메뉴 건너뛰기




Volumn 22, Issue 5, 2012, Pages 158-166

The insulin-like growth factor mutation database (IGFmdb)

Author keywords

Binding affinity; IGF I; IGF II; IGFBP; Insulin; Insulin receptor; Insulin like growth factor; Mutation database; Type 1 insulin like growth factor receptor; Type 2 insulin like growth factor receptor

Indexed keywords

INSULIN DERIVATIVE; ISOPROTEIN; SOMATOMEDIN; SOMATOMEDIN B; SOMATOMEDIN C; SOMATOMEDIN C DERIVATIVE; SOMATOMEDIN C RECEPTOR;

EID: 84865396609     PISSN: 10966374     EISSN: 15322238     Source Type: Journal    
DOI: 10.1016/j.ghir.2012.05.001     Document Type: Article
Times cited : (9)

References (51)
  • 2
    • 1642401437 scopus 로고    scopus 로고
    • Laron syndrome (primary growth hormone resistance or insensitivity): the personal experience 1958-2003
    • Laron Z. Laron syndrome (primary growth hormone resistance or insensitivity): the personal experience 1958-2003. J. Clin. Endocrinol. Metab. 2004, 89:1031-1044.
    • (2004) J. Clin. Endocrinol. Metab. , vol.89 , pp. 1031-1044
    • Laron, Z.1
  • 3
    • 56749184290 scopus 로고    scopus 로고
    • Insulin and insulin-like growth factor signalling in neoplasia
    • Pollak M. Insulin and insulin-like growth factor signalling in neoplasia. Nat. Rev. Cancer 2008, 8:915-928.
    • (2008) Nat. Rev. Cancer , vol.8 , pp. 915-928
    • Pollak, M.1
  • 4
    • 65449168837 scopus 로고    scopus 로고
    • Ligand-induced activation of the insulin receptor: a multi-step process involving structural changes in both the ligand and the receptor
    • Ward C.W., Lawrence M.C. Ligand-induced activation of the insulin receptor: a multi-step process involving structural changes in both the ligand and the receptor. Bioessays 2009, 31:422-434.
    • (2009) Bioessays , vol.31 , pp. 422-434
    • Ward, C.W.1    Lawrence, M.C.2
  • 6
    • 84865389373 scopus 로고    scopus 로고
    • Insulin-like growth factor binding proteins: a structural perspective
    • Forbes B.E., McCarthy P., Norton R.S. Insulin-like growth factor binding proteins: a structural perspective. Front. Endocrin. 2012, 3(38):1-13.
    • (2012) Front. Endocrin. , vol.3 , Issue.38 , pp. 1-13
    • Forbes, B.E.1    McCarthy, P.2    Norton, R.S.3
  • 7
    • 0034916960 scopus 로고    scopus 로고
    • The acid-labile subunit (ALS) of the 150kDa IGF-binding protein complex: an important but forgotten component of the circulating IGF system
    • Boisclair Y.R., Rhoads R.P., Ueki I., Wang J., Ooi G.T. The acid-labile subunit (ALS) of the 150kDa IGF-binding protein complex: an important but forgotten component of the circulating IGF system. J. Endocrinol. 2001, 170:63-70.
    • (2001) J. Endocrinol. , vol.170 , pp. 63-70
    • Boisclair, Y.R.1    Rhoads, R.P.2    Ueki, I.3    Wang, J.4    Ooi, G.T.5
  • 8
    • 0036782071 scopus 로고    scopus 로고
    • Structural biology of insulin and IGF1 receptors: implications for drug design
    • De Meyts P., Whittaker J. Structural biology of insulin and IGF1 receptors: implications for drug design. Nat. Rev. Drug Discov. 2002, 1:769-783.
    • (2002) Nat. Rev. Drug Discov. , vol.1 , pp. 769-783
    • De Meyts, P.1    Whittaker, J.2
  • 10
    • 61349170301 scopus 로고    scopus 로고
    • Interactions of IGF-II with the IGF2R/cation-independent mannose-6-phosphate receptor mechanism and biological outcomes
    • Brown J., Jones E.Y., Forbes B.E. Interactions of IGF-II with the IGF2R/cation-independent mannose-6-phosphate receptor mechanism and biological outcomes. Vitam. Horm. 2009, 80:699-719.
