메뉴 건너뛰기




Volumn 136, Issue 3, 1997, Pages 555-565

Interactions between newly synthesized glycoproteins, calnexin and a network of resident chaperones in the endoplasmic reticulum

Author keywords

[No Author keywords available]

Indexed keywords

CALNEXIN; CHAPERONE; HEMAGGLUTININ;

EID: 0031045007     PISSN: 00219525     EISSN: None     Source Type: Journal    
DOI: 10.1083/jcb.136.3.555     Document Type: Article
Times cited : (188)

References (56)
  • 1
    • 0028152358 scopus 로고
    • A role for Calnexin (IP90) in the assembly of class II molecules
    • Anderson, K.S., and P. Cresswell. 1994. A role for Calnexin (IP90) in the assembly of class II molecules. EMBO (Eur. Mol. Biol. Organ.) J. 13(3):675-682.
    • (1994) EMBO (Eur. Mol. Biol. Organ.) J. , vol.13 , Issue.3 , pp. 675-682
    • Erson, K.S.1    Cresswell, P.2
  • 2
    • 0029564658 scopus 로고
    • Interaction of calreticulin with protein disulfide isomerase
    • Baksh, S., K. Bums, C. Andrin, and M. Michalak. 1995. Interaction of calreticulin with protein disulfide isomerase. J. Biol. Chem. 270:31338-31344.
    • (1995) J. Biol. Chem. , vol.270 , pp. 31338-31344
    • Baksh, S.1    Bums, K.2    Andrin, C.3    Michalak, M.4
  • 3
    • 0022852825 scopus 로고
    • ATP-coupled transport of vesicular stomatitis virus G protein between the endoplasmic reticulum and the Golgi
    • Balch, W.E., M.M. Elliott, and D.S. Keller. 1986. ATP-coupled transport of vesicular stomatitis virus G protein between the endoplasmic reticulum and the Golgi. J. Cell Biol. 261:14681-14689.
    • (1986) J. Cell Biol. , vol.261 , pp. 14681-14689
    • Balch, W.E.1    Elliott, M.M.2    Keller, D.S.3
  • 4
    • 0018647555 scopus 로고
    • Formation of intermolecular disulfide bonds on nascent immunoglobulin polypeptides
    • Bergman, L.W., and W.M. Kuehl. 1979. Formation of intermolecular disulfide bonds on nascent immunoglobulin polypeptides. J. Biol. Chem. 254:5690-5694.
    • (1979) J. Biol. Chem. , vol.254 , pp. 5690-5694
    • Bergman, L.W.1    Kuehl, W.M.2
  • 5
    • 0024454546 scopus 로고
    • Perturbation of cellular calcium induces secretion of luminal ER proteins
    • Booth, C., and L.E. Koch. 1990. Perturbation of cellular calcium induces secretion of luminal ER proteins. Cell. 59:729-737.
    • (1990) Cell , vol.59 , pp. 729-737
    • Booth, C.1    Koch, L.E.2
  • 6
    • 0025816663 scopus 로고
    • Folding of influenza hemagglutinin in the endoplasmic reticulum
    • Bojaakman, I., H. Hoover-Litty, K.R. Wagner, and A. Helenius. 1991. Folding Of influenza hemagglutinin in the endoplasmic reticulum. J. Cell Biol. 114: 401-411.
    • (1991) J. Cell Biol. , vol.114 , pp. 401-411
    • Bojaakman, I.1    Hoover-Litty, H.2    Wagner, K.R.3    Helenius, A.4
  • 7
    • 0029049090 scopus 로고
    • Cotranslational folding and calnexin binding of influenza hemagglutinin in the endoplasmic reticulum
    • Chen, W., J. Helenius, I. Braakman, and A. Helenius. 1995. Cotranslational folding and calnexin binding of influenza hemagglutinin in the endoplasmic reticulum. Proc. Natl. Acad. Sci. USA. 92:6229-6233.
    • (1995) Proc. Natl. Acad. Sci. USA. , vol.92 , pp. 6229-6233
    • Chen, W.1    Helenius, J.2    Braakman, I.3    Helenius, A.4
  • 8
    • 0023006195 scopus 로고
    • Assembly of influenza hemagglutinin trimers and its role in intracelluiar transport
    • Copeland, C.S., R.W. Doms, E.M. Bolzau, R.G. Webster, and A. Helenius. 1986. Assembly of influenza hemagglutinin trimers and its role in intracelluiar transport. J. Cell Biol. 103:1179-1191.
