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Volumn 286, Issue 5, 1999, Pages 1303-1310

Recognition of the carboxyl-terminal signal for GPI modification requires translocation of its hydrophobic domain across the ER membrane

Author keywords

Endoplasmic reticulum; Folate receptor; Glycosyl phosphatidylinositol; LDL receptor; Transmembrane polypeptide

Indexed keywords

CHIMERIC PROTEIN; FOLIC ACID; GLYCOSYLPHOSPHATIDYLINOSITOL; LOW DENSITY LIPOPROTEIN RECEPTOR; MEMBRANE PROTEIN; VITAMIN RECEPTOR;

EID: 0033548673     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1999.2584     Document Type: Article
Times cited : (25)

References (48)
  • 1
    • 0029818146 scopus 로고    scopus 로고
    • Folate Receptor
    • Antony A. C. Folate Receptor. Annu. Rev. Nutr. 16:1996;501-521.
    • (1996) Annu. Rev. Nutr. , vol.16 , pp. 501-521
    • Antony, A.C.1
  • 2
    • 0021867815 scopus 로고
    • Rapid processing of the carboxyl terminus of a trypanosome variant surface glycoprotein
    • Bangs J. D., Hereld D., Krakow J. L., Hart G. W., Englund P. T. Rapid processing of the carboxyl terminus of a trypanosome variant surface glycoprotein. Proc. Natl Acad. Sci. USA. 82:1985;3207-3211.
    • (1985) Proc. Natl Acad. Sci. USA , vol.82 , pp. 3207-3211
    • Bangs, J.D.1    Hereld, D.2    Krakow, J.L.3    Hart, G.W.4    Englund, P.T.5
  • 3
    • 0022539768 scopus 로고
    • Posttranslational modification and intracellular transport of a trypanosome variant surface glycoprotein
    • Bangs J. D., Andrews N. W., Hart G. W., Englund P. T. Posttranslational modification and intracellular transport of a trypanosome variant surface glycoprotein. J. Cell Biol. 103:1986;255-263.
    • (1986) J. Cell Biol. , vol.103 , pp. 255-263
    • Bangs, J.D.1    Andrews, N.W.2    Hart, G.W.3    Englund, P.T.4
  • 4
    • 0029827249 scopus 로고    scopus 로고
    • Yeast Gpi8p is essential for GPI anchor attachment onto proteins
    • Benghezal M., Benachour A., Rusconi S., Aebi M., Conzelmann A. Yeast Gpi8p is essential for GPI anchor attachment onto proteins. EMBO J. 15:1996;6575-6583.
    • (1996) EMBO J. , vol.15 , pp. 6575-6583
    • Benghezal, M.1    Benachour, A.2    Rusconi, S.3    Aebi, M.4    Conzelmann, A.5
  • 5
    • 0018987976 scopus 로고
    • Intracellular protein topogenesis
    • Blobel G. Intracellular protein topogenesis. Proc. Natl Sci. USA. 77:1980;1496-1500.
    • (1980) Proc. Natl Sci. USA , vol.77 , pp. 1496-1500
    • Blobel, G.1
  • 6
    • 0020288417 scopus 로고
    • A prokaryotic membrane anchor sequence: Carboxyl terminus of bacteriophage f1 gene III protein retains it in the membrane
    • Boeke J. D., Model P. A prokaryotic membrane anchor sequence: carboxyl terminus of bacteriophage f1 gene III protein retains it in the membrane. Proc. Natl Acad. Sci. USA. 79:1982;5200-5204.
    • (1982) Proc. Natl Acad. Sci. USA , vol.79 , pp. 5200-5204
    • Boeke, J.D.1    Model, P.2
  • 7
    • 0025203675 scopus 로고
    • Glycolipid anchoring of plasma membrane proteins
    • Cross G. A. M. Glycolipid anchoring of plasma membrane proteins. Annu. Rev. Cell Biol. 6:1990;1-39.
    • (1990) Annu. Rev. Cell Biol. , vol.6 , pp. 1-39
    • Cross, G.A.M.1
  • 8
    • 0022358219 scopus 로고
    • Fine structure of a membrane anchor domain
    • Davis N. G., Boeke J. D., Model P. Fine structure of a membrane anchor domain. J. Mol. Biol. 181:1985;111-121.
