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Volumn 53, Issue 5, 2010, Pages 1917-1922

Direct determination of the insulin - insulin receptor interface using transferred cross-saturation experiments

Author keywords

[No Author keywords available]

Indexed keywords

INSULIN; INSULIN RECEPTOR;

EID: 77949386271     PISSN: 00222623     EISSN: 15204804     Source Type: Journal    
DOI: 10.1021/jm901099v     Document Type: Article
Times cited : (14)

References (38)
  • 1
    • 0028085078 scopus 로고
    • The insulin signaling system
    • Review
    • White, M. F.; Kahn, C. R. The insulin signaling system. J. Biol. Chem. 1994, 269, 1-4, Review.
    • (1994) J. Biol. Chem. , vol.269 , pp. 1-4
    • White, M.F.1    Kahn, C.R.2
  • 3
    • 0034719123 scopus 로고    scopus 로고
    • Mutational analysis of invariant valine B12 in insulin: Implications for receptor binding
    • Nakagawa, S. H.; Tager, H. S.; Steiner, D. F. Mutational analysis of invariant valine B12 in insulin: implications for receptor binding. Biochemistry 2000, 39, 15826-15835.
    • (2000) Biochemistry , vol.39 , pp. 15826-15835
    • Nakagawa, S.H.1    Tager, H.S.2    Steiner, D.F.3
  • 7
    • 3142579218 scopus 로고    scopus 로고
    • Diabetes-associated mutations in insulin: Consecutive residues in the B chain contact distinct domains of the insulin receptor
    • Xu, B.; Hu, S.; Chu, Y.; Huang, K.; Nakagawa, S. H.; Whittaker, J.; Katsoyannis, P. G.; Weiss, M. A. Diabetes-associated mutations in insulin: consecutive residues in the B chain contact distinct domains of the insulin receptor. Biochemistry 2004, 43, 8356-8372.
    • (2004) Biochemistry , vol.43 , pp. 8356-8372
    • Xu, B.1    Hu, S.2    Chu, Y.3    Huang, K.4    Nakagawa, S.H.5    Whittaker, J.6    Katsoyannis, P.G.7    Weiss, M.A.8
  • 8
    • 0016700342 scopus 로고
    • Is the evolution of insulin Darwinian or due to selectively neutral mutation?
    • Blundell, T. L.; Wood, S. P. Is the evolution of insulin Darwinian or due to selectively neutral mutation? Nature 1975, 257, 197-203.
    • (1975) Nature , vol.257 , pp. 197-203
    • Blundell, T.L.1    Wood, S.P.2
  • 10
    • 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 Discovery 2002, 1, 769-783.
    • (2002) Nat. Rev. Drug Discovery , vol.1 , pp. 769-783
    • De Meyts, P.1    Whittaker, J.2
  • 11
    • 48149095486 scopus 로고    scopus 로고
    • The insulin receptor: A prototype for dimeric, allosteric membrane receptors?
    • Review
    • De Meyts, P. The insulin receptor: a prototype for dimeric, allosteric membrane receptors? Trends Biochem. Sci. 2008, 33, 376-384, Review.
    • (2008) Trends Biochem. Sci. , vol.33 , pp. 376-384
    • De Meyts, P.1
  • 12
    • 0025880180 scopus 로고
    • X-ray analysis of the single chain B29-A1 peptide-linked insulin molecule: A completely inactive analogue
    • Derewenda, U.; Derewenda, Z.; Dodson, E. J.; Dodson, G. G.; Bing, X.; Markussen, J. X-ray analysis of the single chain B29-A1 peptide-linked insulin molecule: A completely inactive analogue. J. Mol. Biol. 1991, 220, 425-433.
    • (1991) J. Mol. Biol. , vol.220 , pp. 425-433
    • Derewenda, U.1    Derewenda, Z.2    Dodson, E.J.3    Dodson, G.G.4    Bing, X.5    Markussen, J.6
  • 13
    • 0025996911 scopus 로고
    • Receptor binding redefined by a structural switch in a mutant human insulin