    • (2009) Vitam. Horm. , vol.80 , pp. 699-719
    • Brown, J.1    Jones, E.Y.2    Forbes, B.E.3
  • 11
    • 70449806714 scopus 로고    scopus 로고
    • Keeping IGF-II under control: lessons from the IGF-II-IGF2R crystal structure
    • Brown J., Jones E.Y., Forbes B.E. Keeping IGF-II under control: lessons from the IGF-II-IGF2R crystal structure. Trends Biochem. Sci. 2009, 34:612-619.
    • (2009) Trends Biochem. Sci. , vol.34 , pp. 612-619
    • Brown, J.1    Jones, E.Y.2    Forbes, B.E.3
  • 12
    • 0024539198 scopus 로고
    • Alternative splicing of human insulin receptor messenger RNA
    • Seino S., Bell G.I. Alternative splicing of human insulin receptor messenger RNA. Biochem. Biophys. Res. Commun. 1989, 159:312-316.
    • (1989) Biochem. Biophys. Res. Commun. , vol.159 , pp. 312-316
    • Seino, S.1    Bell, G.I.2
  • 13
    • 0346095210 scopus 로고    scopus 로고
    • The insulin receptor isoform exon 11- (IR-A) in cancer and other diseases: a review
    • Denley A., Wallace J.C., Cosgrove L.J., Forbes B.E. The insulin receptor isoform exon 11- (IR-A) in cancer and other diseases: a review. Horm. Metab. Res. 2003, 35:778-785.
    • (2003) Horm. Metab. Res. , vol.35 , pp. 778-785
    • Denley, A.1    Wallace, J.C.2    Cosgrove, L.J.3    Forbes, B.E.4
  • 14
    • 0032932822 scopus 로고    scopus 로고
    • Insulin receptor isoform A, a newly recognized, high-affinity insulin-like growth factor II receptor in fetal and cancer cells
    • Frasca F., Pandini G., Scalia P., et al. Insulin receptor isoform A, a newly recognized, high-affinity insulin-like growth factor II receptor in fetal and cancer cells. Mol. Cell. Biol. 1999, 19:3278-3288.
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 3278-3288
    • Frasca, F.1    Pandini, G.2    Scalia, P.3
  • 15
    • 33748744723 scopus 로고    scopus 로고
    • Hybrid receptors formed by insulin receptor (IR) and insulin-like growth factor I receptor (IGF-IR) have low insulin and high IGF-1 affinity irrespective of the IR splice variant
    • Slaaby R., Schaffer L., Lautrup-Larsen I., et al. Hybrid receptors formed by insulin receptor (IR) and insulin-like growth factor I receptor (IGF-IR) have low insulin and high IGF-1 affinity irrespective of the IR splice variant. J. Biol. Chem. 2006, 281:25869-25874.
    • (2006) J. Biol. Chem. , vol.281 , pp. 25869-25874
    • Slaaby, R.1    Schaffer, L.2    Lautrup-Larsen, I.3
  • 16
    • 10844223660 scopus 로고    scopus 로고
    • Insulin and its receptor: structure, function and evolution
    • De Meyts P. Insulin and its receptor: structure, function and evolution. Bioessays 2004, 26:1351-1362.
    • (2004) Bioessays , vol.26 , pp. 1351-1362
    • De Meyts, P.1
  • 17
    • 33748639228 scopus 로고    scopus 로고
    • Structure of the insulin receptor ectodomain reveals a folded-over conformation
    • McKern N.M., Lawrence M.C., Streltsov V.A., et al. Structure of the insulin receptor ectodomain reveals a folded-over conformation. Nature 2006, 443:218-221.
