메뉴 건너뛰기




Volumn 111, Issue 33, 2014, Pages

Protective hinge in insulin opens to enable its receptor engagement

(21)  Menting, John G a   Yang, Yanwu b   Chan, Shu Jin c   Phillips, Nelson B b   Smith, Brian J d   Whittaker, Jonathan b   Wickramasinghe, Nalinda P b   Whittaker, Linda J b   Pandyarajan, Vijay b   Wan, Zhu Li b   Yadav, Satya P e   Carroll, Julie M f   Strokes, Natalie b   Roberts Jr , Charles T f,g   Ismail Beigi, Faramarz b   Milewski, Wieslawa c   Steiner, Donald F c   Chauhan, Virander S h   Ward, Colin W a   Weiss, Michael A b,i   more..


Author keywords

Diabetes mellitus; Metabolism; Protein structure; Receptor tyrosine kinase; Signal transduction

Indexed keywords

ALANINE; INSULIN; INSULIN DERIVATIVE; INSULIN RECEPTOR; ISOLEUCINE; PHENYLALANINE; SOMATOMEDIN; TYROSINE; VALINE;

EID: 84906306629     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1412897111     Document Type: Article
Times cited : (134)

References (71)
  • 1
    • 0000557482 scopus 로고
    • Structure of rhombohedral 2 zinc insulin crystals
    • Adams MJ, et al. (1969) Structure of rhombohedral 2 zinc insulin crystals. Nature 224(5218):491-495.
    • (1969) Nature , vol.224 , Issue.5218 , pp. 491-495
    • Adams, M.J.1
  • 2
    • 0024280106 scopus 로고
    • The structure of 2Zn pig insulin crystals at 1.5 A resolution
    • Baker EN, et al. (1988) The structure of 2Zn pig insulin crystals at 1.5 A resolution. Philos Trans R Soc Lond B Biol Sci 319(1195):369-456.
    • (1988) Philos Trans R Soc Lond B Biol Sci , vol.319 , Issue.1195 , pp. 369-456
    • Baker, E.N.1
  • 3
    • 0025880180 scopus 로고
    • X-ray analysis of the single chain B29-A1 peptide-linked insulin molecule. A completely inactive analogue
    • Derewenda U, et al. (1991) X-ray analysis of the single chain B29-A1 peptide-linked insulin molecule. A completely inactive analogue. J Mol Biol 220(2):425-433.
    • (1991) J Mol Biol , vol.220 , Issue.2 , pp. 425-433
    • Derewenda, U.1
  • 4
    • 0025978173 scopus 로고
    • Importance of the character and configuration of residues B24, B25, and B26 in insulin-receptor interactions
    • Mirmira RG, Nakagawa SH, Tager HS (1991) Importance of the character and configuration of residues B24, B25, and B26 in insulin-receptor interactions. J Biol Chem 266(3):1428-1436. (Pubitemid 21908320)
    • (1991) Journal of Biological Chemistry , vol.266 , Issue.3 , pp. 1428-1436
    • Mirmira, R.G.1    Nakagawa, S.H.2    Tager, H.S.3
  • 5
    • 0025996911 scopus 로고
    • Receptor binding redefined by a structural switch in a mutant human insulin
    • Hua QX, Shoelson SE, Kochoyan M, Weiss MA (1991) Receptor binding redefined by a structural switch in a mutant human insulin. Nature 354(6350):238-241. (Pubitemid 21896824)
    • (1991) Nature , vol.354 , Issue.6350 , pp. 238-241
    • Hua, Q.X.1    Shoelson, S.E.2    Kochoyan, M.3    Weiss, M.A.4
  • 6
    • 67649811215 scopus 로고    scopus 로고
    • Enhancing the activity of a protein by stereospecific unfolding: Conformational life cycleof insulin and its evolutionary origins
    • Hua QX, et al. (2009) Enhancing the activity of a protein by stereospecific unfolding: Conformational life cycleof insulin and its evolutionary origins. J Biol Chem 284(21):14586-14596.
