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HLA-E binds to natural killer cell receptors CD94/NKG2A, B and C
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0030988540
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The human major histocompatibility complex class Ib molecule HLA-E binds signal sequence-derived peptides with primary anchor residues at positions 2 and 9
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This paper provides the first identification of peptides binding to HLA-E that derive from the leader sequence of other MHC class I molecules.
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Braud V, Jones EY, McMichael A The human major histocompatibility complex class Ib molecule HLA-E binds signal sequence-derived peptides with primary anchor residues at positions 2 and 9. Eur J Immunol. 27:1997;1164-1169. This paper provides the first identification of peptides binding to HLA-E that derive from the leader sequence of other MHC class I molecules.
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Braud, V.1
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0032524965
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HLA-E surface expression depends on binding of TAP-dependent peptides derived from certain HLA class I signal sequences
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This study reports the identification of MHC leader peptides bound to HLA-E. Cell surface expression depends on the binding of such peptides in a TAP-dependent manner.
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Structural features impose tight peptide binding specificity in the nonclassical MHC molecule HLA-E
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0031963752
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TAP- And tapasin dependent HLA-E surface expression correlates with the binding of an MHC class I leader peptide
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This is a demonstration that HLA-E surface expression depends on the binding of MHC class I leader peptides in a TAP- and tapasin-dependent way.
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Braud VM, Allan DSJ, Wilson D, McMichael AJ TAP- and tapasin dependent HLA-E surface expression correlates with the binding of an MHC class I leader peptide. Curr Biol. 8:1998;1-10. This is a demonstration that HLA-E surface expression depends on the binding of MHC class I leader peptides in a TAP- and tapasin-dependent way.
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Braud, V.M.1
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0031692643
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HLA-E-bound peptides influence recognition by inhibitory and triggering CD94/NKG2 receptors: Preferential response to an HLA-G-derived nonamer
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Llano M, Lee N, Navarro F, Garcia P, Albar JP, Geraghty DE, Lopez-Botet M HLA-E-bound peptides influence recognition by inhibitory and triggering CD94/NKG2 receptors: preferential response to an HLA-G-derived nonamer. Eur J Immunol. 28:1998;2854-2863.
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0032568520
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Murine NKg2d and CD94 are clustered within the natural killer complex and are expressed independently in natural killer cells
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Interaction of HLA-E with peptides and the peptide transporter in vitro: Implications for its function in antigen presentation
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0031093502
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b
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b and, interestingly, the MHC class I leader sequence peptide appears to be dominant.
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This paper suggests that a unique processing pathway for MHC leader sequences exists that does not involve the proteasome.
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CD94/NKG2 is the predominant inhibitory receptor involved in recognition of HLA-G by decidual and peripheral blood NK cells
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54
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55
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+ γδ T cells from the intestinal epithelium that are restricted by MICA and MICB.
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+ γδ T cells from the intestinal epithelium that are restricted by MICA and MICB.
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56
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0032478524
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Crystal structure of the hemochromatosis protein HFE and characterization of its interaction with transferrin receptor
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This paper describes the crystal structure of HFE; the paper shows that the binding groove cannot accommodate peptides or smaller molecules and that the mutations associated with hemochromatosis are likely to disrupt the folding of the molecule. A very interesting characterization of the interaction of HFE with the transferrin receptor follows; it shows that the affinity is very high at pH 7.5 but not at pH 6, consistent with a dissociation in the endosomes after endocytosis.
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Lebron JA, Bennett MJ, Vaughn DE, Chirino AJ, Snow PM, Mintier GA, Feder JN, Bjorkman PJ Crystal structure of the hemochromatosis protein HFE and characterization of its interaction with transferrin receptor. Cell. 93:1998;111-123. This paper describes the crystal structure of HFE; the paper shows that the binding groove cannot accommodate peptides or smaller molecules and that the mutations associated with hemochromatosis are likely to disrupt the folding of the molecule. A very interesting characterization of the interaction of HFE with the transferrin receptor follows; it shows that the affinity is very high at pH 7.5 but not at pH 6, consistent with a dissociation in the endosomes after endocytosis.