    • (2006) Nature , vol.443 , pp. 218-221
    • McKern, N.M.1    Lawrence, M.C.2    Streltsov, V.A.3
  • 18
    • 77951058594 scopus 로고    scopus 로고
    • Structural resolution of a tandem hormone-binding element in the insulin receptor and its implications for design of peptide agonists
    • Smith B.J., Huang K., Kong G., et al. Structural resolution of a tandem hormone-binding element in the insulin receptor and its implications for design of peptide agonists. Proc. Natl. Acad. Sci. U. S. A. 2010, 107:6771-6776.
    • (2010) Proc. Natl. Acad. Sci. U. S. A. , vol.107 , pp. 6771-6776
    • Smith, B.J.1    Huang, K.2    Kong, G.3
  • 19
    • 60749092852 scopus 로고    scopus 로고
    • Harmonic oscillator model of the insulin and IGF1 receptors' allosteric binding and activation
    • Kiselyov V.V., Versteyhe S., Gauguin L., De Meyts P. Harmonic oscillator model of the insulin and IGF1 receptors' allosteric binding and activation. Mol. Syst. Biol. 2009, 5:1-12.
    • (2009) Mol. Syst. Biol. , vol.5 , pp. 1-12
    • Kiselyov, V.V.1    Versteyhe, S.2    Gauguin, L.3    De Meyts, P.4
  • 20
    • 77954387357 scopus 로고    scopus 로고
    • All-atom structural models for complexes of insulin-like growth factors IGF1 and IGF2 with their cognate receptor
    • Vashisth H., Abrams C.F. All-atom structural models for complexes of insulin-like growth factors IGF1 and IGF2 with their cognate receptor. J. Mol. Biol. 2010, 400:645-658.
    • (2010) J. Mol. Biol. , vol.400 , pp. 645-658
    • Vashisth, H.1    Abrams, C.F.2
  • 21
    • 77951214213 scopus 로고    scopus 로고
    • Docking of insulin to a structurally equilibrated insulin receptor ectodomain
    • Vashisth H., Abrams C.F. Docking of insulin to a structurally equilibrated insulin receptor ectodomain. Proteins 2010, 78:1531-1543.
    • (2010) Proteins , vol.78 , pp. 1531-1543
    • Vashisth, H.1    Abrams, C.F.2
  • 22
    • 72749113530 scopus 로고    scopus 로고
    • Structural basis of the aberrant receptor binding properties of hagfish and lamprey insulins
    • Sajid W., Holst P.A., Kiselyov V.V., et al. Structural basis of the aberrant receptor binding properties of hagfish and lamprey insulins. Biochemistry 2009, 48:11283-11295.
    • (2009) Biochemistry , vol.48 , pp. 11283-11295
    • Sajid, W.1    Holst, P.A.2    Kiselyov, V.V.3
  • 23
    • 0034974365 scopus 로고    scopus 로고
    • Evolution of the insulin molecule: insights into structure-activity and phylogenetic relationships
    • Conlon J.M. Evolution of the insulin molecule: insights into structure-activity and phylogenetic relationships. Peptides 2001, 22:1183-1193.
    • (2001) Peptides , vol.22 , pp. 1183-1193
    • Conlon, J.M.1
  • 24
    • 0023898621 scopus 로고
    • Structural analogs of human insulin-like growth factor I with reduced affinity for serum binding proteins and the type 2 insulin-like growth factor receptor
    • Bayne M.L., Applebaum J., Chicchi G.G., Hayes N.S., Green B.G., Cascieri M.A. Structural analogs of human insulin-like growth factor I with reduced affinity for serum binding proteins and the type 2 insulin-like growth factor receptor. J. Biol. Chem. 1988, 263:6233-6239.
    • (1988) J. Biol. Chem. , vol.263 , pp. 6233-6239
    • Bayne, M.L.1    Applebaum, J.2    Chicchi, G.G.3    Hayes, N.S.4    Green, B.G.5    Cascieri, M.A.6
  • 25
    • 0024322899 scopus 로고
    • The C region of human insulin-like growth factor (IGF) I is required for high affinity binding to the type 1 IGF receptor
    • Bayne M.L., Applebaum J., Underwood D., et al. The C region of human insulin-like growth factor (IGF) I is required for high affinity binding to the type 1 IGF receptor. J. Biol. Chem. 1989, 264:11004-11008.