    • (2009) J Biol Chem , vol.284 , Issue.21 , pp. 14586-14596
    • Hua, Q.X.1
  • 7
    • 0020532391 scopus 로고
    • Three mutant insulins in man
    • Shoelson S, et al. (1983) Three mutant insulins in man. Nature 302(5908):540-543. (Pubitemid 13111141)
    • (1983) Nature , vol.302 , Issue.5908 , pp. 540-543
    • Shoelson, S.1    Haneda, M.2    Blix, P.3
  • 8
    • 67649827251 scopus 로고    scopus 로고
    • Decoding the cryptic active conformation of a protein by synthetic photoscanning: Insulin inserts a detachable arm between receptor domains
    • Xu B, et al. (2009) Decoding the cryptic active conformation of a protein by synthetic photoscanning: Insulin inserts a detachable arm between receptor domains. J Biol Chem 284(21):14597-14608.
    • (2009) J Biol Chem , vol.284 , Issue.21 , pp. 14597-14608
    • Xu, B.1
  • 9
    • 0036782071 scopus 로고    scopus 로고
    • Structural biology of insulin and IGF1 receptors: Implications for drug design
    • DOI 10.1038/nrd917
    • De Meyts P, Whittaker J (2002) Structural biology of insulin and IGF1 receptors: implications for drug design. Nat Rev Drug Discov 1(10):769-783. (Pubitemid 37361561)
    • (2002) Nature Reviews Drug Discovery , vol.1 , Issue.10 , pp. 769-783
    • De Meyts, P.1    Whittaker, J.2
  • 10
    • 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 BJ, et al. (2010) Structural resolution of a tandem hormone-binding element in the insulin receptor and its implications for design of peptide agonists. Proc Natl Acad Sci USA 107(15):6771-6776.
    • (2010) Proc Natl Acad Sci USA , vol.107 , Issue.15 , pp. 6771-6776
    • Smith, B.J.1
  • 11
    • 84872162672 scopus 로고    scopus 로고
    • How insulin engages its primary binding site on the insulin receptor
    • Menting JG, et al. (2013) How insulin engages its primary binding site on the insulin receptor. Nature 493(7431):241-245.
    • (2013) Nature , vol.493 , Issue.7431 , pp. 241-245
    • Menting, J.G.1
  • 12
    • 49249126156 scopus 로고    scopus 로고
    • Dehydrophenylalanine (DeltaPhe) as a β breaker: Extended structure terminated by a DeltaPhe-induced turn in the pentapeptide Boc-Phe1-Ala2-Ile3- DeltaPhe4-Ala5-OMe
    • Gupta M, et al. (2008) Dehydrophenylalanine (DeltaPhe) as a β breaker: Extended structure terminated by a DeltaPhe-induced turn in the pentapeptide Boc-Phe1-Ala2-Ile3-DeltaPhe4-Ala5-OMe. ChemBioChem 9(9):1375-1378.
    • (2008) ChemBioChem , vol.9 , Issue.9 , pp. 1375-1378
    • Gupta, M.1
  • 13
    • 0021146005 scopus 로고
    • Changes in receptor binding, biological activity and immunoreactivity of insulin caused by replacing the residues B23- B26 with alanine
    • Kobayashi M, et al. (1984) Changes in receptor binding, biological activity and immunoreactivity of insulin caused by replacing the residues B23-B26 with alanine. Biomed Res 5(3):267-272. (Pubitemid 14010673)
    • (1984) Biomedical Research , vol.5 , Issue.3 , pp. 267-272
    • Kobayashi, M.1    Ohgaku, S.2    Iwasaki, M.3
  • 14
    • 33744834546 scopus 로고    scopus 로고
    • The relationship between the connecting peptide of recombined single chain insulin and its biological function
    • Huang Y, Liang Z, Feng Y (2001) The relationship between the connecting peptide of recombined single chain insulin and its biological function. Sci China C Life Sci 44(6):593-600.