    • (1985) J. Mol. Biol. , vol.181 , pp. 111-121
    • Davis, N.G.1    Boeke, J.D.2    Model, P.3
  • 9
    • 0019464222 scopus 로고
    • The spontaneous insertion of proteins into and across membranes: The helical hairpin hypothesis
    • Engelman D. M., Steitz T. A. The spontaneous insertion of proteins into and across membranes: the helical hairpin hypothesis. Cell. 23:1981;411-422.
    • (1981) Cell , vol.23 , pp. 411-422
    • Engelman, D.M.1    Steitz, T.A.2
  • 10
    • 0023944337 scopus 로고
    • Cell-surface anchoring of proteins via glycosylphosphatidylinositol structures
    • Ferguson M. A. J., Williams A. F. Cell-surface anchoring of proteins via glycosylphosphatidylinositol structures. Annu. Rev. Biochem. 57:1988;285-320.
    • (1988) Annu. Rev. Biochem. , vol.57 , pp. 285-320
    • Ferguson, M.A.J.1    Williams, A.F.2
  • 11
    • 0022635703 scopus 로고
    • Biosynthesis of trypanosome brucei variant surface glycoproteins. N-glycosylation and addition of a phosphatidylinositol membrane anchor
    • Ferguson M. A., Duszenko M., Lamont G. S., Overath P., Cross G. A. Biosynthesis of trypanosome brucei variant surface glycoproteins. N-glycosylation and addition of a phosphatidylinositol membrane anchor. J. Biol. Chem. 261:1986;356-362.
    • (1986) J. Biol. Chem. , vol.261 , pp. 356-362
    • Ferguson, M.A.1    Duszenko, M.2    Lamont, G.S.3    Overath, P.4    Cross, G.A.5
  • 12
    • 0025737738 scopus 로고
    • A glycosylphosphatidylinositol protein anchor from procyclic stage Trypanosoma brucei
    • Field M. C., Menon A. K., Cross G. A. M. A glycosylphosphatidylinositol protein anchor from procyclic stage Trypanosoma brucei. EMBO J. 10:1991;2731-2739.
    • (1991) EMBO J. , vol.10 , pp. 2731-2739
    • Field, M.C.1    Menon, A.K.2    Cross, G.A.M.3
  • 13
    • 0030920440 scopus 로고    scopus 로고
    • Mutational analysis of the C-terminal signal peptide of bovine liver 5′-nucleotidase for GPI anchoring: A study on the significance of the hydrophilic spacer region
    • Furukawa Y., Tsukamoto K., Ikezawa H. Mutational analysis of the C-terminal signal peptide of bovine liver 5′-nucleotidase for GPI anchoring: a study on the significance of the hydrophilic spacer region. Biochim. Biophys. Acta. 1328:1997;185-196.
    • (1997) Biochim. Biophys. Acta , vol.1328 , pp. 185-196
    • Furukawa, Y.1    Tsukamoto, K.2    Ikezawa, H.3
  • 14
    • 0026780325 scopus 로고
    • Phosphatidylinositol glycan (PI-G) anchored membrane proteins
    • Gerber L. D., Kodukula K., Udenfriend S. Phosphatidylinositol glycan (PI-G) anchored membrane proteins. J. Biol. Chem. 267:1992;12168-12173.
    • (1992) J. Biol. Chem. , vol.267 , pp. 12168-12173
    • Gerber, L.D.1    Kodukula, K.2    Udenfriend, S.3
  • 15
    • 0028940341 scopus 로고
    • Yeast Gaa1p is required for attachment of a completed GPI anchor onto proteins
    • Hamburger D., Egerton M., Riezman H. Yeast Gaa1p is required for attachment of a completed GPI anchor onto proteins. J. Cell Biol. 129:1995;629-639.
    • (1995) J. Cell Biol. , vol.129 , pp. 629-639
    • Hamburger, D.1    Egerton, M.2    Riezman, H.3
  • 16
    • 0026349333 scopus 로고
    • Glycosyl-phosphatidylinositol-anchored membrane proteins can be distinguished from transmembrane polypeptide-anchored proteins by differential solubilization and temperature-induced phase separation in Triton X-114
    • Hooper N. M., Bashir A. Glycosyl-phosphatidylinositol-anchored membrane proteins can be distinguished from transmembrane polypeptide-anchored proteins by differential solubilization and temperature-induced phase separation in Triton X-114. Biochem. J. 280:1991;745-751.