    • Hua, Q. X.; Shoelson, S. E.; Kochoyan, M.; Weiss, M. A. Receptor binding redefined by a structural switch in a mutant human insulin. Nature 1991, 354, 238-241.
    • (1991) Nature , vol.354 , pp. 238-241
    • Hua, Q.X.1    Shoelson, S.E.2    Kochoyan, M.3    Weiss, M.A.4
  • 14
    • 0032577326 scopus 로고    scopus 로고
    • A structural switch in a mutant insulin exposes key residues for receptor binding
    • Ludvigsen, S.; Olsen, H. B.; Kaarsholm, N. C. A structural switch in a mutant insulin exposes key residues for receptor binding. J. Mol. Biol. 1998, 279, 1-7.
    • (1998) J. Mol. Biol. , vol.279 , pp. 1-7
    • Ludvigsen, S.1    Olsen, H.B.2    Kaarsholm, N.C.3
  • 15
    • 0028146822 scopus 로고
    • The structural basis of insulin and insulin-like growth factor-1 receptor binding and negative cooperativity, and its relevance to mitogenic versus metabolic signaling
    • De Meyts, P. The structural basis of insulin and insulin-like growth factor-1 receptor binding and negative cooperativity, and its relevance to mitogenic versus metabolic signaling. Diabetologia 1994, 57, S135-S148.
    • (1994) Diabetologia , vol.57
    • De Meyts, P.1
  • 16
    • 0028268592 scopus 로고
    • A model for insulin binding to the insulin receptor
    • Schärfer, L. A model for insulin binding to the insulin receptor. Eur. J. Biochem. 1994, 221, 1127-1132.
    • (1994) Eur. J. Biochem. , vol.221 , pp. 1127-1132
    • Schärfer, L.1
  • 19
    • 0036302354 scopus 로고    scopus 로고
    • Determination of the interface of a large protein complex by transferred cross-saturation measurements
    • Nakanishi, T.; Miyazawa, M.; Sakakura, M.; Terasawa, H.; Takahashi, H.; Shimada, I. Determination of the interface of a large protein complex by transferred cross-saturation measurements. J. Mol. Biol. 2002, 318, 245-249.
    • (2002) J. Mol. Biol. , vol.318 , pp. 245-249
    • Nakanishi, T.1    Miyazawa, M.2    Sakakura, M.3    Terasawa, H.4    Takahashi, H.5    Shimada, I.6
  • 20
    • 33645785076 scopus 로고    scopus 로고
    • Utilization of methyl proton resonances in cross-saturation measurement for determining the interfaces of large protein - Protein complexes
    • Takahashi, H.; Miyazawa, M.; Ina, Y.; Fukunishi, Y.; Mizukoshi, Y.; Nakamura, H.; Shimada, I. Utilization of methyl proton resonances in cross-saturation measurement for determining the interfaces of large protein - protein complexes. J. Biomol. NMR 2006, 34, 167-177.
    • (2006) J. Biomol. NMR , vol.34 , pp. 167-177
    • Takahashi, H.1    Miyazawa, M.2    Ina, Y.3    Fukunishi, Y.4    Mizukoshi, Y.5    Nakamura, H.6    Shimada, I.7
  • 21
    • 0029758766 scopus 로고    scopus 로고
    • Fusion of insulin receptor ectodomains to immunoglobulin constant domains reproduces high-affinity insulin binding in vitro
    • Bass, J.; Kurose, T.; Pashmforoush, M.; Steiner, D. F. Fusion of insulin receptor ectodomains to immunoglobulin constant domains reproduces high-affinity insulin binding in vitro. J. Biol. Chem. 1996, 271, 19367-19375.
    • (1996) J. Biol. Chem. , vol.271 , pp. 19367-19375
    • Bass, J.1    Kurose, T.2    Pashmforoush, M.3    Steiner, D.F.4
  • 22
    • 0036290185 scopus 로고    scopus 로고
    • Complete relaxation and conformational exchange matrix (CORECEMA) analysis of intermolecular saturation transfer effects in reversibly forming ligand - Receptor complexes