    • (2001) Sci China C Life Sci , vol.44 , Issue.6 , pp. 593-600
    • Huang, Y.1    Liang, Z.2    Feng, Y.3
  • 16
    • 0030612833 scopus 로고    scopus 로고
    • Attenuated T2 relaxation by mutual cancellation of dipole-dipole coupling and chemical shift anisotropy indicates an avenue to NMR structures of very large biological macromolecules in solution
    • Pervushin K, Riek R, Wider G, Wüthrich K (1997) Attenuated T2 relaxation by mutual cancellation of dipole-dipole coupling and chemical shift anisotropy indicates an avenue to NMR structures of very large biological macromolecules in solution. Proc Natl Acad Sci USA 94(23):12366-12371.
    • (1997) Proc Natl Acad Sci USA , vol.94 , Issue.23 , pp. 12366-12371
    • Pervushin, K.1    Riek, R.2    Wider, G.3    Wüthrich, K.4
  • 18
    • 84861425552 scopus 로고    scopus 로고
    • Linking crystallographic model and data quality
    • Karplus PA, Diederichs K (2012) Linking crystallographic model and data quality. Science 336(6084):1030-1033.
    • (2012) Science , vol.336 , Issue.6084 , pp. 1030-1033
    • Karplus, P.A.1    Diederichs, K.2
  • 19
    • 6044221427 scopus 로고    scopus 로고
    • Exploiting the right side of the ramachandran plot: Substitution of glycines by D-alanine can significantly increase protein stability
    • DOI 10.1021/ja047119i
    • Anil B, Song B, Tang Y, Raleigh DP (2004) Exploiting the right side of the Ramachandran plot: Substitution of glycines by D-alanine can significantly increase protein stability. J Am Chem Soc 126(41):13194-13195. (Pubitemid 39382725)
    • (2004) Journal of the American Chemical Society , vol.126 , Issue.41 , pp. 13194-13195
    • Anil, B.1    Song, B.2    Tang, Y.3    Raleigh, D.P.4
  • 22
    • 77951214424 scopus 로고    scopus 로고
    • An Achilles' heel in an amyloidogenic protein and its repair: Insulin fibrillation and therapeutic design
    • Yang Y, et al. (2010) An Achilles' heel in an amyloidogenic protein and its repair: Insulin fibrillation and therapeutic design. J Biol Chem 285(14):10806-10821.
    • (2010) J Biol Chem , vol.285 , Issue.14 , pp. 10806-10821
    • Yang, Y.1
  • 23
    • 78650858133 scopus 로고    scopus 로고
    • De novo design of α,β-didehydrophenylalanine containing peptides: From models to applications
    • Gupta M, Chauhan VS (2011) De novo design of α,β- didehydrophenylalanine containing peptides: From models to applications. Biopolymers 95(3):161-173.
    • (2011) Biopolymers , vol.95 , Issue.3 , pp. 161-173
    • Gupta, M.1    Chauhan, V.S.2
  • 24
    • 77950915587 scopus 로고    scopus 로고
    • Solution structure of proinsulin: Connecting domain flexibility and prohormone processing
    • Yang Y, et al. (2010) Solution structure of proinsulin: Connecting domain flexibility and prohormone processing. J Biol Chem 285(11):7847-7851.
    • (2010) J Biol Chem , vol.285 , Issue.11 , pp. 7847-7851
    • Yang, Y.1
  • 27
    • 0035902492 scopus 로고    scopus 로고
    • Probing the mechanism of insulin fibril formation with insulin mutants
    • DOI 10.1021/bi0105983
    • Nielsen L, Frokjaer S, Brange J, Uversky VN, Fink AL (2001) Probing the mechanism of insulin fibril formation with insulin mutants. Biochemistry 40(28):8397-8409. (Pubitemid 32661900)
    • (2001) Biochemistry , vol.40 , Issue.28 , pp. 8397-8409
    • Nielsen, L.1    Frokjaer, S.2    Brange, J.3    Uversky, V.N.4    Fink, A.L.5
  • 29
    • 0347357617 scopus 로고    scopus 로고
    • Protein folding and misfolding
    • Dobson CM (2003) Protein folding and misfolding. Nature 426(6968):884-890.