    • (1986) J. Cell Biol. , vol.103 , pp. 1179-1191
    • Copeland, C.S.1    Doms, R.W.2    Bolzau, E.M.3    Webster, R.G.4    Helenius, A.5
  • 9
    • 0027156495 scopus 로고
    • Interaction with newly synthesized and retained proteins in the endoplasmic reticulum suggests a chaperone function for human integral membrane protein IP90(calnexin)
    • David, V., F. Hochstenbach, S. Rajagopalan, and M.B. Brenner. 1993. Interaction with newly synthesized and retained proteins in the endoplasmic reticulum suggests a chaperone function for human integral membrane protein IP90(calnexin). J. Biol. Chem. 268:9585-9592.
    • (1993) J. Biol. Chem. , vol.268 , pp. 9585-9592
    • David, V.1    Hochstenbach, F.2    Rajagopalan, S.3    Brenner, M.B.4
  • 10
    • 0023033443 scopus 로고
    • Quaternary structure of influenza hemagglutinin after acid treatment
    • Doms, R.W., and A. Helenius. 1986. Quaternary structure of influenza hemagglutinin after acid treatment. J. Virol. 60:833-839.
    • (1986) J. Virol. , vol.60 , pp. 833-839
    • Doms, R.W.1    Helenius, A.2
  • 11
    • 0021984076 scopus 로고
    • Membrane fusion activity of the influenza virus hemagglutinin: The low pH -induced comformationaf change
    • Doms, R.W., A. Helenius, and J. White. 1985. Membrane fusion activity of the influenza virus hemagglutinin: the low pH -induced comformationaf change. J. Biol Chem. 260:2973-2981.
    • (1985) J. Biol Chem. , vol.260 , pp. 2973-2981
    • Doms, R.W.1    Helenius, A.2    White, J.3
  • 12
    • 0026317511 scopus 로고
    • Glucosidase inhibitors: Inhibitors of N-linked oligosaccharide processing
    • Elbein, A.D. 1991. Glucosidase inhibitors: inhibitors of N-linked oligosaccharide processing. FASEB (Fed. Am. Soc. Exp. Biol.) J. 5:3055-3063.
    • (1991) FASEB (Fed. Am. Soc. Exp. Biol.) J. , vol.5 , pp. 3055-3063
    • Elbein, A.D.1
  • 14
    • 0016680128 scopus 로고
    • Deficient uridine diphosphate-N-acetylglucosamine: Glycoprotein N-acetylglucosaminetransferase activity in a clone of Chinese hamster ovary cells with altered surface glyco-proteins
    • Gottlieb, C., J. Baenziger, and S. Kornfeld. 1975. Deficient uridine diphosphate-N-acetylglucosamine: glycoprotein N-acetylglucosaminetransferase activity in a clone of Chinese hamster ovary cells with altered surface glyco-proteins. J. Biol. Chem. 250:3303-3309.
    • (1975) J. Biol. Chem. , vol.250 , pp. 3303-3309
    • Gottlieb, C.1    Baenziger, J.2    Kornfeld, S.3
  • 15
    • 0027141852 scopus 로고
    • A chaperone with a sweet tooth
    • Hammond, C., and A. Helenius. 1993. A chaperone with a sweet tooth. Curr. Biol. 3:884-885.
    • (1993) Curr. Biol. , vol.3 , pp. 884-885
    • Hammond, C.1    Helenius, A.2
  • 16
    • 0028076031 scopus 로고
    • Folding of VSV G protein: Sequential interaction with BiP and calnexin
    • Hammond, C., and A. Helenius. 1994. Folding of VSV G protein: sequential interaction with BiP and calnexin. Science (Wash. DC). 266:456-458.
    • (1994) Science (Wash. DC). , vol.266 , pp. 456-458
    • Hammond, C.1    Helenius, A.2
  • 17
    • 0029094253 scopus 로고
    • Quality control in the secretory pathway
    • Hammond, C., and A. Helenius. 1995. Quality control in the secretory pathway. Curr. Biol. 7:523-529.
    • (1995) Curr. Biol. , vol.7 , pp. 523-529
    • Hammond, C.1    Helenius, A.2
  • 18
    • 0028103695 scopus 로고
    • Role of N-linked oligosaccharides, glucose trimming and calnexin during glycoprotein folding in the endoplasmic reticulum
    • Hammond, C., I. Braakman, and A. Helenius. 1994. Role of N-linked oligosaccharides, glucose trimming and calnexin during glycoprotein folding in the endoplasmic reticulum. Proc. Natl. Acad. Sci. USA. 91:913-917.