    • (1989) J. Biol. Chem. , vol.264 , pp. 11004-11008
    • Bayne, M.L.1    Applebaum, J.2    Underwood, D.3
  • 26
    • 0025840174 scopus 로고
    • The design, expression, and characterization of human insulin-like growth factor II (IGF-II) mutants specific for either the IGF-II/cation-independent mannose 6-phosphate receptor or IGF-I receptor
    • Sakano K., Enjoh T., Numata F., et al. The design, expression, and characterization of human insulin-like growth factor II (IGF-II) mutants specific for either the IGF-II/cation-independent mannose 6-phosphate receptor or IGF-I receptor. J. Biol. Chem. 1991, 266:20626-20635.
    • (1991) J. Biol. Chem. , vol.266 , pp. 20626-20635
    • Sakano, K.1    Enjoh, T.2    Numata, F.3
  • 27
    • 65549110812 scopus 로고    scopus 로고
    • A novel approach to identify two distinct receptor binding surfaces of insulin-like growth factor II
    • Alvino C.L., McNeil K.A., Ong S.C., et al. A novel approach to identify two distinct receptor binding surfaces of insulin-like growth factor II. J. Biol. Chem. 2009, 284:7656-7664.
    • (2009) J. Biol. Chem. , vol.284 , pp. 7656-7664
    • Alvino, C.L.1    McNeil, K.A.2    Ong, S.C.3
  • 28
    • 48149095541 scopus 로고    scopus 로고
    • Alanine scanning of a putative receptor binding surface of insulin-like growth factor-I
    • Gauguin L., Delaine C., Alvino C.L., et al. Alanine scanning of a putative receptor binding surface of insulin-like growth factor-I. J. Biol. Chem. 2008, 283:20821-20829.
    • (2008) J. Biol. Chem. , vol.283 , pp. 20821-20829
    • Gauguin, L.1    Delaine, C.2    Alvino, C.L.3
  • 29
    • 41449090278 scopus 로고    scopus 로고
    • Structural basis for the lower affinity of the insulin-like growth factors for the insulin receptor
    • Gauguin L., Klaproth B., Sajid W., et al. Structural basis for the lower affinity of the insulin-like growth factors for the insulin receptor. J. Biol. Chem. 2008, 283:2604-2613.
    • (2008) J. Biol. Chem. , vol.283 , pp. 2604-2613
    • Gauguin, L.1    Klaproth, B.2    Sajid, W.3
  • 30
    • 34547131599 scopus 로고    scopus 로고
    • A novel binding site for the human insulin-like growth factor-II (IGF-II)/mannose 6-phosphate receptor on IGF-II
    • Delaine C., Alvino C.L., McNeil K.A., et al. A novel binding site for the human insulin-like growth factor-II (IGF-II)/mannose 6-phosphate receptor on IGF-II. J. Biol. Chem. 2007, 282:18886-18894.
    • (2007) J. Biol. Chem. , vol.282 , pp. 18886-18894
    • Delaine, C.1    Alvino, C.L.2    McNeil, K.A.3
  • 31
    • 38049009418 scopus 로고    scopus 로고
    • Structure and functional analysis of the IGF-II/IGF2R interaction
    • Brown J., Delaine C., Zaccheo O.J., et al. Structure and functional analysis of the IGF-II/IGF2R interaction. EMBO J. 2008, 27:265-276.
    • (2008) EMBO J. , vol.27 , pp. 265-276
    • Brown, J.1    Delaine, C.2    Zaccheo, O.J.3
  • 32
    • 80055089655 scopus 로고    scopus 로고
    • Molecular mechanisms underlying insulin-like growth factor action: how mutations in the GH: IGF axis lead to short stature
    • Forbes B.E. Molecular mechanisms underlying insulin-like growth factor action: how mutations in the GH: IGF axis lead to short stature. Pediatr. Endocrinol. Rev. 2011, 8:374-381.