    • (2003) Nature , vol.426 , Issue.6968 , pp. 884-890
    • Dobson, C.M.1
  • 30
    • 2442715309 scopus 로고    scopus 로고
    • Mechanism of insulin fibrillation: The structure of insulin under amyloidogenic conditions resembles a protein-folding intermediate
    • DOI 10.1074/jbc.M314141200
    • Hua QX, Weiss MA (2004) Mechanism of insulin fibrillation: The structure of insulin under amyloidogenic conditions resembles a protein-folding intermediate. J Biol Chem 279(20):21449-21460. (Pubitemid 38656555)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.20 , pp. 21449-21460
    • Hua, Q.-X.1    Weiss, M.A.2
  • 31
    • 0026548864 scopus 로고
    • Mutations at the dimer, hexamer, and receptor-binding surfaces of insulin independently affect insulin-insulin and insulin-receptor interactions
    • Shoelson SE, Lu ZX, Parlautan L, Lynch CS, Weiss MA (1992) Mutations at the dimer, hexamer, and receptor-binding surfaces of insulin independently affect insulin-insulin and insulin-receptor interactions. Biochemistry 31(6):1757-1767.
    • (1992) Biochemistry , vol.31 , Issue.6 , pp. 1757-1767
    • Shoelson, S.E.1    Lu, Z.X.2    Parlautan, L.3    Lynch, C.S.4    Weiss, M.A.5
  • 32
    • 29644434204 scopus 로고    scopus 로고
    • Proinsulin is refractory to protein fibrillation: Topological protection of a precursor protein from cross-β assembly
    • DOI 10.1074/jbc.M507110200
    • Huang K, Dong J, Phillips NB, Carey PR, Weiss MA (2005) Proinsulin is refractory to protein fibrillation: Topological protection of a precursor protein from cross-β assembly. J Biol Chem 280(51):42345-42355. (Pubitemid 43023206)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.51 , pp. 42345-42355
    • Huang, K.1    Dong, J.2    Phillips, N.B.3    Carey, P.R.4    Weiss, M.A.5
  • 33
    • 20444411501 scopus 로고    scopus 로고
    • Characterization of the functional insulin binding epitopes of the full-length insulin receptor
    • DOI 10.1074/jbc.M411320200
    • Whittaker J, Whittaker L (2005) Characterization of the functional insulin binding epitopes of the full-length insulin receptor. J Biol Chem 280(22):20932-20936. (Pubitemid 40805649)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.22 , pp. 20932-20936
    • Whittaker, J.1    Whittaker, L.2
  • 34
    • 0028980325 scopus 로고
    • Mapping of an NH2-terminal ligand binding site of the insulin receptor by alanine scanning mutagenesis
    • Williams PF, Mynarcik DC, Yu GQ, Whittaker J (1995) Mapping of an NH2-terminal ligand binding site of the insulin receptor by alanine scanning mutagenesis. J Biol Chem 270(7):3012-3016.
    • (1995) J Biol Chem , vol.270 , Issue.7 , pp. 3012-3016
    • Williams, P.F.1    Mynarcik, D.C.2    Yu, G.Q.3    Whittaker, J.4
  • 35
    • 0026046559 scopus 로고
    • Disposition of the phenylalanine B25 side chain during insulin-receptor and insulin-insulin interactions
    • Mirmira RG, Tager HS (1991) Disposition of the phenylalanine B25 side chain during insulin-receptor and insulin-insulin interactions. Biochemistry 30(33):8222-8229.
    • (1991) Biochemistry , vol.30 , Issue.33 , pp. 8222-8229
    • Mirmira, R.G.1    Tager, H.S.2
  • 38
    • 84878934226 scopus 로고    scopus 로고
    • Diabetes mellitus due to the toxic misfolding of proinsulin variants
    • Weiss MA (2013) Diabetes mellitus due to the toxic misfolding of proinsulin variants. FEBS Lett 587(13):1942-1950.