    • (1994) Proc. Natl. Acad. Sci. USA. , vol.91 , pp. 913-917
    • Hammond, C.1    Braakman, I.2    Helenius, A.3
  • 19
    • 0029934119 scopus 로고    scopus 로고
    • Calnexin and calreticulin promote folding, delay oligomerization and suppress degradation of influenza hemagglutinin in microsomes
    • Hebert, D., G. Foellmer, and A. Helenius. 1996. Calnexin and calreticulin promote folding, delay oligomerization and suppress degradation of influenza hemagglutinin in microsomes. EMBO (Eur. Mol. Biol. Organ.) J. 15:2961-2968.
    • (1996) EMBO (Eur. Mol. Biol. Organ.) J. , vol.15 , pp. 2961-2968
    • Hebert, D.1    Foellmer, G.2    Helenius, A.3
  • 20
    • 0029024748 scopus 로고
    • Glucose trimming and reglucosylation determines glycoprotein association with calnexin
    • Hebert, D.N., B. Foellmer, and A. Helenius. 1995. Glucose trimming and reglucosylation determines glycoprotein association with calnexin. Cell. 81:425-433.
    • (1995) Cell. , vol.81 , pp. 425-433
    • Hebert, D.N.1    Foellmer, B.2    Helenius, A.3
  • 21
    • 0026659680 scopus 로고
    • The endoplasmic reticulum as a protein folding compartment
    • Helenius, A., T. Marquardt, and I. Braakman. 1992a. The endoplasmic reticulum as a protein folding compartment. TICB. 2:227-231.
    • (1992) TICB. , vol.2 , pp. 227-231
    • Helenius, A.1    Marquardt, T.2    Braakman, I.3
  • 22
    • 0003355223 scopus 로고
    • Protein folding in the endoplasmic reticulum
    • R.G. Rupp and M.S. Oka, editors. Springer Verlag, Berlin/Heidelberg
    • Helenius, A., U. Tatu, T. Marquardt, and I. Braakman. 1992b. Protein folding in the endoplasmic reticulum. In Cell Biology and Biotechnology. R.G. Rupp and M.S. Oka, editors. Springer Verlag, Berlin/Heidelberg.
    • (1992) In Cell Biology and Biotechnology
    • Helenius, A.1    Tatu, U.2    Marquardt, T.3    Braakman, I.4
  • 24
    • 0024461745 scopus 로고
    • Protein oligomerization in the endoplasmic reticulum
    • Hurtley, S.M., and A. Helenius. 1989. Protein oligomerization in the endoplasmic reticulum. Annu. Rev. Cell Biol. 5:277-307.
    • (1989) Annu. Rev. Cell Biol. , vol.5 , pp. 277-307
    • Hurtley, S.M.1    Helenius, A.2
  • 25
  • 26
    • 0028181429 scopus 로고
    • Regulation of MHC Class I transport by the molecular chaperone, calnexin(p88,IP90)
    • Jackson, M.R., M.F. Cohen-Doyle, P.A. Peterson, and D.B. Williams. 1994. Regulation of MHC Class I transport by the molecular chaperone, calnexin(p88,IP90). Science (Wash. DC). 263:384-387.
    • (1994) Science (Wash. DC). , vol.263 , pp. 384-387
    • Jackson, M.R.1    Cohen-Doyle, M.F.2    Peterson, P.A.3    Williams, D.B.4
  • 27
    • 0027993624 scopus 로고
    • Persistence of glucose residues on core oligosaccharides prevents association of TCRα and TCRβ with calnexin and results specifically in accelerated degradation of nascent TCRα proteins within the endoplasmic reticulum
    • Kearse, K.P., D.B. Williams, and A. Singer. 1994. Persistence of glucose residues on core oligosaccharides prevents association of TCRα and TCRβ with calnexin and results specifically in accelerated degradation of nascent TCRα proteins within the endoplasmic reticulum. EMBO (Eur. Mol Biol. Organ.) J. 13:3678-3686.
    • (1994) EMBO (Eur. Mol Biol. Organ.) J. , vol.13 , pp. 3678-3686
    • Kearse, K.P.1    Williams, D.B.2    Singer, A.3
  • 28
    • 0024751077 scopus 로고
    • Architectural editing: Determining the fate of newly synthesized membrane proteins
    • Klausner, R.D. 1989. Architectural editing: determining the fate of newly synthesized membrane proteins. The New Biologist. 1:3-8.