    • (1991) Biochem. J. , vol.280 , pp. 745-751
    • Hooper, N.M.1    Bashir, A.2
  • 17
    • 0028243260 scopus 로고
    • Signal peptide cleavage regions. Functional limits on length and topological implications
    • Jain R. G., Rusch S. L., Kendall D. A. Signal peptide cleavage regions. Functional limits on length and topological implications. J. Biol. Chem. 269:1994;16305-16310.
    • (1994) J. Biol. Chem. , vol.269 , pp. 16305-16310
    • Jain, R.G.1    Rusch, S.L.2    Kendall, D.A.3
  • 18
    • 0031564485 scopus 로고    scopus 로고
    • The presence of GPI-linked protein(s) in an archaeobacterium, Sulfolobus acidocaldarius, closely related to eukaryotes
    • Kobayashi T., Nishizaki R., Ikezawa H. The presence of GPI-linked protein(s) in an archaeobacterium, Sulfolobus acidocaldarius, closely related to eukaryotes. Biochim. Biophys. Acta. 1334:1997;1-4.
    • (1997) Biochim. Biophys. Acta , vol.1334 , pp. 1-4
    • Kobayashi, T.1    Nishizaki, R.2    Ikezawa, H.3
  • 19
    • 0027498149 scopus 로고
    • Biosynthesis of glycosylphosphatidylinositol (GPI)-anchored membrane proteins in intact cells: Specific amino acid requirements adjacent to the site of cleavage and GPI attachment
    • Kodukula K., Gerber L. D., Amthauer R., Brink L., Udenfriend S. Biosynthesis of glycosylphosphatidylinositol (GPI)-anchored membrane proteins in intact cells: specific amino acid requirements adjacent to the site of cleavage and GPI attachment. J. Cell Biol. 120:1993;657-664.
    • (1993) J. Cell Biol. , vol.120 , pp. 657-664
    • Kodukula, K.1    Gerber, L.D.2    Amthauer, R.3    Brink, L.4    Udenfriend, S.5
  • 20
    • 0024336971 scopus 로고
    • Complementary DNA for the folate binding protein correctly predicts anchoring to the membrane by glycosyl-phosphatidylinositol
    • Lacey S. W., Sanders J. M., Rothberg K. G., Anderson R. G., Kamen B. A. Complementary DNA for the folate binding protein correctly predicts anchoring to the membrane by glycosyl-phosphatidylinositol. J. Clin. Invest. 84:1989;715-720.
    • (1989) J. Clin. Invest. , vol.84 , pp. 715-720
    • Lacey, S.W.1    Sanders, J.M.2    Rothberg, K.G.3    Anderson, R.G.4    Kamen, B.A.5
  • 21
    • 0024316809 scopus 로고
    • The glycosyl-phosphatidylinositol anchor of membrane proteins
    • Low M. G. The glycosyl-phosphatidylinositol anchor of membrane proteins. Biochim. Biophys. Acta. 988:1989;427-454.
    • (1989) Biochim. Biophys. Acta , vol.988 , pp. 427-454
    • Low, M.G.1
  • 22
    • 0026517635 scopus 로고
    • Site-specific mutations in the COOH-terminus of placental alkaline phosphatase: A single amino acid change converts a phosphatidylinositol-glycan-anchored protein to a secreted protein
    • Lowe M. E. Site-specific mutations in the COOH-terminus of placental alkaline phosphatase: a single amino acid change converts a phosphatidylinositol-glycan-anchored protein to a secreted protein. J. Cell Biol. 116:1992;799-807.
    • (1992) J. Cell Biol. , vol.116 , pp. 799-807
    • Lowe, M.E.1
  • 23
    • 0029096233 scopus 로고
    • An active carbonyl formed during glycosylphosphatidylinositol addition to a protein is evidence of catalysis by a transamidase
    • Maxwell S. E., Ramalingam S., Gerber L. D., Brink L., Udenfriend S. An active carbonyl formed during glycosylphosphatidylinositol addition to a protein is evidence of catalysis by a transamidase. J. Biol. Chem. 270:1995a;19576-19582.
    • (1995) J. Biol. Chem. , vol.270 , pp. 19576-19582
    • Maxwell, S.E.1    Ramalingam, S.2    Gerber, L.D.3    Brink, L.4    Udenfriend, S.5
  • 24
    • 0028950984 scopus 로고
    • Cleavage without anchor addition accompanies the processing of a nascent protein to its glycosylphosphatidylinositol-anchored form
    • Maxwell S. E., Ramalingam S., Udenfriend S. Cleavage without anchor addition accompanies the processing of a nascent protein to its glycosylphosphatidylinositol-anchored form. Proc. Natl Acad. Sci. USA. 92:1995b;1550-1554.