    • (2013) FEBS Lett , vol.587 , Issue.13 , pp. 1942-1950
    • Weiss, M.A.1
  • 39
    • 0032054714 scopus 로고    scopus 로고
    • The role of assembly in insulin's biosynthesis
    • DOI 10.1016/S0959-440X(98)80037-7
    • Dodson G, Steiner D (1998) The role of assembly in insulin's biosynthesis. Curr Opin Struct Biol 8(2):189-194. (Pubitemid 28221050)
    • (1998) Current Opinion in Structural Biology , vol.8 , Issue.2 , pp. 189-194
    • Dodson, G.1    Steiner, D.2
  • 40
    • 0022549577 scopus 로고
    • Diabetes due to secretion of a structurally abnormal insulin (insulin Wakayama). Clinical and functional characteristics of [Leu(A3)] insulin
    • Nanjo K, et al. (1986) Diabetes due to secretion of a structurally abnormal insulin (insulin Wakayama). Clinical and functional characteristics of [LeuA3] insulin. J Clin Invest 77(2):514-519. (Pubitemid 16037651)
    • (1986) Journal of Clinical Investigation , vol.77 , Issue.2 , pp. 514-519
    • Nanjo, K.1    Sanke, T.2    Miyano, M.3
  • 42
    • 0024553746 scopus 로고
    • Role of the phenylalanine B24 side chain in directing insulin interaction with its receptor. Importance of main chain conformation
    • Mirmira RG, Tager HS (1989) Role of the phenylalanine B24 side chain in directing insulin interaction with its receptor. Importance of main chain conformation. J Biol Chem 264(11):6349-6354. (Pubitemid 19106714)
    • (1989) Journal of Biological Chemistry , vol.264 , Issue.11 , pp. 6349-6354
    • Mirmira, R.G.1    Tager, H.S.2
  • 43
    • 84876262581 scopus 로고    scopus 로고
    • Structural integrity of the B24 site in human insulin is important for hormone functionality
    • Žáková L, et al. (2013) Structural integrity of the B24 site in human insulin is important for hormone functionality. J Biol Chem 288(15):10230-10240.
    • (2013) J Biol Chem , vol.288 , Issue.15 , pp. 10230-10240
    • Žáková, L.1
  • 44
    • 0028968018 scopus 로고
    • Studies on protein stability with T4 lysozyme
    • Matthews BW (1995) Studies on protein stability with T4 lysozyme. Adv Protein Chem 46:249-278.
    • (1995) Adv Protein Chem , vol.46 , pp. 249-278
    • Matthews, B.W.1
  • 45
    • 0032577326 scopus 로고    scopus 로고
    • A structural switch in a mutant insulin exposes key residues for receptor binding
    • DOI 10.1006/jmbi.1998.1801
    • Ludvigsen S, Olsen HB, Kaarsholm NC (1998) A structural switch in a mutant insulin exposes key residues for receptor binding. J Mol Biol 279(1):1-7. (Pubitemid 28252124)
    • (1998) Journal of Molecular Biology , vol.279 , Issue.1 , pp. 1-7
    • Ludvigsen, S.1    Olsen, H.B.2    Kaarsholm, N.C.3
  • 46
    • 0021341053 scopus 로고
    • Human insulin B24 (Phe - Ser). Secretion and metabolicclearance of the abnormal insulin in man and in a dog model
    • Shoelson SE, Polonsky KS, Zeidler A, Rubenstein AH, Tager HS (1984) Human insulin B24 (Phe-Ser). Secretion and metabolic clearance of the abnormal insulin in man and in a dog model. J Clin Invest 73(5):1351-1358. (Pubitemid 14139530)
    • (1984) Journal of Clinical Investigation , vol.73 , Issue.5 , pp. 1351-1358
    • Shoelson, S.E.1    Polonsky, K.S.2    Zeidler, A.3
  • 47
    • 0036782071 scopus 로고    scopus 로고
    • Structural biology of insulin and IGF1 receptors: Implications for drug design
    • DOI 10.1038/nrd917
    • De Meyts P, Whittaker J (2002) Structural biology of insulin and IGF1 receptors: Implications for drug design. Nat Rev Drug Discov 1(10):769-783. (Pubitemid 37361561)
    • (2002) Nature Reviews Drug Discovery , vol.1 , Issue.10 , pp. 769-783