    • (1989) The New Biologist. , vol.1 , pp. 3-8
    • Klausner, R.D.1
  • 29
    • 0026561901 scopus 로고
    • Brefeldin A: Insights into the control of membrane traffic and organelle structure
    • Klausner, R.D., J.G. Donaldson, and J. Lippincott-Schwartz, 1992. Brefeldin A: insights into the control of membrane traffic and organelle structure. J. Cell Biot. 116:1071-1080.
    • (1992) J. Cell Biot. , vol.116 , pp. 1071-1080
    • Klausner, R.D.1    Donaldson, J.G.2    Lippincott-Schwartz, J.3
  • 30
    • 0023336555 scopus 로고
    • Reticuloplasmins: A novel group of proteins in the endoplasmic reticulum
    • Koch, G.L.E. 1987. Reticuloplasmins: a novel group of proteins in the endoplasmic reticulum. J. Cell Sci. 87:491-492.
    • (1987) J. Cell Sci. , vol.87 , pp. 491-492
    • Koch, G.L.E.1
  • 31
    • 0017858332 scopus 로고
    • Proteins of rough microsomal membranes related to ribosome binding
    • Kreibich, G., B.L. Ulrich, and D.D. Sabatini. 1978. Proteins of rough microsomal membranes related to ribosome binding. J. Cell Biol. 77:464-487.
    • (1978) J. Cell Biol. , vol.77 , pp. 464-487
    • Kreibich, G.1    Ulrich, B.L.2    Sabatini, D.D.3
  • 32
    • 0028341304 scopus 로고
    • Association between calnexin and a secretion-incompetent variant of human alantitrypsin
    • Le, A., J.L. Steiner, G.A. Ferrell, J.C. Shaker, and R.N. Sifers. 1994. Association between calnexin and a secretion-incompetent variant of human alantitrypsin. J. Biol. Chem. 269:7514-7519.
    • (1994) J. Biol. Chem. , vol.269 , pp. 7514-7519
    • Le, A.1    Steiner, J.L.2    Ferrell, G.A.3    Shaker, J.C.4    Sifers, R.N.5
  • 33
    • 0028127183 scopus 로고
    • Prolonged association of temperature-sensitive mutants of human P-glycoprotein with calnexin during biogenesis
    • Loo, T.W., and D.M. Clarke. 1994. Prolonged association of temperature-sensitive mutants of human P-glycoprotein with calnexin during biogenesis. J. Biol. Chem. 269:28683-28689.
    • (1994) J. Biol. Chem. , vol.269 , pp. 28683-28689
    • Loo, T.W.1    Clarke, D.M.2
  • 34
    • 0027250528 scopus 로고
    • Post-translational folding of influenza hemagglutinin in isolated endoplasmic reticulum-derived microsomes
    • Marquardt, T., D.N. Hebert, and A. Helenius. 1993. Post-translational folding of influenza hemagglutinin in isolated endoplasmic reticulum-derived microsomes. J. Biol Chem. 268:19618-19625.
    • (1993) J. Biol Chem. , vol.268 , pp. 19618-19625
    • Marquardt, T.1    Hebert, D.N.2    Helenius, A.3
  • 35
    • 0026772964 scopus 로고
    • Involvement of the stress protein HSP47 in procollagen processing in the endoplasmic reticulum
    • Nakai, A., M. Satoh, K. Hirayoshi, and K. Nagata. 1992. Involvement of the stress protein HSP47 in procollagen processing in the endoplasmic reticulum. J. Cell Biol. 117:903-914.
    • (1992) J. Cell Biol. , vol.117 , pp. 903-914
    • Nakai, A.1    Satoh, M.2    Hirayoshi, K.3    Nagata, K.4
  • 36
    • 0028964421 scopus 로고
    • Calreticulin functions as a molecular chaperone in the biosynthesis of myeloperoxidase
    • Nauseef, W.M., S.J. McCormick, and R.A. Clark. 1995. Calreticulin functions as a molecular chaperone in the biosynthesis of myeloperoxidase. J. Biol. Chem. 270:4741-4747.
    • (1995) J. Biol. Chem. , vol.270 , pp. 4741-4747
    • Nauseef, W.M.1    McCormick, S.J.2    Clark, R.A.3
  • 38
    • 0028883409 scopus 로고
    • Calnexin fails to associate with substrate proteins in glucosidase-deficient cell lines
    • Ora, A., and A. Helenius. 1995. Calnexin fails to associate with substrate proteins in glucosidase-deficient cell lines. J. Biol. Chem. 270:26060-26062.
