메뉴 건너뛰기




Volumn 100, Issue 1-3, 2002, Pages 555-575

Transmembrane domains in the functions of Fc receptors

Author keywords

Bioinformatics; Integral membrane protein; Helix association

Indexed keywords

AMINO ACID; FC RECEPTOR; MEMBRANE PROTEIN;

EID: 0037438624     PISSN: 03014622     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0301-4622(02)00306-X     Document Type: Article
Times cited : (25)

References (106)
  • 1
    • 0024461745 scopus 로고
    • Protein oligomerization in the endoplasmic reticulum
    • Hurtley S.M., Helenius A. Protein oligomerization in the endoplasmic reticulum. Annu. Rev. Cell Biol. 2:1989;277-307.
    • (1989) Annu. Rev. Cell Biol. , vol.2 , pp. 277-307
    • Hurtley, S.M.1    Helenius, A.2
  • 2
    • 0018987976 scopus 로고
    • Intracellular protein topogenesis
    • Blobel G. Intracellular protein topogenesis. Proc. Natl. Acad. Sci. USA. 77:1980;1496-1500.
    • (1980) Proc. Natl. Acad. Sci. USA , vol.77 , pp. 1496-1500
    • Blobel, G.1
  • 3
    • 0028865843 scopus 로고
    • 3D domain swapping: A mechanism for oligomer assembly
    • Bennett M.J., Schlunegger M.P., Eisenberg D. 3D domain swapping: a mechanism for oligomer assembly. Prot. Sci. 5:1995;2455-2468.
    • (1995) Prot. Sci. , vol.5 , pp. 2455-2468
    • Bennett, M.J.1    Schlunegger, M.P.2    Eisenberg, D.3
  • 4
    • 0020475449 scopus 로고
    • A simple method for displaying the hydropathic character of a protein
    • Kyte J., Doolittle R.F. A simple method for displaying the hydropathic character of a protein. J. Mol. Biol. 157:1982;105-132.
    • (1982) J. Mol. Biol. , vol.157 , pp. 105-132
    • Kyte, J.1    Doolittle, R.F.2
  • 5
    • 0032403254 scopus 로고    scopus 로고
    • Role of transmembrane domains in the functions of B- and T-cell receptors
    • Zidovetzki R., Rost B., Pecht I. Role of transmembrane domains in the functions of B- and T-cell receptors. Immunol. Lett. 64:1998;97-107.
    • (1998) Immunol. Lett. , vol.64 , pp. 97-107
    • Zidovetzki, R.1    Rost, B.2    Pecht, I.3
  • 6
    • 0026540751 scopus 로고
    • Multichain immune recognition receptors: Similarities in structure and signaling pathways
    • Keegan A.D., Paul W.E. Multichain immune recognition receptors: similarities in structure and signaling pathways. Immunol. Today. 13:1992;63-68.
    • (1992) Immunol. Today , vol.13 , pp. 63-68
    • Keegan, A.D.1    Paul, W.E.2
  • 7
    • 0029893331 scopus 로고    scopus 로고
    • Fc gamma RII-mediated regulation of human B cells
    • Gergely J., Sarmay G. Fc gamma RII-mediated regulation of human B cells. Scand. J. Immunol. 44:1996;1-10.
    • (1996) Scand. J. Immunol. , vol.44 , pp. 1-10
    • Gergely, J.1    Sarmay, G.2
  • 8
    • 0030566715 scopus 로고    scopus 로고
    • Integration of activatory and inhibitory signals in human B-cells
    • Sarmay G., Koncz G., Gergely J. Integration of activatory and inhibitory signals in human B-cells. Immunol. Lett. 54:1996;93-100.
    • (1996) Immunol. Lett. , vol.54 , pp. 93-100
    • Sarmay, G.1    Koncz, G.2    Gergely, J.3
  • 9
    • 0030929805 scopus 로고    scopus 로고
    • Fc receptor biology
    • Daeron M. Fc receptor biology. Annu. Rev. Immunol. 15:1997;203-234.
    • (1997) Annu. Rev. Immunol. , vol.15 , pp. 203-234
    • Daeron, M.1
  • 10
    • 0033430995 scopus 로고    scopus 로고
    • Fc receptor signaling and trafficking: A connection for antigen processing
    • Amigorena S., Bonnerot C. Fc receptor signaling and trafficking: a connection for antigen processing. Immunol. Rev. 172:1999;279-284.
    • (1999) Immunol. Rev. , vol.172 , pp. 279-284
    • Amigorena, S.1    Bonnerot, C.2
  • 11
    • 0027330896 scopus 로고
    • Association of all three types of Fc gamma R (CD64, CD32 and CD16) with a gamma-chain homodimer in cultured human monocytes
    • Masuda M., Roos D. Association of all three types of Fc gamma R (CD64, CD32 and CD16) with a gamma-chain homodimer in cultured human monocytes. J. Immunol. 151:1993;7188-7195.
    • (1993) J. Immunol. , vol.151 , pp. 7188-7195
    • Masuda, M.1    Roos, D.2
  • 12
    • 0000722327 scopus 로고
    • New nomenclature for the Reth motif (or ARH1/TAM/ARAM/YXXL)
    • Cambier J.C. New nomenclature for the Reth motif (or ARH1/TAM/ARAM/YXXL). Immunol. Today. 16:1995;110.
    • (1995) Immunol. Today , vol.16 , pp. 110
    • Cambier, J.C.1
  • 13
    • 0028130057 scopus 로고
    • Fc receptors: Rubor redux
    • Ravetch J.V. Fc receptors: rubor redux. Cell. 78:(4):1994;553-560.
    • (1994) Cell , vol.78 , Issue.4 , pp. 553-560
    • Ravetch, J.V.1
  • 14
    • 0029597781 scopus 로고
    • Functional association between the human myeloid immunoglobulin A Fc receptor (CD89) and FcR gamma chain. Molecular basis for CD89/FcR gamma chain association
    • Morton H.C., van den Herik-Oudijk I.E., Vossebeld P. Functional association between the human myeloid immunoglobulin A Fc receptor (CD89) and FcR gamma chain. Molecular basis for CD89/FcR gamma chain association. J. Biol. Chem. 270:1995;29781-29787.