    • De Meyts, P.1    Whittaker, J.2
  • 48
    • 0035909073 scopus 로고    scopus 로고
    • Crystal structure of human insulin-like growth factor-1: Detergent binding inhibits binding protein interactions
    • DOI 10.1021/bi0109111
    • Vajdos FF, et al. (2001) Crystal structure of human insulin-like growth factor-1: Detergent binding inhibits binding protein interactions. Biochemistry 40(37):11022-11029. (Pubitemid 32847968)
    • (2001) Biochemistry , vol.40 , Issue.37 , pp. 11022-11029
    • Vajdos, F.F.1    Ultsch, M.2    Schaffer, M.L.3    Deshayes, K.D.4    Liu, J.5    Skelton, N.J.6    De Vos, A.M.7
  • 52
    • 78149445119 scopus 로고    scopus 로고
    • Mutant INS-gene induced diabetes of youth: Proinsulin cysteine residues impose dominant-negative inhibition on wild-type proinsulin transport
    • Liu M, et al. (2010) Mutant INS-gene induced diabetes of youth: Proinsulin cysteine residues impose dominant-negative inhibition on wild-type proinsulin transport. PLoS ONE 5(10):e13333.
    • (2010) PLoS ONE , vol.5 , Issue.10
    • Liu, M.1
  • 54
    • 72149118250 scopus 로고    scopus 로고
    • An analytical solution to the kinetics of breakable filament assembly
    • Knowles TPJ, et al. (2009) An analytical solution to the kinetics of breakable filament assembly. Science 326(5959):1533-1537.
    • (2009) Science , vol.326 , Issue.5959 , pp. 1533-1537
    • Knowles, T.P.J.1
  • 55
    • 84874885410 scopus 로고    scopus 로고
    • Electrostatic effects in filamentous protein aggregation
    • Buell AK, et al. (2013) Electrostatic effects in filamentous protein aggregation. Biophys J 104(5):1116-1126.
    • (2013) Biophys J , vol.104 , Issue.5 , pp. 1116-1126
    • Buell, A.K.1
  • 56
    • 0025175762 scopus 로고
    • Cloning of complementary DNAs encoding islet amyloid polypeptide, insulin, and glucagon precursors from a New World rodent, the degu, Octodon degus
    • Nishi M, Steiner DF (1990) Cloning of complementary DNAs encoding islet amyloid polypeptide, insulin, and glucagon precursors from a New World rodent, the degu, Octodon degus. Mol Endocrinol 4(8):1192-1198.
    • (1990) Mol Endocrinol , vol.4 , Issue.8 , pp. 1192-1198
    • Nishi, M.1    Steiner, D.F.2
  • 58
    • 84863884698 scopus 로고    scopus 로고
    • α-Helical element at the hormone-binding surface of the insulin receptor functions as a signaling element to activate its tyrosine kinase
    • Whittaker J, et al. (2012) α-Helical element at the hormone-binding surface of the insulin receptor functions as a signaling element to activate its tyrosine kinase. Proc Natl Acad Sci USA 109(28):11166-11171.
    • (2012) Proc Natl Acad Sci USA , vol.109 , Issue.28 , pp. 11166-11171
    • Whittaker, J.1
  • 59
    • 0037166344 scopus 로고    scopus 로고
    • Functional reconstitution of insulin receptor binding site from non-binding receptor fragments
    • DOI 10.1074/jbc.M112249200
    • Kristensen C, Andersen AS, Ostergaard S, Hansen PH, Brandt J (2002) Functional reconstitution of insulin receptor binding site from non-binding receptor fragments. J Biol Chem 277(21):18340-18345. (Pubitemid 34952378)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.21 , pp. 18340-18345
    • Kristensen, C.1    Andersen, A.S.2    Ostergaard, S.3    Hansen, P.H.4    Brandt, J.5
  • 60
    • 57049086436 scopus 로고    scopus 로고
    • High-affinity insulin binding: Insulin interacts with two receptor ligand binding sites
    • Whittaker L, Hao C, Fu W, Whittaker J (2008) High-affinity insulin binding: Insulin interacts with two receptor ligand binding sites. Biochemistry 47(48):12900-12909.
