메뉴 건너뛰기




Volumn 17, Issue 7, 2003, Pages 1192-1202

Structural analysis of yoked chorionic gonadotropin-luteinizing hormone receptor ectodomain complexes by circular dichroic spectroscopy

Author keywords

[No Author keywords available]

Indexed keywords

CHORIONIC GONADOTROPIN; CHORIONIC GONADOTROPIN RECEPTOR; HYBRID PROTEIN; LUTEINIZING HORMONE RECEPTOR;

EID: 0037634482     PISSN: 08888809     EISSN: None     Source Type: Journal    
DOI: 10.1210/me.2002-0349     Document Type: Article
Times cited : (10)

References (50)
  • 1
    • 0031916977 scopus 로고    scopus 로고
    • The luteinizing hormone receptor
    • Dufau ML 1998 The luteinizing hormone receptor. Annu Rev Physiol 60:461-496
    • (1998) Annu Rev Physiol , vol.60 , pp. 461-496
    • Dufau, M.L.1
  • 2
    • 0036217072 scopus 로고    scopus 로고
    • The lutropin/choriogonadotropin receptor, a 2002 perspective
    • Ascoli M, Fanelli F, Segaloff DL 2002 The lutropin/choriogonadotropin receptor, a 2002 perspective. Endocr Rev 23:141-174
    • (2002) Endocr Rev , vol.23 , pp. 141-174
    • Ascoli, M.1    Fanelli, F.2    Segaloff, D.L.3
  • 3
    • 0033829535 scopus 로고    scopus 로고
    • Molecular architecture and biorecognition processes of the cystine knot protein superfamily: Part I. The glycoprotein hormones
    • Hearn MT, Gomme PT 2000 Molecular architecture and biorecognition processes of the cystine knot protein superfamily: part I. The glycoprotein hormones. J Mol Recognit 13:223-278
    • (2000) J Mol Recognit , vol.13 , pp. 223-278
    • Hearn, M.T.1    Gomme, P.T.2
  • 4
    • 0028773646 scopus 로고
    • Structure of human chorionic gonadotropin at 2.6 Å resolution from MAD analysis of the selenomethionyl protein
    • Wu H, Lustbader JW, Liu Y, Canfield RE, Hendrickson WA 1994 Structure of human chorionic gonadotropin at 2.6 Å resolution 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
    • 0035105355 scopus 로고    scopus 로고
    • Three-dimensional structure of human follicle-stimulating hormone
    • Fox KM, Dias JA, Van Roey P 2001 Three-dimensional structure of human follicle-stimulating hormone. Mol Endocrinol 15:378-389
    • (2001) Mol Endocrinol , vol.15 , pp. 378-389
    • Fox, K.M.1    Dias, J.A.2    Van Roey, P.3
  • 7
    • 0025646717 scopus 로고
    • Extracellular domain of lutropin/choriogonadotropin receptor expressed in transfected cells binds choriogonadotropin with high affinity
    • Xie YB, Wang H, Segaloff DL 1990 Extracellular domain of lutropin/choriogonadotropin receptor expressed in transfected cells binds choriogonadotropin with high affinity. J Biol Chem 265:21411-21414
    • (1990) J Biol Chem , vol.265 , pp. 21411-21414
    • Xie, Y.B.1    Wang, H.2    Segaloff, D.L.3
  • 8
    • 0029093909 scopus 로고
    • Model of human chorionic gonadotropin and lutropin receptor interaction that explains signal transduction of the glycoprotein hormones
    • Moyle WR, Campbell RK, Rao SN, Ayad NG, Bernard MP, Han Y, Wang Y 1995 Model of human chorionic gonadotropin and lutropin receptor interaction that explains signal transduction of the glycoprotein hormones. J Biol Chem 270:20020-20031
    • (1995) J Biol Chem , vol.270 , pp. 20020-20031
    • Moyle, W.R.1    Campbell, R.K.2    Rao, S.N.3    Ayad, N.G.4    Bernard, M.P.5    Han, Y.6    Wang, Y.7
  • 9
    • 0029646089 scopus 로고
    • Structural predictions for the ligand-binding region of glycoprotein hormone receptors and the nature of hormone-receptor interactions
    • Jiang X, Dreano M, Buckler DR, Cheng S, Ythier A, Wu H, Hendrickson WA, el Tayar N 1995 Structural predictions for the ligand-binding region of glycoprotein hormone receptors and the nature of hormone-receptor interactions. Structure 3:1341-1353
    • (1995) Structure , vol.3 , pp. 1341-1353