    • (2011) Pediatr. Endocrinol. Rev. , vol.8 , pp. 374-381
    • Forbes, B.E.1
  • 33
    • 20044391594 scopus 로고    scopus 로고
    • Structural and functional characteristics of the Val44Met insulin-like growth factor I missense mutation: correlation with effects on growth and development
    • Denley A., Wang C.C., McNeil K.A., et al. Structural and functional characteristics of the Val44Met insulin-like growth factor I missense mutation: correlation with effects on growth and development. Mol. Endocrinol. 2005, 19:711-721.
    • (2005) Mol. Endocrinol. , vol.19 , pp. 711-721
    • Denley, A.1    Wang, C.C.2    McNeil, K.A.3
  • 34
    • 70349898604 scopus 로고    scopus 로고
    • Partial primary deficiency of insulin-like growth factor (IGF)-I activity associated with IGF1 mutation demonstrates its critical role in growth and brain development
    • Netchine I., Azzi S., Houang M., et al. Partial primary deficiency of insulin-like growth factor (IGF)-I activity associated with IGF1 mutation demonstrates its critical role in growth and brain development. J. Clin. Endocrinol. Metab. 2009, 94:3913-3921.
    • (2009) J. Clin. Endocrinol. Metab. , vol.94 , pp. 3913-3921
    • Netchine, I.1    Azzi, S.2    Houang, M.3
  • 35
    • 0034908554 scopus 로고    scopus 로고
    • Nomenclature for the description of human sequence variations
    • den Dunnen J.T., Antonarakis S.E. Nomenclature for the description of human sequence variations. Hum. Genet. 2001, 109:121-124.
    • (2001) Hum. Genet. , vol.109 , pp. 121-124
    • den Dunnen, J.T.1    Antonarakis, S.E.2
  • 36
    • 0041571486 scopus 로고    scopus 로고
    • Complex with a phage display-derived peptide provides insight into the function of insulin-like growth factor I
    • Schaffer M.L., Deshayes K., Nakamura G., Sidhu S., Skelton N.J. Complex with a phage display-derived peptide provides insight into the function of insulin-like growth factor I. Biochemistry 2003, 42:9324-9334.
    • (2003) Biochemistry , vol.42 , pp. 9324-9334
    • Schaffer, M.L.1    Deshayes, K.2    Nakamura, G.3    Sidhu, S.4    Skelton, N.J.5
  • 37
    • 0029059589 scopus 로고
    • Solution structure of human insulin-like growth factor II. Relationship to receptor and binding protein interactions
    • Torres A.M., Forbes B.E., Aplin S.E., Wallace J.C., Francis G.L., Norton R.S. Solution structure of human insulin-like growth factor II. Relationship to receptor and binding protein interactions. J. Mol. Biol. 1995, 248:385-401.
    • (1995) J. Mol. Biol. , vol.248 , pp. 385-401
    • Torres, A.M.1    Forbes, B.E.2    Aplin, S.E.3    Wallace, J.C.4    Francis, G.L.5    Norton, R.S.6
  • 38
    • 33748367666 scopus 로고    scopus 로고
    • Structural basis for the inhibition of insulin-like growth factors by insulin-like growth factor-binding proteins
    • Sitar T., Popowicz G.M., Siwanowicz I., Huber R., Holak T.A. Structural basis for the inhibition of insulin-like growth factors by insulin-like growth factor-binding proteins. Proc. Natl. Acad. Sci. U. S. A. 2006, 103:13028-13033.
    • (2006) Proc. Natl. Acad. Sci. U. S. A. , vol.103 , pp. 13028-13033
    • Sitar, T.1    Popowicz, G.M.2    Siwanowicz, I.3    Huber, R.4    Holak, T.A.5
  • 39
    • 0034885755 scopus 로고    scopus 로고
    • Stimulation of human extravillous trophoblast migration by IGF-II is mediated by IGF type 2 receptor involving inhibitory G protein(s) and phosphorylation of MAPK
    • McKinnon T., Chakraborty C., Gleeson L.M., Chidiac P., Lala P.K. Stimulation of human extravillous trophoblast migration by IGF-II is mediated by IGF type 2 receptor involving inhibitory G protein(s) and phosphorylation of MAPK. J. Clin. Endocrinol. Metab. 2001, 86:3665-3674.