    • (1995) J. Biol. Chem. , vol.270 , pp. 26060-26062
    • Ora, A.1    Helenius, A.2
  • 39
    • 0030053103 scopus 로고    scopus 로고
    • Calreticulin interacts with newly synthesized human immunodeficiency virus type I envelope glycoprotein, suggesting a chaperone function similar to that of calnexin
    • Otteken, A., and B. Moss. 1996. Calreticulin interacts with newly synthesized human immunodeficiency virus type I envelope glycoprotein, suggesting a chaperone function similar to that of calnexin. J. Biol. Chem. 271:97-103.
    • (1996) J. Biol. Chem. , vol.271 , pp. 97-103
    • Otteken, A.1    Moss, B.2
  • 40
    • 0027295871 scopus 로고
    • Association of folding intermediates of glycoproteins with calnexin during protein maturation
    • Ou, W.-J., P.H. Cameron, D.Y. Thomas, and J.J.M. Bergeron. 1993. Association of folding intermediates of glycoproteins with calnexin during protein maturation. Nature (Lond.). 364:771-776.
    • (1993) Nature (Lond.). , vol.364 , pp. 771-776
    • Ou, W.-J.1    Cameron, P.H.2    Thomas, D.Y.3    Bergeron, J.J.M.4
  • 41
    • 0025764613 scopus 로고
    • Recycling of proteins between the endoplasmic reticulum and the Golgi complex
    • Pelharn, H.R. 1991. Recycling of proteins between the endoplasmic reticulum and the Golgi complex. Curr. Opin. Cell Biol. 3:585-591.
    • (1991) Curr. Opin. Cell Biol. , vol.3 , pp. 585-591
    • Pelharn, H.R.1
  • 42
    • 0029160540 scopus 로고
    • Calreticulin is a lectin-like molecular chaperone for glycoproteins in the endoplasmic reticulum
    • Peterson, J.R., A. Ora, P. Nguyen Van, and A. Helenius. 1995. Calreticulin is a lectin-like molecular chaperone for glycoproteins in the endoplasmic reticulum. Mol. Biol. Cell. 6:1173-1184.
    • (1995) Mol. Biol. Cell. , vol.6 , pp. 1173-1184
    • Peterson, J.R.1    Ora, A.2    Van Nguyen, P.3    Helenius, A.4
  • 43
    • 0028232167 scopus 로고
    • Participation of the endoplasmic reticulum chaperone calnexin(p88, IP90) in the biogenesis of the cystic fibrosis transmembrane conductance regulator
    • Pind, S., J.R. Riordian, and D.B. Williams. 1994. Participation of the endoplasmic reticulum chaperone calnexin(p88, IP90) in the biogenesis of the cystic fibrosis transmembrane conductance regulator. J. Biol. Chem. 269:12784-32788.
    • (1994) J. Biol. Chem. , vol.269 , pp. 12784-32788
    • Pind, S.1    Riordian, J.R.2    Williams, D.B.3
  • 44
    • 0026317971 scopus 로고
    • A novel glycosylation phenotype expressed by Lec23, Chinese hamster ovary mutant deficient in α-glucosidase I
    • Ray, M.K., J. Yang, S. Sundaram, and P. Stanley. 1991. A novel glycosylation phenotype expressed by Lec23, Chinese hamster ovary mutant deficient in α-glucosidase I. J. Biol. Chem. 266:22818-22825.
    • (1991) J. Biol. Chem. , vol.266 , pp. 22818-22825
    • Ray, M.K.1    Yang, J.2    Sundaram, S.3    Stanley, P.4
  • 45
    • 0025361036 scopus 로고
    • The involvement of calcium in the transport of secretory proteins from the endoplasmic reticulum
    • Sambrook, J.F. 1990. The involvement of calcium in the transport of secretory proteins from the endoplasmic reticulum. Cell. 61:197-199.
    • (1990) Cell. , vol.61 , pp. 197-199
    • Sambrook, J.F.1
  • 46
    • 0023733211 scopus 로고
    • Identification, by a monoclonal antibody, of a 53-kD protein associated with a tubulo-vesicular compartment at the cis-side of the Golgi apparatus
    • Schweizer, A., J.A.M. Fransen, T. Bächi, L. Ginsel, and H.-P. Hauri. 1988. Identification, by a monoclonal antibody, of a 53-kD protein associated with a tubulo-vesicular compartment at the cis-side of the Golgi apparatus. J. Cell Biol. 107:1643-1653.