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Lebron, J.A.1
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57
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9344224529
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A novel MHC class I-like gene is mutated in patients with hereditary haemochromatosis
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Feder JN, Gnirke A, Thomas W, Tsuchihashi Z, Ruddy DA, Basava A, Dormishian F, Domingo R Jr., Ellis MC, Fullan Aet al. A novel MHC class I-like gene is mutated in patients with hereditary haemochromatosis. Nat Genet. 13:1996;399-408.
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Ellis, M.C.9
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58
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0001376313
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HFE gene knockout produces mouse model of hereditary hemochromatosis
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This paper confirms that lack of a functional HFE leads to disease.
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Zhou XY, Tomatsu S, Fleming RE, Parkkila S, Waheed A, Jiang J, Fei Y, Brunt EM, Ruddy DA, Prass CEet al. HFE gene knockout produces mouse model of hereditary hemochromatosis. Proc Natl Acad Sci USA. 95:1998;2492-2497. This paper confirms that lack of a functional HFE leads to disease.
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Zhou, X.Y.1
Tomatsu, S.2
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Jiang, J.6
Fei, Y.7
Brunt, E.M.8
Ruddy, D.A.9
Prass, C.E.10
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59
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0030712463
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Association of the transferrin receptor in human placenta with HFE, the protein defective in hereditary hemochromatosis
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This is the first study to report that HFE associates with the transferrin receptor.
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Parkkila S, Waheed A, Britton RS, Bacon BR, Zhou XY, Tomatsu S, Fleming RE, Sly WS Association of the transferrin receptor in human placenta with HFE, the protein defective in hereditary hemochromatosis. Proc Natl Acad Sci USA. 94:1997;13198-13202. This is the first study to report that HFE associates with the transferrin receptor.
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Proc Natl Acad Sci USA
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Parkkila, S.1
Waheed, A.2
Britton, R.S.3
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Zhou, X.Y.5
Tomatsu, S.6
Fleming, R.E.7
Sly, W.S.8
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60
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13144282684
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The hemochromatosis gene product complexes with the transferrin receptor and lowers its affinity for ligand binding
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This work demonstrates that the mutation C282Y prevents HFE from binding to the transferrin receptor whereas the mutation H63D has no such effect; however, while wild-type HFE decreases the affinity of the transferrin receptor for transferrin, H63D HFE does not. It therefore shows that the two mutations in HFE affect its function at two different levels.
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Feder JN, Penny DM, Irrinki A, Lee VK, Lebron JA, Watson N, Tsuchihashi Z, Sigal E, Bjorkman PJ, Schatzman RC The hemochromatosis gene product complexes with the transferrin receptor and lowers its affinity for ligand binding. Proc Natl Acad Sci USA. 95:1998;1472-1477. This work demonstrates that the mutation C282Y prevents HFE from binding to the transferrin receptor whereas the mutation H63D has no such effect; however, while wild-type HFE decreases the affinity of the transferrin receptor for transferrin, H63D HFE does not. It therefore shows that the two mutations in HFE affect its function at two different levels.
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Proc Natl Acad Sci USA
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Feder, J.N.1
Penny, D.M.2
Irrinki, A.3
Lee, V.K.4
Lebron, J.A.5
Watson, N.6
Tsuchihashi, Z.7
Sigal, E.8
Bjorkman, P.J.9
Schatzman, R.C.10
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61
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0032555601
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Co-trafficking of HFE, a nonclassical major histocompatibility complex class I protein, with the transferrin receptor implies a role in intracellular iron regulation
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Gross CN, Irrinki A, Feder JN, Enns CA Co-trafficking of HFE, a nonclassical major histocompatibility complex class I protein, with the transferrin receptor implies a role in intracellular iron regulation. J Biol Chem. 273:1998;22068-22074.