    • (2001) J. Clin. Endocrinol. Metab. , vol.86 , pp. 3665-3674
    • McKinnon, T.1    Chakraborty, C.2    Gleeson, L.M.3    Chidiac, P.4    Lala, P.K.5
  • 40
    • 0141706853 scopus 로고    scopus 로고
    • Urokinase type plasminogen activator receptor is involved in insulin-like growth factor-induced migration of rhabdomyosarcoma cells in vitro
    • Gallicchio M.A., Kaun C., Wojta J., Binder B., Bach L.A. Urokinase type plasminogen activator receptor is involved in insulin-like growth factor-induced migration of rhabdomyosarcoma cells in vitro. J. Cell. Physiol. 2003, 197:131-138.
    • (2003) J. Cell. Physiol. , vol.197 , pp. 131-138
    • Gallicchio, M.A.1    Kaun, C.2    Wojta, J.3    Binder, B.4    Bach, L.A.5
  • 41
    • 0026343776 scopus 로고
    • Mutants of human insulin-like growth factor II: expression and characterization of analogs with a substitution of TYR27 and/or a deletion of residues 62-67
    • Roth B.V., Burgisser D.M., Luthi C., Humbel R.E. Mutants of human insulin-like growth factor II: expression and characterization of analogs with a substitution of TYR27 and/or a deletion of residues 62-67. Biochem. Biophys. Res. Commun. 1991, 181:907-914.
    • (1991) Biochem. Biophys. Res. Commun. , vol.181 , pp. 907-914
    • Roth, B.V.1    Burgisser, D.M.2    Luthi, C.3    Humbel, R.E.4
  • 42
    • 0026808908 scopus 로고
    • The insulin-like growth factor II (IGF-II)/mannose 6-phosphate receptor mediates IGF-II-induced motility in human rhabdomyosarcoma cells
    • Minniti C.P., Kohn E.C., Grubb J.H., et al. The insulin-like growth factor II (IGF-II)/mannose 6-phosphate receptor mediates IGF-II-induced motility in human rhabdomyosarcoma cells. J. Biol. Chem. 1992, 267:9000-9004.
    • (1992) J. Biol. Chem. , vol.267 , pp. 9000-9004
    • Minniti, C.P.1    Kohn, E.C.2    Grubb, J.H.3
  • 43
    • 59449088639 scopus 로고    scopus 로고
    • Endothelial progenitor cell homing: prominent role of the IGF2-IGF2R-PLCbeta2 axis
    • Maeng Y.S., Choi H.J., Kwon J.Y., et al. Endothelial progenitor cell homing: prominent role of the IGF2-IGF2R-PLCbeta2 axis. Blood 2009, 113:233-243.
    • (2009) Blood , vol.113 , pp. 233-243
    • Maeng, Y.S.1    Choi, H.J.2    Kwon, J.Y.3
  • 44
    • 34548856208 scopus 로고    scopus 로고
    • The insulin-like growth factor type 1 and insulin-like growth factor type 2/mannose-6-phosphate receptors independently regulate ERK1/2 activity in HEK293 cells
    • El-Shewy H.M., Lee M.H., Obeid L.M., Jaffa A.A., Luttrell L.M. The insulin-like growth factor type 1 and insulin-like growth factor type 2/mannose-6-phosphate receptors independently regulate ERK1/2 activity in HEK293 cells. J. Biol. Chem. 2007, 282:26150-26157.