    • (2008) Biochemistry , vol.47 , Issue.48 , pp. 12900-12909
    • Whittaker, L.1    Hao, C.2    Fu, W.3    Whittaker, J.4
  • 62
    • 0029400480 scopus 로고
    • NMRPipe: A multidimensional spectral processing system based on UNIX pipes
    • Delaglio F, et al. (1995) NMRPipe: A multidimensional spectral processing system based on UNIX pipes. J Biomol NMR 6(3):277-293.
    • (1995) J Biomol NMR , vol.6 , Issue.3 , pp. 277-293
    • Delaglio, F.1
  • 63
    • 0347383758 scopus 로고    scopus 로고
    • MODELLER: Generation and Refinement of Homology-Based Protein Structure Models
    • DOI 10.1016/S0076-6879(03)74020-8
    • Fiser A, Sali A (2003) Modeller: Generation and refinement of homology-based protein structure models. Methods Enzymol 374:461-491. (Pubitemid 37531821)
    • (2003) Methods in Enzymology , vol.374 , pp. 461-491
    • Fiser, A.1    Sali, A.2
  • 65
    • 46249092554 scopus 로고    scopus 로고
    • GROMACS 4: Algorithms for highly efficient, load-balanced, and scalable molecular simulation
    • Hess B, Kutzner C, Van Der Spoel D, Lindahl E (2008) GROMACS 4: Algorithms for highly efficient, load-balanced, and scalable molecular simulation. J Chem Theory Comput 4(3):435-447.
    • (2008) J Chem Theory Comput , vol.4 , Issue.3 , pp. 435-447
    • Hess, B.1    Kutzner, C.2    Van Der Spoel, D.3    Lindahl, E.4
  • 66
    • 33645941402 scopus 로고
    • The OPLS [optimized potentials for liquid simulations] potential functions for proteins, energy minimizations for crystals of cyclic peptides and crambin
    • Jorgensen WL, Tirado-Rives J (1988) The OPLS [optimized potentials for liquid simulations] potential functions for proteins, energy minimizations for crystals of cyclic peptides and crambin. J Am Chem Soc 110:1657-1666.
    • (1988) J Am Chem Soc , vol.110 , pp. 1657-1666
    • Jorgensen, W.L.1    Tirado-Rives, J.2
  • 69
    • 76649083949 scopus 로고    scopus 로고
    • Implications for the active form of human insulin based on the structural convergence of highly active hormone analogues
    • Jirácek J, et al. (2010) Implications for the active form of human insulin based on the structural convergence of highly active hormone analogues. Proc Natl Acad Sci USA 107(5):1966-1970.
    • (2010) Proc Natl Acad Sci USA , vol.107 , Issue.5 , pp. 1966-1970
    • Jirácek, J.1
  • 70
    • 47249140371 scopus 로고    scopus 로고
    • Design of an active ultrastable single-chain insulin analog: Synthesis, structure, and therapeutic implications
    • Hua QX, et al. (2008) Design of an active ultrastable single-chain insulin analog: Synthesis, structure, and therapeutic implications. J Biol Chem 283(21):14703-14716.
    • (2008) J Biol Chem , vol.283 , Issue.21 , pp. 14703-14716
    • Hua, Q.X.1
  • 71
    • 84865117076 scopus 로고    scopus 로고
    • Insulin fibrillation and protein design: Topological resistance of single-chain analogs to thermal degradation with application to a pump reservoir
    • Phillips NB, Whittaker J, Ismail-Beigi F, Weiss MA (2012) Insulin fibrillation and protein design: Topological resistance of single-chain analogs to thermal degradation with application to a pump reservoir. J Diabetes Sci Tech 6(2):277-288.
    • (2012) J Diabetes Sci Tech , vol.6 , Issue.2 , pp. 277-288
    • Phillips, N.B.1    Whittaker, J.2    Ismail-Beigi, F.3    Weiss, M.A.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.