    • (1995) Proc. Natl Acad. Sci. USA , vol.92 , pp. 1550-1554
    • Maxwell, S.E.1    Ramalingam, S.2    Udenfriend, S.3
  • 25
    • 0027257177 scopus 로고
    • The structure, biosynthesis and function of glycosylated phosphatidylinositols in the parasitic protozoa and higher eukaryotes
    • McConville M. J., Ferguson M. A. The structure, biosynthesis and function of glycosylated phosphatidylinositols in the parasitic protozoa and higher eukaryotes. Biochem. J. 294:1993;305-324.
    • (1993) Biochem. J. , vol.294 , pp. 305-324
    • McConville, M.J.1    Ferguson, M.A.2
  • 26
    • 0026033050 scopus 로고
    • Glycosylphospholipid membrane anchor attachment. Molecular analysis of the cleavage/attachment site
    • Moran P., Raab H., Kohr W. J., Caras I. W. Glycosylphospholipid membrane anchor attachment. Molecular analysis of the cleavage/attachment site. J. Biol. Chem. 266:1991;1250-1257.
    • (1991) J. Biol. Chem. , vol.266 , pp. 1250-1257
    • Moran, P.1    Raab, H.2    Kohr, W.J.3    Caras, I.W.4
  • 27
    • 0029984842 scopus 로고    scopus 로고
    • Evidence for a glycosylinositolphospholipid-anchored alkaline phosphatase in the aquatic plant Spirodela oligorrhiza
    • Morita N., Nakazato H., Okuyama Y., Kim G. A., Thompson J. Evidence for a glycosylinositolphospholipid-anchored alkaline phosphatase in the aquatic plant Spirodela oligorrhiza. Biochim. Biophys. Acta. 1290:1997;53-62.
    • (1997) Biochim. Biophys. Acta , vol.1290 , pp. 53-62
    • Morita, N.1    Nakazato, H.2    Okuyama, Y.3    Kim, G.A.4    Thompson, J.5
  • 28
    • 0027270310 scopus 로고
    • Analysis of the sequence requirements for glycosylphosphatidylinositol anchoring of Saccharomyces cerevisiae Gas1 protein
    • Nuoffer C., Horvath A., Riezman H. Analysis of the sequence requirements for glycosylphosphatidylinositol anchoring of Saccharomyces cerevisiae Gas1 protein. J. Biol. Chem. 268:1993;10558-10563.
    • (1993) J. Biol. Chem. , vol.268 , pp. 10558-10563
    • Nuoffer, C.1    Horvath, A.2    Riezman, H.3
  • 29
    • 0032511889 scopus 로고    scopus 로고
    • Crystal structure of a bacterial signal peptidase in complex with a β-lactam inhibitor
    • Paetzel M., Dalbey R. E., Strynadka N. C. J. Crystal structure of a bacterial signal peptidase in complex with a β-lactam inhibitor. Nature. 396:1998;186-190.
    • (1998) Nature , vol.396 , pp. 186-190
    • Paetzel, M.1    Dalbey, R.E.2    Strynadka, N.C.J.3
  • 30
    • 0029794879 scopus 로고    scopus 로고
    • COOH-terminal processing of nascent polypeptides by the glycosylphosphatidyl-inositol transamidase in the presence of hydrazine is governed by the same parameters as glycosylphosphatidylinositol addition
    • Ramalingam S., Maxwell S. E., Medof M. E., Chen R., Gerber L. D., Udenfriend S. COOH-terminal processing of nascent polypeptides by the glycosylphosphatidyl-inositol transamidase in the presence of hydrazine is governed by the same parameters as glycosylphosphatidylinositol addition. Proc. Natl Acad. Sci. USA. 93:1996;7528-7533.