    • Jiang, X.1    Dreano, M.2    Buckler, D.R.3    Cheng, S.4    Ythier, A.5    Wu, H.6    Hendrickson, W.A.7    El Tayar, N.8
  • 10
    • 0029757509 scopus 로고    scopus 로고
    • Determination of residues important in hormone binding to the extracellular domain of the luteinizing hormone/chorionic gonadotropin receptor by site-directed mutagenesis and modeling
    • Bhowmick N, Huang J, Puett D, Isaacs NW, Lapthorn AJ 1996 Determination of residues important in hormone binding to the extracellular domain of the luteinizing hormone/chorionic gonadotropin receptor by site-directed mutagenesis and modeling. Mol Endocrinol 10:1147-1159
    • (1996) Mol Endocrinol , vol.10 , pp. 1147-1159
    • Bhowmick, N.1    Huang, J.2    Puett, D.3    Isaacs, N.W.4    Lapthorn, A.J.5
  • 11
    • 0035692811 scopus 로고    scopus 로고
    • The leucine-rich repeat as a protein recognition motif
    • Kobe B, Kajava AV 2001 The leucine-rich repeat as a protein recognition motif. Curr Opin Struct Biol 11:725-732
    • (2001) Curr Opin Struct Biol , vol.11 , pp. 725-732
    • Kobe, B.1    Kajava, A.V.2
  • 12
    • 0033304846 scopus 로고    scopus 로고
    • Identification of ionizable amino acid residues on the extracellular domain of the lutropin receptor involved in ligand binding
    • Bhowmick N, Narayan P, Puett D 1999 Identification of ionizable amino acid residues on the extracellular domain of the lutropin receptor involved in ligand binding. Endocrinology 140:4558-4563
    • (1999) Endocrinology , vol.140 , pp. 4558-4563
    • Bhowmick, N.1    Narayan, P.2    Puett, D.3
  • 13
    • 0035793620 scopus 로고    scopus 로고
    • Hormone interactions to Leu-rich repeats in the gonadotropin receptors. I. Analysis of Leu-rich repeats of human luteinizing hormone/chorionic gonadotropin receptor and follicle-stimulating hormone receptor
    • Song YS, Ji I, Beauchamp J, Isaacs NW, Ji TH 2001 Hormone interactions to Leu-rich repeats in the gonadotropin receptors. I. Analysis of Leu-rich repeats of human luteinizing hormone/chorionic gonadotropin receptor and follicle-stimulating hormone receptor. J Biol Chem 276:3426-3435
    • (2001) J Biol Chem , vol.276 , pp. 3426-3435
    • Song, Y.S.1    Ji, I.2    Beauchamp, J.3    Isaacs, N.W.4    Ji, T.H.5
  • 14
    • 0026724205 scopus 로고
    • Receptor-binding regions in human glycoprotein hormones
    • Keutmann HT 1992 Receptor-binding regions in human glycoprotein hormones. Mol Cell Endocrinol 86:C1-C6
    • (1992) Mol Cell Endocrinol , vol.86
    • Keutmann, H.T.1
  • 15
    • 0026778135 scopus 로고
    • Identification of hormone-binding regions of the luteinizing hormone/human chorionic gonadotropin receptor using synthetic peptides
    • Roche PC, Ryan RJ, McCormick DJ 1992 Identification of hormone-binding regions of the luteinizing hormone/human chorionic gonadotropin receptor using synthetic peptides. Endocrinology 131:268-274
    • (1992) Endocrinology , vol.131 , pp. 268-274
    • Roche, P.C.1    Ryan, R.J.2    McCormick, D.J.3
  • 16
    • 0025847496 scopus 로고
    • Amino-terminal leucine-rich repeats in gonadotropin receptors determine hormone selectivity
    • Braun T, Schofield PR, Sprengel R 1991 Amino-terminal leucine-rich repeats in gonadotropin receptors determine hormone selectivity. EMBO J 10:1885-1890
    • (1991) EMBO J , vol.10 , pp. 1885-1890
    • Braun, T.1    Schofield, P.R.2    Sprengel, R.3
  • 17
    • 0032577468 scopus 로고    scopus 로고
    • The amino-terminal region of the luteinizing hormone/choriogonadotropin receptor contacts both subunits of human choriogonadotropin. I. Mutational analysis
    • Hong S, Phang T, Ji I, Ji TH 1998 The amino-terminal region of the luteinizing hormone/choriogonadotropin receptor contacts both subunits of human choriogonadotropin. I. Mutational analysis. J Biol Chem 273:13835-13840
