메뉴 건너뛰기




Volumn 43, Issue 17, 2004, Pages 5109-5118

Disulfide Bond Rearrangement during Formation of the Chorionic Gonadotropin β-Subunit Cystine Knot in Vivo

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; CHEMICAL BONDS; PROTEINS; X RAYS;

EID: 2142764423     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi049856x     Document Type: Article
Times cited : (11)

References (29)
  • 1
    • 0019729482 scopus 로고
    • Glycoprotein hormones: Structure and function
    • Pierce, J. G., and Parsons, T. F. (1981) Glycoprotein hormones: structure and function, Annu. Rev. Biochem. 50, 465-495.
    • (1981) Annu. Rev. Biochem. , vol.50 , pp. 465-495
    • Pierce, J.G.1    Parsons, T.F.2
  • 3
    • 0028773646 scopus 로고
    • Structure of human chorionic gonadotropin at 2.6 A resolufion from MAD analysis of the selenomethionyl protein
    • Wu, H., Lustbader, J. W., Liu, Y., Canfield, R. E., and Hendrickson, W. A. (1994) Structure of human chorionic gonadotropin at 2.6 A resolufion from MAD analysis of the selenomethionyl protein, Structure 2, 545-558.
    • (1994) Structure , vol.2 , pp. 545-558
    • Wu, H.1    Lustbader, J.W.2    Liu, Y.3    Canfield, R.E.4    Hendrickson, W.A.5
  • 6
    • 0026800851 scopus 로고
    • Intracellular folding pathway of human chorionic gonadotropin beta subunit
    • Huth, J. R., Mountjoy, K., Perini, F., and Ruddon, R. W. (1992) Intracellular folding pathway of human chorionic gonadotropin beta subunit, J. Biol. Chem. 267, 8870-8879.
    • (1992) J. Biol. Chem. , vol.267 , pp. 8870-8879
    • Huth, J.R.1    Mountjoy, K.2    Perini, F.3    Ruddon, R.W.4
  • 7
    • 0026786419 scopus 로고
    • Kinetics of folding and assembly of the human chorionic gonadotropin beta subunit in transfected Chinese hamster ovary cells
    • Bedows, E., Huth, J. R., and Ruddon, R. W. (1992) Kinetics of folding and assembly of the human chorionic gonadotropin beta subunit in transfected Chinese hamster ovary cells, J. Biol. Chem. 267, 8880-8886.
    • (1992) J. Biol. Chem. , vol.267 , pp. 8880-8886
    • Bedows, E.1    Huth, J.R.2    Ruddon, R.W.3
  • 8
    • 0027156984 scopus 로고
    • Disulfide bond mutations affect the folding of the human chorionic gonadotropin-beta subunit in transfected Chinese hamster ovary cells
    • Bedows, E., Huth, J. R., Suganuma, N., Bartels, C. F., Boime, I., and Ruddon, R. W. (1993) Disulfide bond mutations affect the folding of the human chorionic gonadotropin-beta subunit in transfected Chinese hamster ovary cells, J. Biol. Chem. 268, 11655-11662.
    • (1993) J. Biol. Chem. , vol.268 , pp. 11655-11662
    • Bedows, E.1    Huth, J.R.2    Suganuma, N.3    Bartels, C.F.4    Boime, I.5    Ruddon, R.W.6
  • 9
    • 0026786741 scopus 로고
    • Domain-dependent protein folding is indicated by the intracellular kinetics of disulfide bond formation of human chorionic gonadotropin beta subunit
    • Huth, J. R., Mountjoy, K., Perini, F., Bedows, E., and Ruddon, R. W. (1992) Domain-dependent protein folding is indicated by the intracellular kinetics of disulfide bond formation of human chorionic gonadotropin beta subunit, J. Biol. Chem. 267, 21396-21403.