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J Biol Chem
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Enns, C.A.4
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62
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0031002910
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Immunohistochemistry of HLA H, the protein defective in patients with hereditary hemochromatosis, reveals unique pattern of expression in gastrointestinal tract
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Parkkila S, Waheed A, Britton RS, Feder JN, Tsuchihashi Z, Schatzman RC, Bacon BR, Sly WS Immunohistochemistry of HLA H, the protein defective in patients with hereditary hemochromatosis, reveals unique pattern of expression in gastrointestinal tract. Proc Natl Acad Sci USA. 94:1997;2534-2539.
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Proc Natl Acad Sci USA
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Parkkila, S.1
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Britton, R.S.3
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Schatzman, R.C.6
Bacon, B.R.7
Sly, W.S.8
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63
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0032427653
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Kupper cell staining by an HFE specific monoclonal antibody-implications for hereditary haemochromatosis
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in press
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Bastin JM, Jones M, O'Callaghan CA, Schimanski L, Mason DY, Townsend ARM: Kupper cell staining by an HFE specific monoclonal antibody-implications for hereditary haemochromatosis. Br J Haematol 1998, in press.
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Br J Haematol
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Bastin, J.M.1
Jones, M.2
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Schimanski, L.4
Mason, D.Y.5
Townsend, A.R.M.6
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64
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17644434333
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The hemochromatosis founder mutation in HLA-H disrupts beta2-microglobulin interaction and cell surface expression
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This paper describes the lack of trafficking of the mutated HFE (C282Y), due to a lack of association with β2 microglobulin.
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Feder JN, Tsuchihashi Z, Irrinki A, Lee VK, Mapa FA, Morikang E, Prass CE, Starnes SM, Wolff RK, Parkkila Set al. The hemochromatosis founder mutation in HLA-H disrupts beta2-microglobulin interaction and cell surface expression. J Biol Chem. 272:1997;14025-14028. This paper describes the lack of trafficking of the mutated HFE (C282Y), due to a lack of association with β2 microglobulin.
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J Biol Chem
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Feder, J.N.1
Tsuchihashi, Z.2
Irrinki, A.3
Lee, V.K.4
Mapa, F.A.5
Morikang, E.6
Prass, C.E.7
Starnes, S.M.8
Wolff, R.K.9
Parkkila, S.10
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65
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0030732164
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Hereditary hemochromatosis: Effects of C282Y and H63D mutations on association with beta2-microglobulin, intracellular processing, and cell surface expression of the HFE protein in COS-7 cells
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This paper describes the lack of trafficking of the mutated HFE (C282Y), due to a lack of association with β2 microglobulin.
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Waheed A, Parkkila S, Zhou XY, Tomatsu S, Tsuchihashi Z, Feder JN, Schatzman RC, Britton RS, Bacon BR, Sly WS Hereditary hemochromatosis: effects of C282Y and H63D mutations on association with beta2-microglobulin, intracellular processing, and cell surface expression of the HFE protein in COS-7 cells. Proc Natl Acad Sci USA. 94:1997;12384-12389. This paper describes the lack of trafficking of the mutated HFE (C282Y), due to a lack of association with β2 microglobulin.
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Proc Natl Acad Sci USA
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Waheed, A.1
Parkkila, S.2
Zhou, X.Y.3
Tomatsu, S.4
Tsuchihashi, Z.5
Feder, J.N.6
Schatzman, R.C.7
Britton, R.S.8
Bacon, B.R.9
Sly, W.S.10
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66
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0028588920
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Recognition of a lipid antigen by CD1-restricted alpha beta+ T cells
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Beckman EM, Porcelli SA, Morita CT, Behar SM, Furlong ST, Brenner MB Recognition of a lipid antigen by CD1-restricted alpha beta+ T cells. Nature. 372:1994;691-694.