    • (1988) J. Cell Biol. , vol.107 , pp. 1643-1653
    • Schweizer, A.1    Fransen, J.A.M.2    Bächi, T.3    Ginsel, L.4    Hauri, H.-P.5
  • 47
    • 0028100171 scopus 로고
    • Retention and retrieval: Both mechanisms cooperate to maintain Calreticulin in the endoplasmic reticulum
    • Sonnichsen, B., J. Füllefrug, P. Nguyen Van, W. Diekmann, D.G. Robinson, and G. Meiskes. 1994. Retention and retrieval: both mechanisms cooperate to maintain Calreticulin in the endoplasmic reticulum. J. Cell Sci. 107:2705-2717.
    • (1994) J. Cell Sci. , vol.107 , pp. 2705-2717
    • Sonnichsen, B.1    Füllefrug, J.2    Van Nguyen, P.3    Diekmann, W.4    Robinson, D.G.5    Meiskes, G.6
  • 48
    • 15844386822 scopus 로고    scopus 로고
    • Definition of the lectin-like properties of the molecular chaperone, Calreticulin, and demonstration of its copurification with endomannosidase from rat liver Golgi
    • Spiro, R.G., Q. Zhu, V. Bhoyroo, and H.-D. Söling. 1996. Definition of the lectin-like properties of the molecular chaperone, Calreticulin, and demonstration of its copurification with endomannosidase from rat liver Golgi. J. Biol Chem. 271:11588-11594.
    • (1996) J. Biol Chem. , vol.271 , pp. 11588-11594
    • Spiro, R.G.1    Zhu, Q.2    Bhoyroo, V.3    Söling, H.-D.4
  • 49
    • 0028906029 scopus 로고
    • Folding and oligomerization of influenza hemagglutinin in the ER and the intermediate compartment
    • Tatu, U., C. Hammond, and A. Helenius. 1995. Folding and oligomerization of influenza hemagglutinin in the ER and the intermediate compartment. EMBO (Eur. Mol. Biol. Organ.) J. 14:1340-1348.
    • (1995) EMBO (Eur. Mol. Biol. Organ.) J. , vol.14 , pp. 1340-1348
    • Tatu, U.1    Hammond, C.2    Helenius, A.3
  • 50
    • 0029100978 scopus 로고
    • Calnexin influences folding of human class I histocompatibility proteins but not their assembly with B2-microglobulin
    • Tector, M., and R.D. Salter. 1995. Calnexin influences folding of human class I histocompatibility proteins but not their assembly with B2-microglobulin. J. Biol. Chem. 270:19638-19642.
    • (1995) J. Biol. Chem. , vol.270 , pp. 19638-19642
    • Tector, M.1    Salter, R.D.2
  • 52
    • 0029134004 scopus 로고
    • Chaperone function of Calreticulin when expressed in the endoplasmic reticulum as the membrane-anchored and soluble forms
    • Wada, I., S.-i. Imai, M. Kai, F. Sakane, and H. Kanon. 1995. Chaperone function of Calreticulin when expressed in the endoplasmic reticulum as the membrane-anchored and soluble forms. J. Biol. Chem. 270:20298-20304.
    • (1995) J. Biol. Chem. , vol.270 , pp. 20298-20304
    • Wada, I.1    Imai, S.-I.2    Kai, M.3    Sakane, F.4    Kanon, H.5
  • 55
    • 0029952519 scopus 로고    scopus 로고
    • Structural basis of lectin carbohydrate recognition
    • Weis, W.I., and K. Drickamer. 1996. Structural basis of lectin carbohydrate recognition. Annu. Rev. Biochem. 65:441-473.
    • (1996) Annu. Rev. Biochem. , vol.65 , pp. 441-473
    • Weis, W.I.1    Drickamer, K.2
  • 56
    • 0026754497 scopus 로고
    • Divalent cation dependent stimulation of ligand binding to the 46 kDa mannose 6-phosphate receptor correlates with divalent cation-dependent tetramerization
    • Zhongmin, M., J.H. Grubb, and W.S. Sly. 1992. Divalent cation dependent stimulation of ligand binding to the 46 kDa mannose 6-phosphate receptor correlates with divalent cation-dependent tetramerization. J. Biol. Chem. 267:19017-19022.
    • (1992) J. Biol. Chem. , vol.267 , pp. 19017-19022
    • Zhongmin, M.1    Grubb, J.H.2    Sly, W.S.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.