    • (1998) J Biol Chem , vol.273 , pp. 13835-13840
    • Hong, S.1    Phang, T.2    Ji, I.3    Ji, T.H.4
  • 18
    • 0029948074 scopus 로고    scopus 로고
    • Mutational analyses of the extracellular domain of the full-length lutropin/choriogonadotropin receptor suggest leucine-rich repeats 1-6 are involved in hormone binding
    • Thomas D, Rozell TG, Liu X, Segaloff DL 1996 Mutational analyses of the extracellular domain of the full-length lutropin/choriogonadotropin receptor suggest leucine-rich repeats 1-6 are involved in hormone binding. Mol Endocrinol 10:760-768
    • (1996) Mol Endocrinol , vol.10 , pp. 760-768
    • Thomas, D.1    Rozell, T.G.2    Liu, X.3    Segaloff, D.L.4
  • 19
    • 0035025154 scopus 로고    scopus 로고
    • High-level bacterial expression of a natively folded, soluble extracellular domain fusion protein of the human luteinizing hormone/chorionic gonadotropin receptor in the cytoplasm of Escherichia coli
    • Lobel LI, Pollak S, Klein J, Lustbader JW 2001 High-level bacterial expression of a natively folded, soluble extracellular domain fusion protein of the human luteinizing hormone/chorionic gonadotropin receptor in the cytoplasm of Escherichia coli. Endocrine 14:205-212
    • (2001) Endocrine , vol.14 , pp. 205-212
    • Lobel, L.I.1    Pollak, S.2    Klein, J.3    Lustbader, J.W.4
  • 20
    • 0035910404 scopus 로고    scopus 로고
    • Purification and structural analysis of a soluble human chorionogonadotropin hormone-receptor complex
    • Remy JJ, Nespoulous C, Grosclaude J, Grebert D, Couture L, Pajot E, Salesse R 2001 Purification and structural analysis of a soluble human chorionogonadotropin hormone-receptor complex. J Biol Chem 276:1681-1687
    • (2001) J Biol Chem , vol.276 , pp. 1681-1687
    • Remy, J.J.1    Nespoulous, C.2    Grosclaude, J.3    Grebert, D.4    Couture, L.5    Pajot, E.6    Salesse, R.7
  • 21
    • 0035046135 scopus 로고    scopus 로고
    • High-level expression of a functional single-chain human chorionic gonadotropin-luteinizing hormone receptor ectodomain complex in insect cells
    • Fralish GB, Narayan P, Puett D 2001 High-level expression of a functional single-chain human chorionic gonadotropin-luteinizing hormone receptor ectodomain complex in insect cells. Endocrinology 142:1517-1524
    • (2001) Endocrinology , vol.142 , pp. 1517-1524
    • Fralish, G.B.1    Narayan, P.2    Puett, D.3
  • 22
    • 0028882196 scopus 로고
    • Functional expression of yoked human chorionic gonadotropin in baculovirus-infected insect cells
    • Narayan P, Wu C, Puett D 1995 Functional expression of yoked human chorionic gonadotropin in baculovirus-infected insect cells. Mol Endocrinol 9:1720-1726
    • (1995) Mol Endocrinol , vol.9 , pp. 1720-1726
    • Narayan, P.1    Wu, C.2    Puett, D.3
  • 23
    • 0029856730 scopus 로고    scopus 로고
    • Protein engineering of a novel constitutively active hormone-receptor complex
    • Wu C, Narayan P, Puett D 1996 Protein engineering of a novel constitutively active hormone-receptor complex. J Biol Chem 271:31638-31642
    • (1996) J Biol Chem , vol.271 , pp. 31638-31642
    • Wu, C.1    Narayan, P.2    Puett, D.3
  • 24
    • 85047681976 scopus 로고    scopus 로고
    • A biologically active single chain human chorionic gonadotropin analog with altered receptor binding properties
    • Narayan P, Gray J, Puett D 2000 A biologically active single chain human chorionic gonadotropin analog with altered receptor binding properties. Endocrinology 141:67-71
    • (2000) Endocrinology , vol.141 , pp. 67-71
    • Narayan, P.1    Gray, J.2    Puett, D.3
  • 26
    • 0025201419 scopus 로고
    • Intronic nature of the rat luteinizing hormone receptor gene defines a soluble receptor subspecies with hormone binding activity
