterologous cells where it inhibits lysis by the human MAC. Glycosylphosphatidylinositols 47-77 CD59 molecule (CD59 blood group) Homo sapiens 25-29 7683035-3 1993 Like purified E CD59, SP CD59 also possesses a glycosyl phosphatidyl inositol (GPI) anchor and incorporates into the membranes of heterologous cells where it inhibits lysis by the human MAC. Glycosylphosphatidylinositols 79-82 CD59 molecule (CD59 blood group) Homo sapiens 25-29 7681703-8 1993 In conclusion, it appears that the expression of glycosylphosphatidylinositol-linked membrane proteins by leukemic cells was heterogeneous and discordant in our patient, and that the leukemic cells were derived from the PNH clone because of their deficiency of CD59/MACIF. Glycosylphosphatidylinositols 49-77 CD59 molecule (CD59 blood group) Homo sapiens 266-271 1372164-6 1992 Platelet CD59 antigen is anchored to the membrane via a glycosyl-phosphatidylinositol link, and consequently it is suggested that deficiency of this protein might be responsible for the increased thrombotic tendency observed in paroxysmal nocturnal haemoglobinuria. Glycosylphosphatidylinositols 56-85 CD59 molecule (CD59 blood group) Homo sapiens 9-13 1383132-4 1992 CD59 Ag on HAEC is similar in size to the erythrocyte protein and is anchored via glycosyl phosphatidylinositol. Glycosylphosphatidylinositols 82-111 CD59 molecule (CD59 blood group) Homo sapiens 0-4 1378024-2 1992 The cDNA of HRF20 was transfected into Chinese hamster ovary (CHO) cells resulting in expression of human HRF20 protein on the cell surface anchored via glycosylphosphatidyl inositol. Glycosylphosphatidylinositols 153-182 CD59 molecule (CD59 blood group) Homo sapiens 12-17 1378024-2 1992 The cDNA of HRF20 was transfected into Chinese hamster ovary (CHO) cells resulting in expression of human HRF20 protein on the cell surface anchored via glycosylphosphatidyl inositol. Glycosylphosphatidylinositols 153-182 CD59 molecule (CD59 blood group) Homo sapiens 106-111 1374058-1 1992 CD59 is a widely expressed cell surface glycosylphosphatidylinositol (GPI)-linked glycoprotein which acts as an inhibitor of the assembly of the membrane attack complex of autologous complement. Glycosylphosphatidylinositols 40-68 CD59 molecule (CD59 blood group) Homo sapiens 0-4 1688497-7 1990 These studies show that the effects of PIPLC on MIRL are similar to those observed for other human erythrocyte membrane proteins that are anchored by a glycosyl phosphatidylinositol moiety. Glycosylphosphatidylinositols 152-181 CD59 molecule (CD59 blood group) Homo sapiens 48-52 1370313-8 1992 Inab E expressed a normal amount of membrane inhibitor of reactive lysis (MIRL, CD59), a glycosyl phosphatidylinositol anchored protein that is also deficient in PNH. Glycosylphosphatidylinositols 89-118 CD59 molecule (CD59 blood group) Homo sapiens 80-84 1715364-1 1991 mAb against human glycosyl-phosphatidylinositol-linked leucocyte surface Ag CD59 and CD55 immunoprecipitated from detergent lysates of HPB ALL cell line in addition to the respective Ag a common 80-kDa glycoprotein component and (glyco)lipids. Glycosylphosphatidylinositols 18-47 CD59 molecule (CD59 blood group) Homo sapiens 76-80 2606909-5 1989 The carboxy-terminal sequence confirmed that MACIF is a glycosylphosphatidylinositol (GPI)-anchored protein. Glycosylphosphatidylinositols 56-84 CD59 molecule (CD59 blood group) Homo sapiens 45-50 2606909-5 1989 The carboxy-terminal sequence confirmed that MACIF is a glycosylphosphatidylinositol (GPI)-anchored protein. Glycosylphosphatidylinositols 86-89 CD59 molecule (CD59 blood group) Homo sapiens 45-50 31886324-7 2020 LL-37 co-stained with integrin alpha3, tetraspanin CD9, GPI-linked CD59 and costimulatory molecule CD276 (B7-H3) in these vesicles. Glycosylphosphatidylinositols 56-59 CD59 molecule (CD59 blood group) Homo sapiens 67-71 29541246-1 2018 Cluster of differentiation 59 (CD59) is a glycosylphosphatidylinositol-anchored protein. Glycosylphosphatidylinositols 42-70 CD59 molecule (CD59 blood group) Homo sapiens 31-35 30032750-1 2018 CD59 and decay-accelerating factor (DAF) are glycosylphosphatidylinositol (GPI)-anchored complement regulatory proteins critical for regulating complement activation on the host cell surface. Glycosylphosphatidylinositols 45-73 CD59 molecule (CD59 blood group) Homo sapiens 0-4 30032750-1 2018 CD59 and decay-accelerating factor (DAF) are glycosylphosphatidylinositol (GPI)-anchored complement regulatory proteins critical for regulating complement activation on the host cell surface. Glycosylphosphatidylinositols 75-78 CD59 molecule (CD59 blood group) Homo sapiens 0-4 30032754-2 2018 Its pathology is driven by chronic complement dysregulation resulting from the lack of the glycosyl phosphatidyl inositol-linked regulators DAF and CD59 on susceptible erythrocytes. Glycosylphosphatidylinositols 91-121 CD59 molecule (CD59 blood group) Homo sapiens 148-152 30193519-3 2018 A molecular basis of PNH is a somatic mutation of PIGA gene causing a lack of glycosyl phosphatidyl inositol which binds many important antigens to cell surface membrane including inhibitors of activated complement CD59 and CD55 antigens. Glycosylphosphatidylinositols 78-108 CD59 molecule (CD59 blood group) Homo sapiens 215-219 29772810-4 2018 Here, we refine a previously developed micropatterning approach combined with single molecule tracking to quantify the influence of the glycosylphosphatidylinositol-anchored (GPI-anchored) protein CD59 on its molecular environment directly in the live cell plasma membrane. Glycosylphosphatidylinositols 136-164 CD59 molecule (CD59 blood group) Homo sapiens 197-201 30484243-4 2018 We performed single fluorescent-molecule imaging and revealed that ganglioside probes dynamically enter and exit rafts containing CD59, a glycosylphosphatidylinositol (GPI)-anchored protein, both before and after stimulation. Glycosylphosphatidylinositols 138-166 CD59 molecule (CD59 blood group) Homo sapiens 130-134 30484243-4 2018 We performed single fluorescent-molecule imaging and revealed that ganglioside probes dynamically enter and exit rafts containing CD59, a glycosylphosphatidylinositol (GPI)-anchored protein, both before and after stimulation. Glycosylphosphatidylinositols 168-171 CD59 molecule (CD59 blood group) Homo sapiens 130-134