    • (1995) J. Biol. Chem. , vol.270 , pp. 29781-29787
    • Morton, H.C.1    Van den Herik-Oudijk, I.E.2    Vossebeld, P.3
  • 16
    • 0028672732 scopus 로고
    • Molecular basis of Fc receptor function
    • Hulett M.D., Hogarth P.M. Molecular basis of Fc receptor function. Adv. Immunol. 57:1994;1-127.
    • (1994) Adv. Immunol. , vol.57 , pp. 1-127
    • Hulett, M.D.1    Hogarth, P.M.2
  • 18
    • 0026716643 scopus 로고
    • Membrane protein structure prediction. Hydrophobicity analysis and the positive-inside rule
    • von Heijne G. Membrane protein structure prediction. Hydrophobicity analysis and the positive-inside rule. J. Mol. Biol. 225:1992;487-494.
    • (1992) J. Mol. Biol. , vol.225 , pp. 487-494
    • Von Heijne, G.1
  • 20
    • 0029902780 scopus 로고    scopus 로고
    • Bridging the protein sequence-structure gap by structure predictions
    • Rost B., Sander C. Bridging the protein sequence-structure gap by structure predictions. Annu. Rev. Biophys. Biomol. Struct. 25:1996;113-136.
    • (1996) Annu. Rev. Biophys. Biomol. Struct. , vol.25 , pp. 113-136
    • Rost, B.1    Sander, C.2
  • 21
    • 0030038634 scopus 로고    scopus 로고
    • Topology prediction for helical transmembrane proteins at 86% accuracy
    • Rost B., Fariselli P., Casadio R. Topology prediction for helical transmembrane proteins at 86% accuracy. Protein Sci. 5:1996;1704-1718.
    • (1996) Protein Sci. , vol.5 , pp. 1704-1718
    • Rost, B.1    Fariselli, P.2    Casadio, R.3
  • 22
    • 0031307343 scopus 로고    scopus 로고
    • Better 1D predictions by experts with machines
    • Rost B. Better 1D predictions by experts with machines. Proteins Suppl. 1:1997;192-197.
    • (1997) Proteins Suppl. , vol.1 , pp. 192-197
    • Rost, B.1
  • 24
    • 0014062165 scopus 로고
    • Use of helical wheels to represent the structures of proteins and to identify segments with helical potential
    • Schiffer M., Edmundson A.B. Use of helical wheels to represent the structures of proteins and to identify segments with helical potential. Biophys. J. 7:1967;121-135.
    • (1967) Biophys. J. , vol.7 , pp. 121-135
    • Schiffer, M.1    Edmundson, A.B.2
  • 26
    • 0029738872 scopus 로고    scopus 로고
    • Experimentally determined hydrophobicity scale for proteins at membrane interfaces
    • Wimley W.C., White S.H. Experimentally determined hydrophobicity scale for proteins at membrane interfaces. Nat. Struct. Biol. 3:1996;842-848.
    • (1996) Nat. Struct. Biol. , vol.3 , pp. 842-848
    • Wimley, W.C.1    White, S.H.2
  • 27
    • 0024491621 scopus 로고
    • Complete structure and expression in transfected cells of high affinity IgE receptor
    • Blank U., Ra C., Miller L., White K., Metzger H., Kinet J.P. Complete structure and expression in transfected cells of high affinity IgE receptor. Nature. 337:1989;187-189.
    • (1989) Nature , vol.337 , pp. 187-189
    • Blank, U.1    Ra, C.2    Miller, L.3    White, K.4    Metzger, H.5    Kinet, J.P.6
  • 28
    • 0022366834 scopus 로고
    • Identification of the components of the murine T cell antigen receptor complex
    • Samelson L.E., Harford J.B., Klausner R.D. Identification of the components of the murine T cell antigen receptor complex. Cell. 43:1985;223-231.
    • (1985) Cell , vol.43 , pp. 223-231
    • Samelson, L.E.1    Harford, J.B.2    Klausner, R.D.3
  • 29
    • 0025012782 scopus 로고
    • A peptide sequence confers retention and rapid degradation in the endoplasmic reticulum
    • Bonifacino J.S., Suzuki C.K., Klausner R.D. A peptide sequence confers retention and rapid degradation in the endoplasmic reticulum. Science. 247:1990;79-82.
    • (1990) Science , vol.247 , pp. 79-82
    • Bonifacino, J.S.1    Suzuki, C.K.2    Klausner, R.D.3
  • 30
    • 0025114865 scopus 로고
    • Colocalized transmembrane determinants for ER degradation and subunit assembly explain the intracellular fate of TCR chains
    • Bonifacino J.S., Cosson P., Klausner R.D. Colocalized transmembrane determinants for ER degradation and subunit assembly explain the intracellular fate of TCR chains. Cell. 63:(1990):1990;503-513.
    • (1990) Cell , vol.63 , Issue.1990 , pp. 503-513
    • Bonifacino, J.S.1    Cosson, P.2    Klausner, R.D.3
  • 31
    • 0023902867 scopus 로고
    • Characterization of the human monocyte high affinity Fc receptor (hu FcRI)
    • Peltz G., Frederick K., Anderson C.L., Peterlin B.M. Characterization of the human monocyte high affinity Fc receptor (hu FcRI). Mol. Immunol. 25:1988;243-250.
    • (1988) Mol. Immunol. , vol.25 , pp. 243-250
    • Peltz, G.1    Frederick, K.2    Anderson, C.L.3    Peterlin, B.M.4
  • 32
    • 0031646641 scopus 로고    scopus 로고
    • Molecular characterization of six variant Fcgamma receptor class I (CD64) transcripts
    • Ernst L.K., Duchemin A.M., Miller K.L., Anderson C.L. Molecular characterization of six variant Fcgamma receptor class I (CD64) transcripts. Mol. Immunol. 35:1998;943-954.