    • (1996) Proc. Natl Acad. Sci. USA , vol.93 , pp. 7528-7533
    • Ramalingam, S.1    Maxwell, S.E.2    Medof, M.E.3    Chen, R.4    Gerber, L.D.5    Udenfriend, S.6
  • 31
    • 0024267353 scopus 로고
    • Lipid analysis of the glycoinositol phospholipid membrane anchor of human erthrocyte acetylcholinesterase. Palmitoylation of inositol results in resistance to phosphatidylinositol-specific phospholipase C
    • Roberts W. L., Myher J. J., Kuksis A., Low M. G., Rosenberry T. L. Lipid analysis of the glycoinositol phospholipid membrane anchor of human erthrocyte acetylcholinesterase. Palmitoylation of inositol results in resistance to phosphatidylinositol-specific phospholipase C. J. Biol. Chem. 263:1988a;18766-18775.
    • (1988) J. Biol. Chem. , vol.263 , pp. 18766-18775
    • Roberts, W.L.1    Myher, J.J.2    Kuksis, A.3    Low, M.G.4    Rosenberry, T.L.5
  • 32
    • 0024230917 scopus 로고
    • Structural characterization of the glycoinositol phospholipid membrane anchor of human erythrocyte acetylcholinesterase by fast atom bombardment mass spectrometry
    • Roberts W. L., Santikam S., Reinhold V. N., Rosenberry T. L. Structural characterization of the glycoinositol phospholipid membrane anchor of human erythrocyte acetylcholinesterase by fast atom bombardment mass spectrometry. J. Biol. Chem. 263:1988b;18776-18784.
    • (1988) J. Biol. Chem. , vol.263 , pp. 18776-18784
    • Roberts, W.L.1    Santikam, S.2    Reinhold, V.N.3    Rosenberry, T.L.4
  • 33
    • 0020064690 scopus 로고
    • Mechanisms for the incorporation of proteins in membranes and organelles
    • Sabatini D. D., Kreibich G., Morimoto T., Adesnik M. Mechanisms for the incorporation of proteins in membranes and organelles. J. Cell Biol. 92:1982;1-22.
    • (1982) J. Cell Biol. , vol.92 , pp. 1-22
    • Sabatini, D.D.1    Kreibich, G.2    Morimoto, T.3    Adesnik, M.4
  • 34
    • 0030713346 scopus 로고    scopus 로고
    • Expression levels of functional folate receptors α and β are related to the number of N-glycosylated sites
    • Shen F., Wang H., Zheng X., Ratnam M. Expression levels of functional folate receptors α and β are related to the number of N-glycosylated sites. Biochem. J. 327:1997;759-764.
    • (1997) Biochem. J. , vol.327 , pp. 759-764
    • Shen, F.1    Wang, H.2    Zheng, X.3    Ratnam, M.4
  • 35
    • 0030890351 scopus 로고    scopus 로고
    • Detection of glycosyl-phosphatidylinositol-anchored proteins on the surface of Nicotiana tabacum protoplasts
    • Takos A. M., Dry I. B., Soole K. L. Detection of glycosyl-phosphatidylinositol-anchored proteins on the surface of Nicotiana tabacum protoplasts. FEBS Letters. 405:1997;1-4.
    • (1997) FEBS Letters , vol.405 , pp. 1-4
    • Takos, A.M.1    Dry, I.B.2    Soole, K.L.3
  • 36
    • 0017884417 scopus 로고
    • The hydrophobic effect and the organization of living matter
    • Tanford C. The hydrophobic effect and the organization of living matter. Science. 200:1978;1012-1018.
    • (1978) Science , vol.200 , pp. 1012-1018
    • Tanford, C.1
  • 37
    • 0028981209 scopus 로고
    • How glycosylphosphatidylinositol-anchored membrane proteins are made
    • Udenfriend S., Kodukula K. How glycosylphosphatidylinositol-anchored membrane proteins are made. Annu. Rev. Biochem. 64:1995;563-591.
    • (1995) Annu. Rev. Biochem. , vol.64 , pp. 563-591
    • Udenfriend, S.1    Kodukula, K.2
  • 38
    • 0029100260 scopus 로고
    • Soluble constituents of the ER lumen are required for GPI anchoring of a model protein
    • Vidugiriene J., Menon A. K. Soluble constituents of the ER lumen are required for GPI anchoring of a model protein. EMBO J. 14:1995;4686-4694.
    • (1995) EMBO J. , vol.14 , pp. 4686-4694
    • Vidugiriene, J.1    Menon, A.K.2
  • 39
    • 0000651660 scopus 로고
    • The distribution of positively charged residues in bacterial inner membrane proteins correlates with the trans-membrane topology
    • Von Heijne G. The distribution of positively charged residues in bacterial inner membrane proteins correlates with the trans-membrane topology. EMBO J. 5:1986;3021-3027.