    • (1992) J. Biol. Chem. , vol.267 , pp. 21396-21403
    • Huth, J.R.1    Mountjoy, K.2    Perini, F.3    Bedows, E.4    Ruddon, R.W.5
  • 10
    • 0036481738 scopus 로고    scopus 로고
    • Comparison of chorionic gonadotropin expression in human and macaque (Macaca fascicularis) trophoblasts
    • Wilken, J. A., Matsumoto, K., Laughlin, L. S., Lasley, B. L., and Bedows, E. (2002) Comparison of chorionic gonadotropin expression in human and macaque (Macaca fascicularis) trophoblasts, Am. J. Primatol. 56, 89-97.
    • (2002) Am. J. Primatol. , vol.56 , pp. 89-97
    • Wilken, J.A.1    Matsumoto, K.2    Laughlin, L.S.3    Lasley, B.L.4    Bedows, E.5
  • 11
    • 2142844350 scopus 로고    scopus 로고
    • Chorionic gonadotropin: Structure-activity relationships of a cystine knot-containing hormone
    • Bedows, E. (2002) Chorionic gonadotropin: Structure-activity relationships of a cystine knot-containing hormone, Recent Res. Dev. Endocrinol. 3, 235-247.
    • (2002) Recent Res. Dev. Endocrinol. , vol.3 , pp. 235-247
    • Bedows, E.1
  • 12
    • 0036215657 scopus 로고    scopus 로고
    • Role of disulphide bond formation in folding, secrefion, and assembly of human chorionic gonadotropin subunits
    • Bedows, E., Darling, R. J., Wilken, J. A., and Sherman, S. A. (2002) Role of disulphide bond formation in folding, secrefion, and assembly of human chorionic gonadotropin subunits, Indian J. Exp. Biol. 40, 467-476.
    • (2002) Indian J. Exp. Biol. , vol.40 , pp. 467-476
    • Bedows, E.1    Darling, R.J.2    Wilken, J.A.3    Sherman, S.A.4
  • 13
    • 0027236954 scopus 로고
    • Production of high-titer helper-free retroviruses by transient transfection
    • Pear, W. S., Nolan, G. P., Scott, M. L., and Baltimore, D. (1993) Production of high-titer helper-free retroviruses by transient transfection, Proc. Natl. Acad. Sci. U.S.A. 90, 8392-8396.
    • (1993) Proc. Natl. Acad. Sci. U.S.A. , vol.90 , pp. 8392-8396
    • Pear, W.S.1    Nolan, G.P.2    Scott, M.L.3    Baltimore, D.4
  • 14
    • 0034686019 scopus 로고    scopus 로고
    • Cystine knot mutafions affect the folding of the glycoprotein hormone alpha-subunit. Differential secretion and assembly of partially folded intermediates
    • Darling, R. J., Ruddon, R. W., Perini, F., and Bedows, E. (2000) Cystine knot mutafions affect the folding of the glycoprotein hormone alpha-subunit. Differential secretion and assembly of partially folded intermediates, J. Biol. Chem. 275, 15413-15421.
    • (2000) J. Biol. Chem. , vol.275 , pp. 15413-15421
    • Darling, R.J.1    Ruddon, R.W.2    Perini, F.3    Bedows, E.4
  • 15
    • 0031054145 scopus 로고    scopus 로고
    • A single amino acid substitution, Gly 117His, confers phosphotriesterase (organophosphorus acid anhydride hydrolase) activity on human butyrylcholinesterase
    • Lockridge, O., Blong, R. M., Masson, P., Froment, M. T., Millard, C. B., and Broomfield, C. A. (1997) A single amino acid substitution, Gly 117His, confers phosphotriesterase (organophosphorus acid anhydride hydrolase) activity on human butyrylcholinesterase, Biochemistry 36, 786-795.
    • (1997) Biochemistry , vol.36 , pp. 786-795
    • Lockridge, O.1    Blong, R.M.2    Masson, P.3    Froment, M.T.4    Millard, C.B.5    Broomfield, C.A.6
  • 16
    • 1842831872 scopus 로고    scopus 로고
    • Identification of Phosphorylation Sites by Edman Degradation
    • Steinke, L., and Cook, R. G. (2003) Identification of Phosphorylation Sites by Edman Degradation, Methods Mol. Biol. 211, 301-307.