    • (2007) J. Biol. Chem. , vol.282 , pp. 26150-26157
    • El-Shewy, H.M.1    Lee, M.H.2    Obeid, L.M.3    Jaffa, A.A.4    Luttrell, L.M.5
  • 45
    • 82055194400 scopus 로고    scopus 로고
    • Phospholipase C and protein kinase C-beta 2 mediate insulin-like growth factor II-dependent sphingosine kinase 1 activation
    • El-Shewy H.M., Abdel-Samie S.A., Al Qalam A.M., et al. Phospholipase C and protein kinase C-beta 2 mediate insulin-like growth factor II-dependent sphingosine kinase 1 activation. Mol. Endocrinol. 2011, 25:2144-2156.
    • (2011) Mol. Endocrinol. , vol.25 , pp. 2144-2156
    • El-Shewy, H.M.1    Abdel-Samie, S.A.2    Al Qalam, A.M.3
  • 46
    • 17644365138 scopus 로고    scopus 로고
    • Chemokines, sphingosine-1-phosphate, and cell migration in secondary lymphoid organs
    • Cyster J.G. Chemokines, sphingosine-1-phosphate, and cell migration in secondary lymphoid organs. Annu. Rev. Immunol. 2005, 23:127-159.
    • (2005) Annu. Rev. Immunol. , vol.23 , pp. 127-159
    • Cyster, J.G.1
  • 47
    • 0027746313 scopus 로고
    • Synthesis and characterization of IGF-II analogs: applications in the evaluation of IGF receptor function and IGF-independent actions of IGFBPs
    • Oh Y., Muller H.L., Zhang H., Ling N., Rosenfeld R.G. Synthesis and characterization of IGF-II analogs: applications in the evaluation of IGF receptor function and IGF-independent actions of IGFBPs. Adv. Exp. Med. Biol. 1993, 343:41-54.
    • (1993) Adv. Exp. Med. Biol. , vol.343 , pp. 41-54
    • Oh, Y.1    Muller, H.L.2    Zhang, H.3    Ling, N.4    Rosenfeld, R.G.5
  • 48
    • 0027160909 scopus 로고
    • Insulin-like growth factor (IGF)-II binding to IGF-binding proteins and IGF receptors is modified by deletion of the N-terminal hexapeptide or substitution of arginine for glutamate-6 in IGF-II
    • Francis G.L., Aplin S.E., Milner S.J., McNeil K.A., Ballard F.J., Wallace J.C. Insulin-like growth factor (IGF)-II binding to IGF-binding proteins and IGF receptors is modified by deletion of the N-terminal hexapeptide or substitution of arginine for glutamate-6 in IGF-II. Biochem. J. 1993, 293:713-719.
    • (1993) Biochem. J. , vol.293 , pp. 713-719
    • Francis, G.L.1    Aplin, S.E.2    Milner, S.J.3    McNeil, K.A.4    Ballard, F.J.5    Wallace, J.C.6
  • 49
    • 0027175177 scopus 로고
    • Binding of mutants of human insulin-like growth factor II to insulin-like growth factor binding proteins 1-6
    • Bach L.A., Hsieh S., Sakano K., Fujiwara H., Perdue J.F., Rechler M.M. Binding of mutants of human insulin-like growth factor II to insulin-like growth factor binding proteins 1-6. J. Biol. Chem. 1993, 268:9246-9254.
    • (1993) J. Biol. Chem. , vol.268 , pp. 9246-9254
    • Bach, L.A.1    Hsieh, S.2    Sakano, K.3    Fujiwara, H.4    Perdue, J.F.5    Rechler, M.M.6
  • 50
    • 2942596337 scopus 로고    scopus 로고
    • Binding site for the C-domain of insulin-like growth factor (IGF) binding protein-6 on IGF-II; implications for inhibition of IGF actions
    • Headey S.J., Keizer D.W., Yao S., Wallace J.C., Bach L.A., Norton R.S. Binding site for the C-domain of insulin-like growth factor (IGF) binding protein-6 on IGF-II; implications for inhibition of IGF actions. FEBS Lett. 2004, 568:19-22.
    • (2004) FEBS Lett. , vol.568 , pp. 19-22
    • Headey, S.J.1    Keizer, D.W.2    Yao, S.3    Wallace, J.C.4    Bach, L.A.5    Norton, R.S.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.