    • (1998) Mol. Immunol. , vol.35 , pp. 943-954
    • Ernst, L.K.1    Duchemin, A.M.2    Miller, K.L.3    Anderson, C.L.4
  • 33
    • 0025186626 scopus 로고
    • Molecular cloning and expression of the mouse high affinity Fc receptor for IgG
    • Sears D.W., Osman N., Tate B., McKenzie I.F., Hogarth P.M. Molecular cloning and expression of the mouse high affinity Fc receptor for IgG. J. Immunol. 144:1990;371-378.
    • (1990) J. Immunol. , vol.144 , pp. 371-378
    • Sears, D.W.1    Osman, N.2    Tate, B.3    McKenzie, I.F.4    Hogarth, P.M.5
  • 34
    • 0024980981 scopus 로고
    • Antigen receptor tail clue
    • Reth M. Antigen receptor tail clue. Nature. 338:1989;383-384.
    • (1989) Nature , vol.338 , pp. 383-384
    • Reth, M.1
  • 35
    • 0024531803 scopus 로고
    • Isolation and expression of functional high-affinity Fc receptor complementary DNAs
    • Allen J.M., Seed B. Isolation and expression of functional high-affinity Fc receptor complementary DNAs. Science. 243:1989;378-381.
    • (1989) Science , vol.243 , pp. 378-381
    • Allen, J.M.1    Seed, B.2
  • 36
    • 0027180653 scopus 로고
    • Association of the high-affinity receptor for IgG (Fc gamma RI) with the gamma subunit of the IgE receptor
    • Ernst L.K., Duchemin A.M., Anderson C.L. Association of the high-affinity receptor for IgG (Fc gamma RI) with the gamma subunit of the IgE receptor. Proc. Natl. Acad. Sci. USA. 90:1993;6023-6027.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 6023-6027
    • Ernst, L.K.1    Duchemin, A.M.2    Anderson, C.L.3
  • 37
    • 0029953055 scopus 로고    scopus 로고
    • A novel role for the Fc receptor gamma subunit: Enhancement of Fc gamma R ligand affinity
    • Miller K.L., Duchemin A.M., Anderson C.L. A novel role for the Fc receptor gamma subunit: enhancement of Fc gamma R ligand affinity. J. Exp. Med. 183:1996;2227-2233.
    • (1996) J. Exp. Med. , vol.183 , pp. 2227-2233
    • Miller, K.L.1    Duchemin, A.M.2    Anderson, C.L.3
  • 38
    • 0029383784 scopus 로고
    • The interaction between human Fc gamma RI and the gamma-chain is mediated solely via the 21 amino acid transmembrane domain of Fc gamma RI
    • Harrison P.T., Bjorkhaug L., Hutchinson M.J., Allen J.M. The interaction between human Fc gamma RI and the gamma-chain is mediated solely via the 21 amino acid transmembrane domain of Fc gamma RI. Mol. Membr. Biol. 12:1995;309-312.
    • (1995) Mol. Membr. Biol. , vol.12 , pp. 309-312
    • Harrison, P.T.1    Bjorkhaug, L.2    Hutchinson, M.J.3    Allen, J.M.4
  • 39
    • 0028984029 scopus 로고
    • Two distinct regions in theFcγRI initiate distinct signaling pathways involved in endocytosis and phagocytosis
    • Davis W., Harrison P.T., Hutchinson M.J., Allen J.M. Two distinct regions in theFcγRI initiate distinct signaling pathways involved in endocytosis and phagocytosis. EMBO J. 14:1995;432-441.
    • (1995) EMBO J. , vol.14 , pp. 432-441
    • Davis, W.1    Harrison, P.T.2    Hutchinson, M.J.3    Allen, J.M.4
  • 40
    • 0026592447 scopus 로고
    • Structure and mapping of the gene encoding mouse high affinity Fc gamma RI and chromosomal location of the human Fc gamma RI gene
    • Osman N., Kozak C.A., McKenzie I.F., Hogarth P.M. Structure and mapping of the gene encoding mouse high affinity Fc gamma RI and chromosomal location of the human Fc gamma RI gene. J. Immunol. 148:1992;1570-1575.
    • (1992) J. Immunol. , vol.148 , pp. 1570-1575
    • Osman, N.1    Kozak, C.A.2    McKenzie, I.F.3    Hogarth, P.M.4
  • 41
    • 0027245603 scopus 로고
    • Linkage on chromosome 3 of autoimmune diabetes and defective Fc receptor for IgG in NOD mice
    • Prins J.B., Todd J.A., Rodrigues N.R., et al. Linkage on chromosome 3 of autoimmune diabetes and defective Fc receptor for IgG in NOD mice. Science. 260:1993;695-698.
    • (1993) Science , vol.260 , pp. 695-698
    • Prins, J.B.1    Todd, J.A.2    Rodrigues, N.R.3
  • 42
    • 0034152220 scopus 로고    scopus 로고
    • Mouse FcgammaRI: Identification and functional characterization of five new alleles
    • Gavin A.L., Leiter E.H., Hogarth P.M. Mouse FcgammaRI: identification and functional characterization of five new alleles. Immunogenetics. 51:2000;206-211.
    • (2000) Immunogenetics , vol.51 , pp. 206-211
    • Gavin, A.L.1    Leiter, E.H.2    Hogarth, P.M.3
  • 44
    • 0019934717 scopus 로고
    • The helical hydrophobic moment: A measure of the amphiphilicity of a helix
    • Eisenberg D., Weiss R.M., Terwilliger T.C. The helical hydrophobic moment: a measure of the amphiphilicity of a helix. Nature. 299:1982;371-374.