    • (2003) Methods Mol. Biol. , vol.211 , pp. 301-307
    • Steinke, L.1    Cook, R.G.2
  • 17
    • 0032230333 scopus 로고    scopus 로고
    • Dissociation of early folding events from assembly of the human lutropin beta-subunit
    • Muyan, M., Ruddon, R. W., Norton, S. E., Boime, I., and Bedows, E. (1998) Dissociation of early folding events from assembly of the human lutropin beta-subunit, Mol. Endocrinol. 12, 1640-1649.
    • (1998) Mol. Endocrinol. , vol.12 , pp. 1640-1649
    • Muyan, M.1    Ruddon, R.W.2    Norton, S.E.3    Boime, I.4    Bedows, E.5
  • 18
    • 0033305129 scopus 로고    scopus 로고
    • A naturally occurring genetic variant in the human chorionic gonadotropin-beta gene 5 is assembly inefficient
    • Miller-Lindholm, A. K., Bedows, E., Bartels, C. F., Ramey, J., Maclin, V., and Ruddon, R. W. (1999) A naturally occurring genetic variant in the human chorionic gonadotropin-beta gene 5 is assembly inefficient, Endocrinology 140, 3496-3506.
    • (1999) Endocrinology , vol.140 , pp. 3496-3506
    • Miller-Lindholm, A.K.1    Bedows, E.2    Bartels, C.F.3    Ramey, J.4    Maclin, V.5    Ruddon, R.W.6
  • 19
    • 0027182764 scopus 로고
    • Protein folding and assembly in vitro parallel intracellular folding and assembly. Catalysis of folding and assembly of the human chorionic gonadotropin alpha beta dimer by protein disulfide isomerase
    • Huth, J. R., Perini, F., Lockridge, O., Bedows, E., and Ruddon, R. W. (1993) Protein folding and assembly in vitro parallel intracellular folding and assembly. Catalysis of folding and assembly of the human chorionic gonadotropin alpha beta dimer by protein disulfide isomerase, J. Biol. Chem. 268, 16472-16482.
    • (1993) J. Biol. Chem. , vol.268 , pp. 16472-16482
    • Huth, J.R.1    Perini, F.2    Lockridge, O.3    Bedows, E.4    Ruddon, R.W.5
  • 20
    • 0031572858 scopus 로고    scopus 로고
    • The crystal structure of vascular endothelial growth factor (VEGF) refined to 1.93 A resolution: Multiple copy flexibility and receptor binding
    • Muller, Y. A., Christinger, H. W., Keyt, B. A., and de Vos, A. M. (1997) The crystal structure of vascular endothelial growth factor (VEGF) refined to 1.93 A resolution: multiple copy flexibility and receptor binding, Structure 5, 1325-1338.
    • (1997) Structure , vol.5 , pp. 1325-1338
    • Muller, Y.A.1    Christinger, H.W.2    Keyt, B.A.3    De Vos, A.M.4
  • 21
    • 0028239914 scopus 로고
    • Misfolded human chorionic gonadotropin beta subunits are secreted from transfected Chinese hamster ovary cells
    • Bedows, E., Norton, S. E., Huth, J. R., Suganuma, N., Boime, I., and Ruddon, R. W. (1994) Misfolded human chorionic gonadotropin beta subunits are secreted from transfected Chinese hamster ovary cells, J. Biol. Chem. 269, 10574-10580.
    • (1994) J. Biol. Chem. , vol.269 , pp. 10574-10580
    • Bedows, E.1    Norton, S.E.2    Huth, J.R.3    Suganuma, N.4    Boime, I.5    Ruddon, R.W.6
  • 22
    • 0029780765 scopus 로고    scopus 로고
    • Novel covalent chaperone complexes associated with human chorionic gonadotropin beta subunit folding intermediates
    • Feng, W., Bedows, E., Norton, S. E., and Ruddon, R. W. (1996) Novel covalent chaperone complexes associated with human chorionic gonadotropin beta subunit folding intermediates, J. Biol. Chem. 271, 18543-18548.