    • Jayalakshmi, V.; Krishna, N. R. Complete relaxation and conformational exchange matrix (CORECEMA) analysis of intermolecular saturation transfer effects in reversibly forming ligand - receptor complexes. J. Magn. Reson. 2002, 155, 106-118.
    • (2002) J. Magn. Reson. , vol.155 , pp. 106-118
    • Jayalakshmi, V.1    Krishna, N.R.2
  • 23
    • 0028241787 scopus 로고
    • Highresolution structure of an engineered biologically potent insulin monomer, B16 Tyr - His, as determined by nuclear magnetic resonance spectroscopy
    • Ludvigsen, S.; Roy, M.; Thogersen, H.; Kaarsholm, N. C. Highresolution structure of an engineered biologically potent insulin monomer, B16 Tyr - His, as determined by nuclear magnetic resonance spectroscopy. Biochemistry 1994, 33, 7998-8006.
    • (1994) Biochemistry , vol.33 , pp. 7998-8006
    • Ludvigsen, S.1    Roy, M.2    Thogersen, H.3    Kaarsholm, N.C.4
  • 26
    • 0030015918 scopus 로고    scopus 로고
    • Solution structure of an engineered insulin monomer at neutral pH
    • Olsen, H. B.; Ludvigsen, S.; Kaarsholm, N. C. Solution structure of an engineered insulin monomer at neutral pH. Biochemistry 1996, 35, 8836-8845.
    • (1996) Biochemistry , vol.35 , pp. 8836-8845
    • Olsen, H.B.1    Ludvigsen, S.2    Kaarsholm, N.C.3
  • 27
    • 0033117675 scopus 로고    scopus 로고
    • Streamlined procedure for the production of normal and altered versions of recombinant human proinsulin
    • Mackin, R. B. Streamlined procedure for the production of normal and altered versions of recombinant human proinsulin. Protein Expression Purif. 1999, 15, 308-313.
    • (1999) Protein Expression Purif. , vol.15 , pp. 308-313
    • Mackin, R.B.1
  • 29
    • 0037205766 scopus 로고    scopus 로고
    • NMR structure determination and investigation using a reduced proton (REDPRO) labeling strategy for proteins
    • Shekhtman, A.; Ghose, R.; Goger, M.; Cowburn, D. NMR structure determination and investigation using a reduced proton (REDPRO) labeling strategy for proteins. FEBS Lett. 2002, 524, 177-182.
    • (2002) FEBS Lett. , vol.524 , pp. 177-182
    • Shekhtman, A.1    Ghose, R.2    Goger, M.3    Cowburn, D.4
  • 32
    • 0028674451 scopus 로고
    • Multidimensional heteronuclear nuclear magnetic resonance of proteins
    • Clore, G. M.; Gronenborn, A. M. Multidimensional heteronuclear nuclear magnetic resonance of proteins. Methods Enzymol 1994, 239, 349-363.
    • (1994) Methods Enzymol , vol.239 , pp. 349-363
    • Clore, G.M.1    Gronenborn, A.M.2
  • 35
    • 0034051065 scopus 로고    scopus 로고
    • A novel NMR method for determining the interfaces of large proteinprotein complexes
    • Takahashi, H.; Nakanishi, T.; Kami, K.; Arata, Y.; Shimada, I. A novel NMR method for determining the interfaces of large proteinprotein complexes. Nat. Struct. Biol. 2000, 7, 220-223.
    • (2000) Nat. Struct. Biol. , vol.7 , pp. 220-223
    • Takahashi, H.1    Nakanishi, T.2    Kami, K.3    Arata, Y.4    Shimada, I.5
  • 37
    • 0034461768 scopus 로고    scopus 로고
    • Drug-like properties and the causes of poor solubility and poor permeability
    • Review
    • Lipinski, C. A. Drug-like properties and the causes of poor solubility and poor permeability. J. Pharmacol. Toxicol. Methods 2000, 44, 235-249, Review.
    • (2000) J. Pharmacol. Toxicol. Methods , vol.44 , pp. 235-249
    • Lipinski, C.A.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.