    • (1982) Nature , vol.299 , pp. 371-374
    • Eisenberg, D.1    Weiss, R.M.2    Terwilliger, T.C.3
  • 45
    • 0024342834 scopus 로고
    • Alternative membrane forms of Fc gamma RIII(CD16) on human natural killer cells and neutrophils. Cell type-specific expression of two genes that differ in single nucleotide substitutions
    • Ravetch J.V., Perussia B. Alternative membrane forms of Fc gamma RIII(CD16) on human natural killer cells and neutrophils. Cell type-specific expression of two genes that differ in single nucleotide substitutions. J. Exp. Med. 170:1989;481-497.
    • (1989) J. Exp. Med. , vol.170 , pp. 481-497
    • Ravetch, J.V.1    Perussia, B.2
  • 46
    • 0024151595 scopus 로고
    • Structure and function of Fc receptors on macrophages and lymphocytes
    • Mellman I., Koch T., Healey G., et al. Structure and function of Fc receptors on macrophages and lymphocytes. J. Cell. Sci. Suppl. 9:1988;45-65.
    • (1988) J. Cell. Sci. Suppl. , vol.9 , pp. 45-65
    • Mellman, I.1    Koch, T.2    Healey, G.3
  • 47
    • 0024460749 scopus 로고
    • A macrophage Fc gamma receptor and the mast cell receptor for IgE share an identical subunit
    • Ra C., Jouvin M.H., Blank U., Kinet J.P. A macrophage Fc gamma receptor and the mast cell receptor for IgE share an identical subunit. Nature. 341:1989;752-754.
    • (1989) Nature , vol.341 , pp. 752-754
    • Ra, C.1    Jouvin, M.H.2    Blank, U.3    Kinet, J.P.4
  • 49
    • 0024811801 scopus 로고
    • A single amino acid in the glycosyl phosphatidylinositol attachment domain determines the membrane topology of Fc gamma RIII
    • Kurosaki T., Ravetch J.V. A single amino acid in the glycosyl phosphatidylinositol attachment domain determines the membrane topology of Fc gamma RIII. Nature. 342:1989;805-807.
    • (1989) Nature , vol.342 , pp. 805-807
    • Kurosaki, T.1    Ravetch, J.V.2
  • 50
    • 0026525967 scopus 로고
    • Signal transduction by Fc gamma RIII (CD16) is mediated through the gamma chain
    • Wirthmueller U., Kurosaki T., Murakami M.S., Ravetch J.V. Signal transduction by Fc gamma RIII (CD16) is mediated through the gamma chain. J. Exp. Med. 175:1992;1381-1390.
    • (1992) J. Exp. Med. , vol.175 , pp. 1381-1390
    • Wirthmueller, U.1    Kurosaki, T.2    Murakami, M.S.3    Ravetch, J.V.4
  • 51
    • 0025237245 scopus 로고
    • Fc gamma receptor type III (CD16) is included in the zeta NK receptor complex expressed by human natural killer cells
    • Anderson P., Caligiuri M., O Brien C., Manley T., Ritz J., Schlossman S.F. Fc gamma receptor type III (CD16) is included in the zeta NK receptor complex expressed by human natural killer cells. Proc. Natl. Acad. Sci. USA. 87:1990;2274-2278.
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 2274-2278
    • Anderson, P.1    Caligiuri, M.2    O Brien, C.3    Manley, T.4    Ritz, J.5    Schlossman, S.F.6
  • 52
    • 0026542308 scopus 로고
    • The beta subunit of the Fc epsilon RI is associated with the Fc gamma RIII on mast cells
    • Kurosaki T., Gander I., Wirthmueller U., Ravetch J.V. The beta subunit of the Fc epsilon RI is associated with the Fc gamma RIII on mast cells. J. Exp. Med. 175:1992;447-451.
    • (1992) J. Exp. Med. , vol.175 , pp. 447-451
    • Kurosaki, T.1    Gander, I.2    Wirthmueller, U.3    Ravetch, J.V.4
  • 53
    • 0025735616 scopus 로고
    • A subunit common to an IgG Fc receptor and the T-cell receptor mediates assembly through different interactions
    • Kurosaki T., Gander I., Ravetch J.V. A subunit common to an IgG Fc receptor and the T-cell receptor mediates assembly through different interactions. Proc. Natl. Acad. Sci. USA. 88:1991;3837-3841.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 3837-3841
    • Kurosaki, T.1    Gander, I.2    Ravetch, J.V.3
  • 54
    • 0026082601 scopus 로고
    • Analysis of Fc gamma RIII (CD16) membrane expression and association with CD3 zeta and Fc epsilon RI-gamma by site-directed mutation
    • Lanier L.L., Yu G., Phillips J.H. Analysis of Fc gamma RIII (CD16) membrane expression and association with CD3 zeta and Fc epsilon RI-gamma by site-directed mutation. J. Immunol. 146:1991;1571-1576.
    • (1991) J. Immunol. , vol.146 , pp. 1571-1576
    • Lanier, L.L.1    Yu, G.2    Phillips, J.H.3
  • 55
  • 56
    • 0027243197 scopus 로고
    • Rat class III Fc gamma receptor isoforms differ in IgG subclass-binding specificity and fail to associate productively with rat CD3 zeta
    • Farber D.L., Giorda R., Nettleton M.Y., Trucco M., Kochan J.P., Sears D.W. Rat class III Fc gamma receptor isoforms differ in IgG subclass-binding specificity and fail to associate productively with rat CD3 zeta. J. Immunol. 150:1993;4364-4375.
    • (1993) J. Immunol. , vol.150 , pp. 4364-4375
    • Farber, D.L.1    Giorda, R.2    Nettleton, M.Y.3    Trucco, M.4    Kochan, J.P.5    Sears, D.W.6
  • 57
    • 0025342380 scopus 로고
    • Reactivity of cloned, expressed human Fc gamma RIII isoforms with monoclonal antibodies which distinguish cell-type-specific and allelic forms of Fc gamma RIII
    • Trounstine M.L., Peltz G.A., Yssel H., et al. Reactivity of cloned, expressed human Fc gamma RIII isoforms with monoclonal antibodies which distinguish cell-type-specific and allelic forms of Fc gamma RIII. Int. Immunol. 2:1990;303-310.