    • Tsai-Morris CH, Buczko E, Wang W, Dufau ML 1990 Intronic nature of the rat luteinizing hormone receptor gene defines a soluble receptor subspecies with hormone binding activity. J Biol Chem 265:19385-19388
    • (1990) J Biol Chem , vol.265 , pp. 19385-19388
    • Tsai-Morris, C.H.1    Buczko, E.2    Wang, W.3    Dufau, M.L.4
  • 27
    • 0027458346 scopus 로고
    • High expression of the hormone binding active extracellular domain (1-294) of rat lutropin receptor in Escherichia coli
    • Chen W, Bahl OP 1993 High expression of the hormone binding active extracellular domain (1-294) of rat lutropin receptor in Escherichia coli. Mol Cell Endocrinol 91:35-41
    • (1993) Mol Cell Endocrinol , vol.91 , pp. 35-41
    • Chen, W.1    Bahl, O.P.2
  • 28
    • 0029094166 scopus 로고
    • Functional glycosylation sites of the rat luteinizing hormone receptor required for ligand binding
    • Zhang R, Cai H, Fatima N, Buczko E, Dufau ML 1995 Functional glycosylation sites of the rat luteinizing hormone receptor required for ligand binding. J Biol Chem 270:21722-21728
    • (1995) J Biol Chem , vol.270 , pp. 21722-21728
    • Zhang, R.1    Cai, H.2    Fatima, N.3    Buczko, E.4    Dufau, M.L.5
  • 29
    • 0033304617 scopus 로고    scopus 로고
    • The β-subunit of human choriogonadotropin interacts with the exodomain of the luteinizing hormone/choriogonadotropin receptor and changes its interaction with the α-subunit
    • Hong SH, Ji IH, Ji TH 1999 The β-subunit of human choriogonadotropin interacts with the exodomain of the luteinizing hormone/choriogonadotropin receptor and changes its interaction with the α-subunit. Mol Endocrinol 13:1285-1294
    • (1999) Mol Endocrinol , vol.13 , pp. 1285-1294
    • Hong, S.H.1    Ji, I.H.2    Ji, T.H.3
  • 30
    • 0035793543 scopus 로고    scopus 로고
    • The role of the hinge region of the luteinizing hormone receptor in hormone interaction and signal generation
    • Zeng H, Phang T, Song YS, Ji I, Ji TH 2001 The role of the hinge region of the luteinizing hormone receptor in hormone interaction and signal generation. J Biol Chem 276:3451-3458
    • (2001) J Biol Chem , vol.276 , pp. 3451-3458
    • Zeng, H.1    Phang, T.2    Song, Y.S.3    Ji, I.4    Ji, T.H.5
  • 31
    • 0030042763 scopus 로고    scopus 로고
    • Methods to estimate the conformation of proteins and polypeptides from circular dichroism data
    • Greenfield NJ 1996 Methods to estimate the conformation of proteins and polypeptides from circular dichroism data. Anal Biochem 235:1-10
    • (1996) Anal Biochem , vol.235 , pp. 1-10
    • Greenfield, N.J.1
  • 32
    • 0019873820 scopus 로고
    • Estimation of globular protein secondary structure from circular dichroism
    • Provencher SW, Glockner J 1981 Estimation of globular protein secondary structure from circular dichroism. Biochemistry 20:33-37
    • (1981) Biochemistry , vol.20 , pp. 33-37
    • Provencher, S.W.1    Glockner, J.2
  • 33
    • 0027988296 scopus 로고
    • Protein secondary structure from circular dichroism spectroscopy. Combining variable selection principle and cluster analysis with neural network, ridge regression and self-consistent methods
    • Sreerama N, Woody RW 1994 Protein secondary structure from circular dichroism spectroscopy. Combining variable selection principle and cluster analysis with neural network, ridge regression and self-consistent methods. J Mol Biol 242:497-507
    • (1994) J Mol Biol , vol.242 , pp. 497-507
    • Sreerama, N.1    Woody, R.W.2
  • 34
    • 0027447099 scopus 로고
    • A self-consistent method for the analysis of protein secondary structure from circular dichroism
    • Sreerama N, Woody RW 1993 A self-consistent method for the analysis of protein secondary structure from circular dichroism. Anal Biochem 209:32-44
    • (1993) Anal Biochem , vol.209 , pp. 32-44
    • Sreerama, N.1    Woody, R.W.2