    • (1996) J. Biol. Chem. , vol.271 , pp. 18543-18548
    • Feng, W.1    Bedows, E.2    Norton, S.E.3    Ruddon, R.W.4
  • 23
    • 0029040839 scopus 로고
    • The asparagine-linked oligosaccharides of the human chorionic gonadotropin beta subunit facilitate correct disulfide bond pairing
    • Feng, W., Matzuk, M. M., Mountjoy, K., Bedows, E., Ruddon, R. W., and Boime, I. (1995) The asparagine-linked oligosaccharides of the human chorionic gonadotropin beta subunit facilitate correct disulfide bond pairing, J. Biol. Chem. 270, 11851-11859.
    • (1995) J. Biol. Chem. , vol.270 , pp. 11851-11859
    • Feng, W.1    Matzuk, M.M.2    Mountjoy, K.3    Bedows, E.4    Ruddon, R.W.5    Boime, I.6
  • 24
    • 0030037083 scopus 로고    scopus 로고
    • Protein folding in the endoplasmic reticulum: Lessons from the human chorionic gonadotropin beta subunit
    • Ruddon, R. W., Sherman, S. A., and Bedows, E. (1996) Protein folding in the endoplasmic reticulum: lessons from the human chorionic gonadotropin beta subunit, Protein Sci. 5, 1443-1452.
    • (1996) Protein Sci. , vol.5 , pp. 1443-1452
    • Ruddon, R.W.1    Sherman, S.A.2    Bedows, E.3
  • 25
    • 0034644437 scopus 로고    scopus 로고
    • Folding studies on the human chorionic gonadotropin beta-subunit using optical spectroscopy of peptide fragments
    • Gangani, R. A., Silva, D., Sherman, S. A., Perini, F., Bedows, E., and Keiderling, T. A. (2000) Folding studies on the human chorionic gonadotropin beta-subunit using optical spectroscopy of peptide fragments, J. Am. Chem. Soc. 122, 8623-8630.
    • (2000) J. Am. Chem. Soc. , vol.122 , pp. 8623-8630
    • Gangani, R.A.1    Silva, D.2    Sherman, S.A.3    Perini, F.4    Bedows, E.5    Keiderling, T.A.6
  • 26
    • 0026666246 scopus 로고
    • Kinetic role of normative species in the folding of bovine pancreatic trypsin inhibitor
    • Weissman, J. S., and Kim, P. S. (1992) Kinetic role of normative species in the folding of bovine pancreatic trypsin inhibitor, Proc. Natl. Acad. Sci. U.S.A. 89, 9900-9904.
    • (1992) Proc. Natl. Acad. Sci. U.S.A. , vol.89 , pp. 9900-9904
    • Weissman, J.S.1    Kim, P.S.2
  • 27
    • 0017815610 scopus 로고
    • Experimental studies of protein folding and unfolding
    • Creighton, T. E. (1978) Experimental studies of protein folding and unfolding, Prog. Biophys. Mol. Biol. 33, 231-297.
    • (1978) Prog. Biophys. Mol. Biol. , vol.33 , pp. 231-297
    • Creighton, T.E.1
  • 28
    • 0025345415 scopus 로고
    • Intermediates in the folding reactions of small proteins
    • Kim, P. S., and Baldwin, R. L. (1990) Intermediates in the folding reactions of small proteins, Annu. Rev. Biochem. 59, 631-660.
    • (1990) Annu. Rev. Biochem. , vol.59 , pp. 631-660
    • Kim, P.S.1    Baldwin, R.L.2
  • 29
    • 0031030579 scopus 로고    scopus 로고
    • Assisted protein folding
    • Ruddon, R. W., and Bedows, E. (1997) Assisted protein folding, J. Biol. Chem. 272, 3125-3128.
    • (1997) J. Biol. Chem. , vol.272 , pp. 3125-3128
    • Ruddon, R.W.1    Bedows, E.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.