    • (1990) Int. Immunol. , vol.2 , pp. 303-310
    • Trounstine, M.L.1    Peltz, G.A.2    Yssel, H.3
  • 59
    • 0024282589 scopus 로고
    • The Fc gamma receptor of natural killer cells is a phospholipid-linked membrane protein
    • Simmons D., Seed B. The Fc gamma receptor of natural killer cells is a phospholipid-linked membrane protein. Nature. 333:1988;568-750.
    • (1988) Nature , vol.333 , pp. 568-750
    • Simmons, D.1    Seed, B.2
  • 60
    • 0041835849 scopus 로고
    • Human Fc gamma RIII: Cloning, expression, and identification of the chromosomal locus of two Fc receptors for IgG
    • Peltz G.A., Grundy H.O., Lebo R.V., Yssel H., Barsh G.S., Moore K.W. Human Fc gamma RIII: cloning, expression, and identification of the chromosomal locus of two Fc receptors for IgG. Proc. Natl. Acad. Sci. USA. 86:1989;1013-1017.
    • (1989) Proc. Natl. Acad. Sci. USA , vol.86 , pp. 1013-1017
    • Peltz, G.A.1    Grundy, H.O.2    Lebo, R.V.3    Yssel, H.4    Barsh, G.S.5    Moore, K.W.6
  • 61
    • 0025303561 scopus 로고
    • Characterization and expression of an Fc gamma receptor cDNA cloned from rat natural killer cells
    • Zeger D.L., Hogarth P.M., Sears D.W. Characterization and expression of an Fc gamma receptor cDNA cloned from rat natural killer cells. Proc. Natl. Acad. Sci. USA. 87:1990;3425-3429.
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 3425-3429
    • Zeger, D.L.1    Hogarth, P.M.2    Sears, D.W.3
  • 63
    • 0025304685 scopus 로고
    • Cellular distribution, regulation, and biochemical nature of an Fc alpha receptor in humans
    • Monteiro R.C., Kubagawa H., Cooper M.D. Cellular distribution, regulation, and biochemical nature of an Fc alpha receptor in humans. J. Exp. Med. 171:1990;597-613.
    • (1990) J. Exp. Med. , vol.171 , pp. 597-613
    • Monteiro, R.C.1    Kubagawa, H.2    Cooper, M.D.3
  • 64
    • 0026582770 scopus 로고
    • Molecular heterogeneity of Fc alpha receptors detected by receptor-specific monoclonal antibodies
    • Monteiro R.C., Cooper M.D., Kubagawa H. Molecular heterogeneity of Fc alpha receptors detected by receptor-specific monoclonal antibodies. J. Immunol. 148:1992;1764-1770.
    • (1992) J. Immunol. , vol.148 , pp. 1764-1770
    • Monteiro, R.C.1    Cooper, M.D.2    Kubagawa, H.3
  • 65
    • 0027361087 scopus 로고
    • Definition of immunoglobulin A receptors on eosinophils and their enhanced expression in allergic individuals
    • Monteiro R.C., Hostoffer R.W., Cooper M.D., Bonner J.R., Gartland G.L., Kubagawa H. Definition of immunoglobulin A receptors on eosinophils and their enhanced expression in allergic individuals. J. Clin. Invest. 92:1993;1681-1685.
    • (1993) J. Clin. Invest. , vol.92 , pp. 1681-1685
    • Monteiro, R.C.1    Hostoffer, R.W.2    Cooper, M.D.3    Bonner, J.R.4    Gartland, G.L.5    Kubagawa, H.6
  • 66
    • 0025007135 scopus 로고
    • The structure and function of human IgA
    • Kerr M.A. The structure and function of human IgA. Biochem. J. 271:1990;285-296.
    • (1990) Biochem. J. , vol.271 , pp. 285-296
    • Kerr, M.A.1
  • 67
    • 0027053111 scopus 로고
    • Receptors for IgA on phagocytic cells
    • Shen L. Receptors for IgA on phagocytic cells. Immunol. Res. 11:1992;273-282.
    • (1992) Immunol. Res. , vol.11 , pp. 273-282
    • Shen, L.1
  • 69
    • 0030000811 scopus 로고    scopus 로고
    • Cloning and characterization of Fc alpha Rb, a novel Fc alpha receptor (CD89) isoform expressed in eosinophils and neutrophils
    • van Dijk T.B., Bracke M., Caldenhoven E., et al. Cloning and characterization of Fc alpha Rb, a novel Fc alpha receptor (CD89) isoform expressed in eosinophils and neutrophils. Blood. 88:1996;4229-4238.
    • (1996) Blood , vol.88 , pp. 4229-4238
    • Van Dijk, T.B.1    Bracke, M.2    Caldenhoven, E.3
  • 70
    • 0028026937 scopus 로고
    • Association of IgA-Fc receptors (Fc alpha R) with Fc epsilon RI gamma 2 subunits in U937 cells. Aggregation induces the tyrosine phosphorylation of gamma 2
    • Pfefferkorn L.C., Yeaman G.R. Association of IgA-Fc receptors (Fc alpha R) with Fc epsilon RI gamma 2 subunits in U937 cells. Aggregation induces the tyrosine phosphorylation of gamma 2. J. Immunol. 153:1994;3228-3236.
    • (1994) J. Immunol. , vol.153 , pp. 3228-3236
    • Pfefferkorn, L.C.1    Yeaman, G.R.2
  • 71
    • 0033564274 scopus 로고    scopus 로고
    • Human immunoglobulin A receptor (FcαRI, CD89) function in transgenic mice requires both FcR γ chain and CR3 (CD11b/CD18)
    • van Egmond M., van Vuuren A.J.H., Morton H.C., et al. Human immunoglobulin A receptor (FcαRI, CD89) function in transgenic mice requires both FcR γ chain and CR3 (CD11b/CD18). Blood. 93:1999;4387-4394.