  • 35
    • 0033042935 scopus 로고    scopus 로고
    • Estimation of the number of α-helical and β-strand segments in proteins using circular dichroism spectroscopy
    • Sreerama N, Venyaminov SY, Woody RW 1999 Estimation of the number of α-helical and β-strand segments in proteins using circular dichroism spectroscopy. Protein Sci 8:370-380
    • (1999) Protein Sci , vol.8 , pp. 370-380
    • Sreerama, N.1    Venyaminov, S.Y.2    Woody, R.W.3
  • 36
    • 0035968185 scopus 로고    scopus 로고
    • Hormone-induced conformational change of the purified soluble hormone binding domain of follitropin receptor complexed with single chain follitropin
    • Schmidt A, MacColl R, Lindau-Shepard B, Buckler DR, Dias JA 2001 Hormone-induced conformational change of the purified soluble hormone binding domain of follitropin receptor complexed with single chain follitropin. J Biol Chem 276:23373-23381
    • (2001) J Biol Chem , vol.276 , pp. 23373-23381
    • Schmidt, A.1    MacColl, R.2    Lindau-Shepard, B.3    Buckler, D.R.4    Dias, J.A.5
  • 37
    • 0019871893 scopus 로고
    • Information content in the circular dichroism of proteins
    • Hennessey Jr JP, Johnson Jr WC 1981 Information content in the circular dichroism of proteins. Biochemistry 20:1085-1094
    • (1981) Biochemistry , vol.20 , pp. 1085-1094
    • Hennessey J.P., Jr.1    Johnson W.C., Jr.2
  • 38
    • 0016763284 scopus 로고
    • Gonadotropin and subunit conformation
    • Holladay LA, Puett D 1975 Gonadotropin and subunit conformation. Arch Biochem Biophys 171:708-720
    • (1975) Arch Biochem Biophys , vol.171 , pp. 708-720
    • Holladay, L.A.1    Puett, D.2
  • 40
    • 0024893140 scopus 로고
    • Helix formation in reduced, S-carboxymethylated human choriogonadotropin β sub-unit and tryptic peptides
    • Puett D, Birken S 1989 Helix formation in reduced, S-carboxymethylated human choriogonadotropin β sub-unit and tryptic peptides. J Protein Chem 8:779-794
    • (1989) J Protein Chem , vol.8 , pp. 779-794
    • Puett, D.1    Birken, S.2
  • 41
    • 0020328269 scopus 로고
    • Circular dichroic and immunological properties of human choriogonadotropin-β carboxyl terminal peptides
    • Puett D, Ryan RJ, Stevens VC 1982 Circular dichroic and immunological properties of human choriogonadotropin-β carboxyl terminal peptides. Int J Pept Protein Res 19:506-513
    • (1982) Int J Pept Protein Res , vol.19 , pp. 506-513
    • Puett, D.1    Ryan, R.J.2    Stevens, V.C.3
  • 42
    • 0037384140 scopus 로고    scopus 로고
    • Consequences of single chain translation on the structure of two chorionic gonadotropin yoked analogs in α-β and β-α configurations
    • Fralish GB, Narayan P, Puett D 2003 Consequences of single chain translation on the structure of two chorionic gonadotropin yoked analogs in α-β and β-α configurations. Mol Endocrinol 17:757-767
    • (2003) Mol Endocrinol , vol.17 , pp. 757-767
    • Fralish, G.B.1    Narayan, P.2    Puett, D.3
  • 43
    • 0028097211 scopus 로고
    • Hormone-binding properties and glycosylation pattern of a recombinant form of the extracellular domain of the luteinizing hormone/chorionic gonadotropin receptor expressed in mammalian cells
    • Thomas DM, Segaloff DL 1994 Hormone-binding properties and glycosylation pattern of a recombinant form of the extracellular domain of the luteinizing hormone/chorionic gonadotropin receptor expressed in mammalian cells. Endocrinology 135:1902-1912
    • (1994) Endocrinology , vol.135 , pp. 1902-1912
    • Thomas, D.M.1    Segaloff, D.L.2
  • 44
    • 0037040202 scopus 로고    scopus 로고
    • The ectodomain of the luteinizing hormone receptor interacts with exoloop 2 to constrain the transmembrane region: Studies using chimeric human and fly receptors