    • (1986) EMBO J. , vol.5 , pp. 3021-3027
    • Von Heijne, G.1
  • 40
    • 0030968672 scopus 로고    scopus 로고
    • Getting greasy: How transmembrane polypeptide segments integrate into the lipid bilayer
    • Von Heijne G. Getting greasy: how transmembrane polypeptide segments integrate into the lipid bilayer. Mol. Microbiol. 24:1997;249-253.
    • (1997) Mol. Microbiol. , vol.24 , pp. 249-253
    • Von Heijne, G.1
  • 41
    • 0032511879 scopus 로고    scopus 로고
    • Life and death of a signal peptide
    • Von Heijne G. Life and death of a signal peptide. Nature. 396:1998;111-113.
    • (1998) Nature , vol.396 , pp. 111-113
    • Von Heijne, G.1
  • 42
    • 0018485028 scopus 로고
    • Trans-membrane translocation of proteins
    • Von Heijne G., Blomberg C. Trans-membrane translocation of proteins. Eur. J. Biochem. 97:1979;175-181.
    • (1979) Eur. J. Biochem. , vol.97 , pp. 175-181
    • Von Heijne, G.1    Blomberg, C.2
  • 43
    • 0030694625 scopus 로고    scopus 로고
    • Proteolysis of the carboxyl-terminal GPI signal independent of GPI modification as a mechanism for selective protein secretion
    • Wang J., Shen F., Yan W., Wu M., Ratnam M. Proteolysis of the carboxyl-terminal GPI signal independent of GPI modification as a mechanism for selective protein secretion. Biochemistry. 36:1997;14583-14592.
    • (1997) Biochemistry , vol.36 , pp. 14583-14592
    • Wang, J.1    Shen, F.2    Yan, W.3    Wu, M.4    Ratnam, M.5
  • 45
    • 0025572743 scopus 로고
    • A positively charged region is a determinant of the orientation of cytoplasmic membrane proteins in Escherichia coli
    • Yamane K., Akiyama Y., Ito K., Mizushima S. A positively charged region is a determinant of the orientation of cytoplasmic membrane proteins in Escherichia coli. J. Biol. Chem. 265:1990;21166-21171.
    • (1990) J. Biol. Chem. , vol.265 , pp. 21166-21171
    • Yamane, K.1    Akiyama, Y.2    Ito, K.3    Mizushima, S.4
  • 46
    • 0028867956 scopus 로고
    • Preferred sites of glycosylphosphatidylinositol modification in folate receptors and constraints in the primary structure of the hydrophobic portion of the signal
    • Yan W., Ratnam M. Preferred sites of glycosylphosphatidylinositol modification in folate receptors and constraints in the primary structure of the hydrophobic portion of the signal. Biochemistry. 34:1995;14594-14600.
    • (1995) Biochemistry , vol.34 , pp. 14594-14600
    • Yan, W.1    Ratnam, M.2
  • 47
    • 0032498235 scopus 로고    scopus 로고
    • The hydrophobic domains in the carboxyl-terminal signal for GPI modification and in the amino-terminal leader peptide have similar structural requirements
    • Yan W., Shen F., Dillon B., Ratnam M. The hydrophobic domains in the carboxyl-terminal signal for GPI modification and in the amino-terminal leader peptide have similar structural requirements. J. Mol. Biol. 275:1998;25-33.
    • (1998) J. Mol. Biol. , vol.275 , pp. 25-33
    • Yan, W.1    Shen, F.2    Dillon, B.3    Ratnam, M.4
  • 48
    • 0030778207 scopus 로고    scopus 로고
    • The affected gene underlying the class K glycosylphosphatidylinositol (GPI) surface protein defect codes for the GPI transamidase
    • Yu J., Nagarajan S., Knez J. J., Udenfriend S., Chen R., Medof M. E. The affected gene underlying the class K glycosylphosphatidylinositol (GPI) surface protein defect codes for the GPI transamidase. Proc. Natl Acad. Sci. USA. 94:1997;12580-12585.
    • (1997) Proc. Natl Acad. Sci. USA , vol.94 , pp. 12580-12585
    • Yu, J.1    Nagarajan, S.2    Knez, J.J.3    Udenfriend, S.4    Chen, R.5    Medof, M.E.6


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