    • (1999) Blood , vol.93 , pp. 4387-4394
    • Van Egmond, M.1    Van Vuuren, A.J.H.2    Morton, H.C.3
  • 72
    • 0033548477 scopus 로고    scopus 로고
    • Alternative endocytic pathway for immunoglobulin A Fc receptors (CD89) depends on the lack of FcRgamma association and protects against degradation of bound ligand
    • Launay P., Patry C., Lehuen A., Pasquier B., Blank U., Monteiro R.C. Alternative endocytic pathway for immunoglobulin A Fc receptors (CD89) depends on the lack of FcRgamma association and protects against degradation of bound ligand. J. Biol. Chem. 274:1999;7216-7225.
    • (1999) J. Biol. Chem. , vol.274 , pp. 7216-7225
    • Launay, P.1    Patry, C.2    Lehuen, A.3    Pasquier, B.4    Blank, U.5    Monteiro, R.C.6
  • 73
    • 0029990573 scopus 로고    scopus 로고
    • Identification of Fc alpha receptor (CD89) isoforms generated by alternative splicing that are differentially expressed between blood monocytes and alveolar macrophages
    • Patry C., Sibille Y., Lehuen A., Monteiro R.C. Identification of Fc alpha receptor (CD89) isoforms generated by alternative splicing that are differentially expressed between blood monocytes and alveolar macrophages. J. Immunol. 156:1996;4442-4448.
    • (1996) J. Immunol. , vol.156 , pp. 4442-4448
    • Patry, C.1    Sibille, Y.2    Lehuen, A.3    Monteiro, R.C.4
  • 75
    • 0033983453 scopus 로고    scopus 로고
    • Asparagine-mediated self-association of a model transmembrane helix
    • Choma C., Gratkowski H., Lear J.D., DeGrado W.F. Asparagine-mediated self-association of a model transmembrane helix. Nat. Struct. Biol. 7:2000;161-166.
    • (2000) Nat. Struct. Biol. , vol.7 , pp. 161-166
    • Choma, C.1    Gratkowski, H.2    Lear, J.D.3    DeGrado, W.F.4
  • 77
    • 0024565449 scopus 로고
    • Expression of high-affinity binding of human immunoglobulin E by transfected cells
    • Miller L., Blank U., Metzger H., Kinet J.P. Expression of high-affinity binding of human immunoglobulin E by transfected cells. Science. 244:1989;334-337.
    • (1989) Science , vol.244 , pp. 334-337
    • Miller, L.1    Blank, U.2    Metzger, H.3    Kinet, J.P.4
  • 78
    • 0025214695 scopus 로고
    • Characterization and expression of the gene for the human Fc receptor gamma subunit. Definition of a new gene family
    • Kuster H., Thompson H., Kinet J.P. Characterization and expression of the gene for the human Fc receptor gamma subunit. Definition of a new gene family. J. Biol. Chem. 265:1990;6448-6452.
    • (1990) J. Biol. Chem. , vol.265 , pp. 6448-6452
    • Kuster, H.1    Thompson, H.2    Kinet, J.P.3
  • 79
    • 0026520202 scopus 로고
    • Association of the human Fc epsilon RI gamma subunit with novel cell surface polypeptides
    • Schoneich J.T., Wilkinson V.L., Kado-Fong H., Presky D.H., Kochan J.P. Association of the human Fc epsilon RI gamma subunit with novel cell surface polypeptides. J. Immunol. 148:1992;2181-2185.
    • (1992) J. Immunol. , vol.148 , pp. 2181-2185
    • Schoneich, J.T.1    Wilkinson, V.L.2    Kado-Fong, H.3    Presky, D.H.4    Kochan, J.P.5
  • 80
    • 0024449425 scopus 로고
    • Complete structure of the mouse mast cell receptor for IgE (Fc epsilon RI) and surface expression of chimeric receptors (rat-mouse-human) on transfected cells
    • Ra C., Jouvin M.H., Kinet J.P. Complete structure of the mouse mast cell receptor for IgE (Fc epsilon RI) and surface expression of chimeric receptors (rat-mouse-human) on transfected cells. J. Biol. Chem. 264:1989;15323-15327.
    • (1989) J. Biol. Chem. , vol.264 , pp. 15323-15327
    • Ra, C.1    Jouvin, M.H.2    Kinet, J.P.3
  • 81
    • 0023928548 scopus 로고
    • Isolation of the gene coding for the alpha subunit of the human high affinity IgE receptor
    • Kochan J., Pettine L.F., Hakimi J., Kishi K., Kinet J.P. Isolation of the gene coding for the alpha subunit of the human high affinity IgE receptor. Nucleic Acids Res. 16:1988;3584.
    • (1988) Nucleic Acids Res. , vol.16 , pp. 3584
    • Kochan, J.1    Pettine, L.F.2    Hakimi, J.3    Kishi, K.4    Kinet, J.P.5
  • 82
    • 0024121497 scopus 로고
    • Human and rat mast cell high-affinity immunoglobulin E receptors: Characterization of putative alpha-chain gene products
    • Shimizu A., Tepler I., Benfey P.N., Berenstein E.H., Siraganian R.P., Leder P. Human and rat mast cell high-affinity immunoglobulin E receptors: characterization of putative alpha-chain gene products. Proc. Natl. Acad. Sci. USA. 85:1988;1907-1911.
    • (1988) Proc. Natl. Acad. Sci. USA , vol.85 , pp. 1907-1911
    • Shimizu, A.1    Tepler, I.2    Benfey, P.N.3    Berenstein, E.H.4    Siraganian, R.P.5    Leder, P.6
  • 83
    • 0023730721 scopus 로고
    • CDNA heterogeneity suggests structural variants related to the high-affinity IgE receptor
    • Liu F.T., Albrandt K., Robertson M.W. cDNA heterogeneity suggests structural variants related to the high-affinity IgE receptor. Proc. Natl. Acad. Sci. USA. 85:1988;5639-5643.