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Beckman, E.M.1
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Furlong, S.T.5
Brenner, M.B.6
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67
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0028980830
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CD1-restricted T cell recognition of microbial lipoglycan antigens
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Sieling PA, Chatterjee D, Porcelli SA, Prigozy TI, Mazzaccaro RJ, Soriano T, Bloom BR, Brenner MB, Kronenberg M, Brennan PJet al. CD1-restricted T cell recognition of microbial lipoglycan antigens. Science. 269:1995;227-230.
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Sieling, P.A.1
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Soriano, T.6
Bloom, B.R.7
Brenner, M.B.8
Kronenberg, M.9
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68
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0030265731
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CD1c restricts responses of mycobacteria-specific T cells. Evidence for antigen presentation by a second member of the human CD1 family
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Beckman EM, Melian A, Behar SM, Sieling PA, Chatterjee D, Furlong ST, Matsumoto R, Rosat JP, Modlin RL, Porcelli SA CD1c restricts responses of mycobacteria-specific T cells. Evidence for antigen presentation by a second member of the human CD1 family. J Immunol. 157:1996;2795-2803.
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Beckman, E.M.1
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Behar, S.M.3
Sieling, P.A.4
Chatterjee, D.5
Furlong, S.T.6
Matsumoto, R.7
Rosat, J.P.8
Modlin, R.L.9
Porcelli, S.A.10
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69
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0030826451
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Structural requirements for glycolipid antigen recognition by CD1b-restricted T cells
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This paper describes the identification of another group of lipid antigens bound to CD1b. It shows that variations in the lipid tails do not significantly affect T cell recognition, suggesting that they are buried in the binding groove of CD1. Variations in the carbohydrate groups, however, affect T cell recognition - consistent with a direct contact with the TCR.
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Moody DB, Reinhold BB, Guy MR, Beckman EM, Frederique DE, Furlong ST, Ye S, Reinhold VN, Sieling PA, Modlin RLet al. Structural requirements for glycolipid antigen recognition by CD1b-restricted T cells. Science. 278:1997;283-286. This paper describes the identification of another group of lipid antigens bound to CD1b. It shows that variations in the lipid tails do not significantly affect T cell recognition, suggesting that they are buried in the binding groove of CD1. Variations in the carbohydrate groups, however, affect T cell recognition - consistent with a direct contact with the TCR.
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Science
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Moody, D.B.1
Reinhold, B.B.2
Guy, M.R.3
Beckman, E.M.4
Frederique, D.E.5
Furlong, S.T.6
Ye, S.7
Reinhold, V.N.8
Sieling, P.A.9
Modlin, R.L.10
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70
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0032033389
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Molecular interaction of CD1b with lipoglycan antigens
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This reports the characterization of the kinetics of binding of CD1b to lipid antigens. CD1b binds with high affinity and the binding is optimal at acidic pH, consistent with the colocalization of CD1b and lipid antigens in endosomes.
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Ernst WA, Maher J, Cho S, Niazi KR, Chatterjee D, Moody DB, Besra GS, Watanabe Y, Jensen PE, Porcelli SAet al. Molecular interaction of CD1b with lipoglycan antigens. Immunity. 8:1998;331-340. This reports the characterization of the kinetics of binding of CD1b to lipid antigens. CD1b binds with high affinity and the binding is optimal at acidic pH, consistent with the colocalization of CD1b and lipid antigens in endosomes.
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(1998)
Immunity
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Ernst, W.A.1
Maher, J.2
Cho, S.3
Niazi, K.R.4
Chatterjee, D.5
Moody, D.B.6
Besra, G.S.7
Watanabe, Y.8
Jensen, P.E.9
Porcelli, S.A.10
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71
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0030826423
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Crystal structure of mouse CD1: An MHC-like fold with a large hydrophobic binding groove
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Here, the crystal structure of mouse CD1d reveals a narrower and deeper binding groove which is highly hydrophobic. This is consistent with the binding of lipid antigens.