    • Nishi S, Nakabayashi K, Kobilka B, Hsueh AJ 2002 The ectodomain of the luteinizing hormone receptor interacts with exoloop 2 to constrain the transmembrane region: studies using chimeric human and fly receptors. J Biol Chem 277:3958-3964
    • (2002) J Biol Chem , vol.277 , pp. 3958-3964
    • Nishi, S.1    Nakabayashi, K.2    Kobilka, B.3    Hsueh, A.J.4
  • 45
    • 0033054119 scopus 로고    scopus 로고
    • Characterization of a region of the lutropin receptor extracellular domain near transmembrane helix 1 that is important in ligand-mediated signaling
    • Alvarez CA, Narayan P, Huang J, Puett D 1999 Characterization of a region of the lutropin receptor extracellular domain near transmembrane helix 1 that is important in ligand-mediated signaling. Endocrinology 140:1775-1782
    • (1999) Endocrinology , vol.140 , pp. 1775-1782
    • Alvarez, C.A.1    Narayan, P.2    Huang, J.3    Puett, D.4
  • 46
    • 0034730516 scopus 로고    scopus 로고
    • Activation of the luteinizing hormone receptor following substitution of Ser-277 with selective hydrophobic residues in the ectodomain hinge region
    • Nakabayashi K, Kudo M, Kobilka B, Hsueh AJ 2000 Activation of the luteinizing hormone receptor following substitution of Ser-277 with selective hydrophobic residues in the ectodomain hinge region. J Biol Chem 275:30264-30271
    • (2000) J Biol Chem , vol.275 , pp. 30264-30271
    • Nakabayashi, K.1    Kudo, M.2    Kobilka, B.3    Hsueh, A.J.4
  • 47
    • 0034457935 scopus 로고    scopus 로고
    • The extracellular domain suppresses constitutive activity of the transmembrane domain of the human TSH receptor: Implications for hormone-receptor interaction and antagonist design
    • Zhang M, Tong KP, Fremont V, Chen J, Narayan P, Puett D, Weintraub BD, Szkudlinski MW 2000 The extracellular domain suppresses constitutive activity of the transmembrane domain of the human TSH receptor: implications for hormone-receptor interaction and antagonist design. Endocrinology 141:3514-3517
    • (2000) Endocrinology , vol.141 , pp. 3514-3517
    • Zhang, M.1    Tong, K.P.2    Fremont, V.3    Chen, J.4    Narayan, P.5    Puett, D.6    Weintraub, B.D.7    Szkudlinski, M.W.8
  • 48
    • 0035839426 scopus 로고    scopus 로고
    • The position of the α and β subunits in a single chain variant of human chorionic gonadotropin affects the heterodimeric interaction of the subunits and receptor-binding epitopes
    • Ben-Menahem D, Jablonka-Shariff A, Hyde RK, Pixley MR, Srivastava S, Berger P, Boime I 2001 The position of the α and β subunits in a single chain variant of human chorionic gonadotropin affects the heterodimeric interaction of the subunits and receptor-binding epitopes. J Biol Chem 276:29871-29879
    • (2001) J Biol Chem , vol.276 , pp. 29871-29879
    • Ben-Menahem, D.1    Jablonka-Shariff, A.2    Hyde, R.K.3    Pixley, M.R.4    Srivastava, S.5    Berger, P.6    Boime, I.7
  • 49
    • 0033310391 scopus 로고    scopus 로고
    • The biological action of choriogonadotropin is not dependent on the complete native quaternary interactions between the subunits
    • Jackson AM, Berger P, Pixley M, Klein C, Hsueh AJ, Boime I 1999 The biological action of choriogonadotropin is not dependent on the complete native quaternary interactions between the subunits. Mol Endocrinol 13:2175-2188
    • (1999) Mol Endocrinol , vol.13 , pp. 2175-2188
    • Jackson, A.M.1    Berger, P.2    Pixley, M.3    Klein, C.4    Hsueh, A.J.5    Boime, I.6
  • 50
    • 0024448151 scopus 로고
    • Calculation of protein extinction coefficients from amino acid sequence data
    • Gill SC, von Hippel PH 1989 Calculation of protein extinction coefficients from amino acid sequence data. Anal Biochem 182:319-326
    • (1989) Anal Biochem , vol.182 , pp. 319-326
    • Gill, S.C.1    Von Hippel, P.H.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.