    • (1988) Proc. Natl. Acad. Sci. USA , vol.85 , pp. 5639-5643
    • Liu, F.T.1    Albrandt, K.2    Robertson, M.W.3
  • 84
    • 0023666964 scopus 로고
    • A cDNA presumptively coding for the alpha subunit of the receptor with high affinity for immunoglobulin E
    • Kinet J.P., Metzger H., Hakimi J., Kochan J. A cDNA presumptively coding for the alpha subunit of the receptor with high affinity for immunoglobulin E. Biochemistry. 26:1987;4605-4610.
    • (1987) Biochemistry , vol.26 , pp. 4605-4610
    • Kinet, J.P.1    Metzger, H.2    Hakimi, J.3    Kochan, J.4
  • 85
    • 0027998862 scopus 로고
    • Differential control of the tyrosine kinases Lyn and Syk by the two signaling chains of the high affinity immunoglobulin E receptor
    • Jouvin M.H., Adamczewski M., Numerof R., Letourneur O., Valle A., Kinet J.P. Differential control of the tyrosine kinases Lyn and Syk by the two signaling chains of the high affinity immunoglobulin E receptor. J. Biol. Chem. 269:1994;5918-5925.
    • (1994) J. Biol. Chem. , vol.269 , pp. 5918-5925
    • Jouvin, M.H.1    Adamczewski, M.2    Numerof, R.3    Letourneur, O.4    Valle, A.5    Kinet, J.P.6
  • 86
    • 0030604541 scopus 로고    scopus 로고
    • The Fc(epsilon)RIbeta subunit functions as an amplifier of Fc(epsilon)RIgamma-mediated cell activation signals
    • Lin S., Cicala C., Scharenberg A.M., Kinet J.P. The Fc(epsilon)RIbeta subunit functions as an amplifier of Fc(epsilon)RIgamma-mediated cell activation signals. Cell. 85:1996;985-995.
    • (1996) Cell , vol.85 , pp. 985-995
    • Lin, S.1    Cicala, C.2    Scharenberg, A.M.3    Kinet, J.P.4
  • 87
    • 0030566709 scopus 로고    scopus 로고
    • Complement peptides and mast cell triggering
    • Erdei A., Pecht I. Complement peptides and mast cell triggering. Immunol. Lett. 54:1996;109-112.
    • (1996) Immunol. Lett. , vol.54 , pp. 109-112
    • Erdei, A.1    Pecht, I.2
  • 88
    • 0033679212 scopus 로고    scopus 로고
    • A second amplifier function for the allergy-associated Fc(epsilon)RI-beta subunit
    • Donnadieu E., Jouvin M.H., Kinet J.P. A second amplifier function for the allergy-associated Fc(epsilon)RI-beta subunit. Immunity. 12:2000;515-523.
    • (2000) Immunity , vol.12 , pp. 515-523
    • Donnadieu, E.1    Jouvin, M.H.2    Kinet, J.P.3
  • 89
    • 0026549928 scopus 로고
    • Determination of the sequence coding for the beta subunit of the human high-affinity IgE receptor
    • Maekawa K., Imagawa N., Tanaka Y., Harada S. Determination of the sequence coding for the beta subunit of the human high-affinity IgE receptor. FEBS Lett. 302:1992;161-165.
    • (1992) FEBS Lett. , vol.302 , pp. 161-165
    • Maekawa, K.1    Imagawa, N.2    Tanaka, Y.3    Harada, S.4
  • 90
    • 0032924723 scopus 로고    scopus 로고
    • Molecular cloning of cDNAs encoding dog high-affinity IgE receptor alpha, beta, and gamma chains
    • Goitsuka R., Hayashi N., Nagase M., et al. Molecular cloning of cDNAs encoding dog high-affinity IgE receptor alpha, beta, and gamma chains. Immunogenetics. 49:1999;580-582.
    • (1999) Immunogenetics , vol.49 , pp. 580-582
    • Goitsuka, R.1    Hayashi, N.2    Nagase, M.3
  • 91
    • 0042793194 scopus 로고
    • Isolation and characterization of cDNAs coding for the beta subunit of the high-affinity receptor for immunoglobulin E
    • Kinet J.P., Blank U., Ra C., White K., Metzger H., Kochan J. Isolation and characterization of cDNAs coding for the beta subunit of the high-affinity receptor for immunoglobulin E. Proc. Natl. Acad. Sci. USA. 85:1988;6483-6487.
    • (1988) Proc. Natl. Acad. Sci. USA , vol.85 , pp. 6483-6487
    • Kinet, J.P.1    Blank, U.2    Ra, C.3    White, K.4    Metzger, H.5    Kochan, J.6
  • 92
    • 0025045115 scopus 로고
    • Surface expression of mutated subunits of the high affinity mast cell receptor for IgE
    • Varin-Blank N., Metzger H. Surface expression of mutated subunits of the high affinity mast cell receptor for IgE. J. Biol. Chem. 265:1990;15685-15694.
    • (1990) J. Biol. Chem. , vol.265 , pp. 15685-15694
    • Varin-Blank, N.1    Metzger, H.2
  • 93
    • 0012471115 scopus 로고    scopus 로고
    • Spectroscopy-based modeling of the 3D structure of the beta subunit of the high affinity IgE receptor
    • Zloh M., Esposito D., Gibbons W.A. Spectroscopy-based modeling of the 3D structure of the beta subunit of the high affinity IgE receptor. Mol. Simulation. 24:2000;421-447.
    • (2000) Mol. Simulation , vol.24 , pp. 421-447
    • Zloh, M.1    Esposito, D.2    Gibbons, W.A.3
  • 94
    • 0028979725 scopus 로고
    • Fc epsilon RI-beta polymorphism and risk of atopy in a general population sample
    • Hill M.R., James A.L., Faux J.A., et al. Fc epsilon RI-beta polymorphism and risk of atopy in a general population sample. Br. Med. J. 311:1995;776-779.