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Zeng Z, Castano AR, Segelke BW, Stura EA, Peterson PA, Wilson IA Crystal structure of mouse CD1: an MHC-like fold with a large hydrophobic binding groove. Science. 277:1997;339-345. Here, the crystal structure of mouse CD1d reveals a narrower and deeper binding groove which is highly hydrophobic. This is consistent with the binding of lipid antigens.
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Science
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Zeng, Z.1
Castano, A.R.2
Segelke, B.W.3
Stura, E.A.4
Peterson, P.A.5
Wilson, I.A.6
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72
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0032033694
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The tyrosine-containing cytoplasmic tail of CD1b is essential for its efficient presentation of bacterial lipid antigens
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This paper demonstrates that CD1b is targeted to endosomal compartments by signals present in its cytoplasmic tail. Lipid antigens colocalize in these compartments.
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Jackman RM, Stenger S, Lee A, Moody DB, Rogers RA, Niazi KR, Sugita M, Modlin RL, Peters PJ, Porcelli SA The tyrosine-containing cytoplasmic tail of CD1b is essential for its efficient presentation of bacterial lipid antigens. Immunity. 8:1998;341-351. This paper demonstrates that CD1b is targeted to endosomal compartments by signals present in its cytoplasmic tail. Lipid antigens colocalize in these compartments.
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Immunity
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Jackman, R.M.1
Stenger, S.2
Lee, A.3
Moody, D.B.4
Rogers, R.A.5
Niazi, K.R.6
Sugita, M.7
Modlin, R.L.8
Peters, P.J.9
Porcelli, S.A.10
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73
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0030907414
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The mannose receptor delivers lipoglycan antigens to endosomes for presentation to T cells by CD1b molecules
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This study demonstrates that lipid antigens colocalize with CD1b in endosomal compartments and that the mannose receptor can be involved in this process.
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Prigozy TI, Sieling PA, Clemens D, Stewart PL, Behar SM, Porcelli SA, Brenner MB, Modlin RL, Kronenberg M The mannose receptor delivers lipoglycan antigens to endosomes for presentation to T cells by CD1b molecules. Immunity. 6:1997;187-197. This study demonstrates that lipid antigens colocalize with CD1b in endosomal compartments and that the mannose receptor can be involved in this process.
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Immunity
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Prigozy, T.I.1
Sieling, P.A.2
Clemens, D.3
Stewart, P.L.4
Behar, S.M.5
Porcelli, S.A.6
Brenner, M.B.7
Modlin, R.L.8
Kronenberg, M.9
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74
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0030765980
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Differential effects of cytolytic T cell subsets on intracellular infection
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+ T cells which kill infected macrophages and the bacteria via a granule-dependent mechanism.
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+ T cells which kill infected macrophages and the bacteria via a granule-dependent mechanism.
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Science
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Stenger, S.1
Mazzaccaro, R.J.2
Uyemura, K.3
Cho, S.4
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Rosat, J.P.6
Sette, A.7
Brenner, M.B.8
Porcelli, S.A.9
Bloom, B.R.10
Modlin, R.L.11
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75
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CD1d-restricted and TCR-mediated activation of Valpha14 NKT cells by glycosylceramides
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Kawano, T.1
Cui, J.2
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Sato, H.9
Kondo, E.10
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76
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0032193207
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Selective ability of mouse CD1 to present glycolipids: Α-galactosylceramide specifically stimulates Vα14+NK T lymphocytes
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Burdin N, Brossay L, Koezuka Y, Smiley ST, Grusby MJ, Gui M, Taniguchi M, Hayakawa K, Kronenberg M Selective ability of mouse CD1 to present glycolipids: α-galactosylceramide specifically stimulates Vα14+NK T lymphocytes. J Immunol. 161:1998;3271-3281.
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Burdin, N.1
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Hayakawa, K.8
Kronenberg, M.9
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77
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0032489652
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Natural ligand of mouse CD1d1: Cellular glycosylphosphatidylinositol
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