    • (1995) Br. Med. J. , vol.311 , pp. 776-779
    • Hill, M.R.1    James, A.L.2    Faux, J.A.3
  • 95
    • 0030054886 scopus 로고    scopus 로고
    • A new variant of the beta subunit of the high-affinity receptor for immunoglobulin E (Fc epsilon RI-beta E237G): Associations with measures of atopy and bronchial hyper-responsiveness
    • Hill M.R., Cookson W.O. A new variant of the beta subunit of the high-affinity receptor for immunoglobulin E (Fc epsilon RI-beta E237G): associations with measures of atopy and bronchial hyper-responsiveness. Hum. Mol. Genet. 5:1996;959-962.
    • (1996) Hum. Mol. Genet. , vol.5 , pp. 959-962
    • Hill, M.R.1    Cookson, W.O.2
  • 96
    • 0035367173 scopus 로고    scopus 로고
    • Helical membrane proteins: Diversity of functions in the context of simple architecture
    • Ubarretxena-Belandia I., Engelman D.M. Helical membrane proteins: diversity of functions in the context of simple architecture. Curr. Opin. Struct. Biol. 11:2001;370-376.
    • (2001) Curr. Opin. Struct. Biol. , vol.11 , pp. 370-376
    • Ubarretxena-Belandia, I.1    Engelman, D.M.2
  • 97
    • 0030777759 scopus 로고    scopus 로고
    • The effect of point mutations on the free energy of transmembrane alpha-helix dimerization
    • Fleming K.G., Ackerman A.L., Engelman D.M. The effect of point mutations on the free energy of transmembrane alpha-helix dimerization. J. Mol. Biol. 272:1997;266-275.
    • (1997) J. Mol. Biol. , vol.272 , pp. 266-275
    • Fleming, K.G.1    Ackerman, A.L.2    Engelman, D.M.3
  • 98
    • 0032817780 scopus 로고    scopus 로고
    • Helix packing in polytopic membrane proteins: Role of glycine in transmembrane helix association
    • Javadpour M.M., Eilers M., Groesbeek M., Smith S.O. Helix packing in polytopic membrane proteins: role of glycine in transmembrane helix association. Biophys. J. 77:1999;1609-1618.
    • (1999) Biophys. J. , vol.77 , pp. 1609-1618
    • Javadpour, M.M.1    Eilers, M.2    Groesbeek, M.3    Smith, S.O.4
  • 99
    • 0031563818 scopus 로고    scopus 로고
    • Helix packing in membrane proteins
    • Bowie J.U. Helix packing in membrane proteins. J. Mol. Biol. 272:1997;780-789.
    • (1997) J. Mol. Biol. , vol.272 , pp. 780-789
    • Bowie, J.U.1
  • 100
    • 0034614541 scopus 로고    scopus 로고
    • Helix tilt of the M2 transmembrane peptide from influenza A virus: An intrinsic property
    • Kovacs F.A., Denny J.K., Song Z., Quine J.R., Cross T.A. Helix tilt of the M2 transmembrane peptide from influenza A virus: an intrinsic property. Mol. Biol. 295:2000;117-125.
    • (2000) Mol. Biol. , vol.295 , pp. 117-125
    • Kovacs, F.A.1    Denny, J.K.2    Song, Z.3    Quine, J.R.4    Cross, T.A.5
  • 101
    • 0035843981 scopus 로고    scopus 로고
    • Effects of 'hydrophobic mismatch' on the location of transmembrane helices in the ER membrane
    • Monne M., von Heijne G. Effects of 'hydrophobic mismatch' on the location of transmembrane helices in the ER membrane. FEBS Lett. 496:2001;96-100.
    • (2001) FEBS Lett. , vol.496 , pp. 96-100
    • Monne, M.1    Von Heijne, G.2
  • 102
    • 0031740415 scopus 로고    scopus 로고
    • Hydrophobic mismatch between proteins and lipids in membranes
    • Killian J.A. Hydrophobic mismatch between proteins and lipids in membranes. Biochim. Biophys. Acta. 1376:1998;401-415.
    • (1998) Biochim. Biophys. Acta. , vol.1376 , pp. 401-415
    • Killian, J.A.1
  • 103
    • 0031466450 scopus 로고    scopus 로고
    • Modulation of class I major histocompatibility complex antigen cell-surface stability by transmembrane domain length variation
    • Osborn C.K., Grigoriev V., Crew M.D. Modulation of class I major histocompatibility complex antigen cell-surface stability by transmembrane domain length variation. Mol. Immunol. 34:1997;771-780.
    • (1997) Mol. Immunol. , vol.34 , pp. 771-780
    • Osborn, C.K.1    Grigoriev, V.2    Crew, M.D.3
  • 104
    • 0027457742 scopus 로고
    • Transmembrane domain length affects charge-mediated retention and degradation of proteins within the endoplasmic reticulum
    • Lankford S.P., Cosson P., Bonifacino J.S., Klausner R.D. Transmembrane domain length affects charge-mediated retention and degradation of proteins within the endoplasmic reticulum. J. Biol. Chem. 268:1993;4814-4820.
    • (1993) J. Biol. Chem. , vol.268 , pp. 4814-4820
    • Lankford, S.P.1    Cosson, P.2    Bonifacino, J.S.3    Klausner, R.D.4
  • 105
    • 0031013825 scopus 로고    scopus 로고
    • T-cell antigen receptor transmembrane peptides modulate T-cell function and T cell-mediated disease
    • Manolios N., Collier S., Taylor J., Pollard J., Harrison L.C., Bender V. T-cell antigen receptor transmembrane peptides modulate T-cell function and T cell-mediated disease. Nat. Med. 3:1997;84-88.
    • (1997) Nat. Med. , vol.3 , pp. 84-88
    • Manolios, N.1    Collier, S.2    Taylor, J.3    Pollard, J.4    Harrison, L.C.5    Bender, V.6
  • 106
    • 0034522595 scopus 로고    scopus 로고
    • T cell receptor mimic peptides and their potential application in T-cell-mediated disease
    • Enk A.H., Knop. T cell receptor mimic peptides and their potential application in T-cell-mediated disease. Int. Arch. Allergy Immunol. 123:2000;275-281.
    • (2000) Int. Arch. Allergy Immunol. , vol.123 , pp. 275-281
    • Enk, A.H.1    Knop2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.