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Volumn 363, Issue 5, 2006, Pages 977-988

Using Evolutionary Information and Ancestral Sequences to Understand the Sequence-Function Relationship in GLP-1 Agonists

Author keywords

diabetes; molecular evolution; phylogeny; protein family; sequence function mapping

Indexed keywords

GLUCAGON LIKE PEPTIDE 1 AGONIST; GLUCAGON LIKE PEPTIDE 1 DERIVATIVE; GLUCAGON LIKE PEPTIDE 1 RECEPTOR; UNCLASSIFIED DRUG;

EID: 33750018966     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2006.08.066     Document Type: Article
Times cited : (20)

References (69)
  • 1
    • 0029671221 scopus 로고    scopus 로고
    • Angiotensin ii-forming activity in a reconstructed ancestral chymase
    • Chandrasekharan U., Sanker S., Glynias M., Karnik S., and Husain A. Angiotensin ii-forming activity in a reconstructed ancestral chymase. Science 271 (1996) 502-505
    • (1996) Science , vol.271 , pp. 502-505
    • Chandrasekharan, U.1    Sanker, S.2    Glynias, M.3    Karnik, S.4    Husain, A.5
  • 2
    • 0035826690 scopus 로고    scopus 로고
    • Evolution of vertebrate steroid receptors from an ancestral estrogen receptor by ligand exploitation and serial genome expansions
    • Thornton J. Evolution of vertebrate steroid receptors from an ancestral estrogen receptor by ligand exploitation and serial genome expansions. Proc. Natl Acad. Sci. USA 98 (2001) 5671-5676
    • (2001) Proc. Natl Acad. Sci. USA , vol.98 , pp. 5671-5676
    • Thornton, J.1
  • 3
    • 0141431993 scopus 로고    scopus 로고
    • Resurrecting the ancestral steroid receptor: ancient origin of estrogen signaling
    • Thornton J., Need E., and Crews D. Resurrecting the ancestral steroid receptor: ancient origin of estrogen signaling. Science 301 (2003) 1714-1717
    • (2003) Science , vol.301 , pp. 1714-1717
    • Thornton, J.1    Need, E.2    Crews, D.3
  • 4
    • 0037117541 scopus 로고    scopus 로고
    • Complementary advantageous substitutions in the evolution of an antiviral RNase of higher primates
    • Zhang J., and Rosenberg H. Complementary advantageous substitutions in the evolution of an antiviral RNase of higher primates. Proc. Natl Acad. Sci. USA 99 (2002) 5486-5491
    • (2002) Proc. Natl Acad. Sci. USA , vol.99 , pp. 5486-5491
    • Zhang, J.1    Rosenberg, H.2
  • 5
    • 0028895702 scopus 로고
    • Reconstructing the evolutionary history of the artiodactyl ribonuclease superfamily
    • Jermann T.M., Opitz J.G., Stackhouse J., and Benner S.A. Reconstructing the evolutionary history of the artiodactyl ribonuclease superfamily. Nature 374 (1995) 57-59
    • (1995) Nature , vol.374 , pp. 57-59
    • Jermann, T.M.1    Opitz, J.G.2    Stackhouse, J.3    Benner, S.A.4
  • 8
    • 19944399387 scopus 로고    scopus 로고
    • Applications of ancestral protein reconstruction in understanding protein function: GFP-like proteins
    • Chang B., Ugalde J., and Matz M. Applications of ancestral protein reconstruction in understanding protein function: GFP-like proteins. Methods Enzymol. 395 (2005) 652-670
    • (2005) Methods Enzymol. , vol.395 , pp. 652-670
    • Chang, B.1    Ugalde, J.2    Matz, M.3
  • 9
    • 0141828152 scopus 로고    scopus 로고
    • Inferring the palaeoenvironment of ancient bacteria on the basis of resurrected proteins
    • Gaucher E., Thomson J., Burgan M., and Benner S. Inferring the palaeoenvironment of ancient bacteria on the basis of resurrected proteins. Nature 425 (2003) 285-288
    • (2003) Nature , vol.425 , pp. 285-288
    • Gaucher, E.1    Thomson, J.2    Burgan, M.3    Benner, S.4
  • 10
    • 0023104829 scopus 로고
    • Truncated glucagon-like peptide I, an insulin-releasing hormone from the distal gut
    • Holst J.J., Ørskov C., Nielsen O.V., and Schwartz T.W. Truncated glucagon-like peptide I, an insulin-releasing hormone from the distal gut. FEBS Letters 211 (1987) 169-174
    • (1987) FEBS Letters , vol.211 , pp. 169-174
    • Holst, J.J.1    Ørskov, C.2    Nielsen, O.V.3    Schwartz, T.W.4
  • 11
    • 0023107555 scopus 로고
    • Insulinotropin: glucagon-like peptide I (7-37) co-encoded in the glucagon gene is a potent stimulator of insulin release in the perfused rat pancreas
    • Mojsov S., Weir G.C., and Habener J.F. Insulinotropin: glucagon-like peptide I (7-37) co-encoded in the glucagon gene is a potent stimulator of insulin release in the perfused rat pancreas. J. Clin. Invest. 79 (1987) 616-619
    • (1987) J. Clin. Invest. , vol.79 , pp. 616-619
    • Mojsov, S.1    Weir, G.C.2    Habener, J.F.3
  • 12
    • 0344357096 scopus 로고
    • Glucagon-like peptide I stimulates insulin gene expression and increases cyclic AMP levels in a rat islet cell line
    • Drucker D.J., Philippe J., Mojsov S., Chick W.L., and Habener J.F. Glucagon-like peptide I stimulates insulin gene expression and increases cyclic AMP levels in a rat islet cell line. Proc. Natl Acad. Sci. USA 84 (1987) 3434-3438
    • (1987) Proc. Natl Acad. Sci. USA , vol.84 , pp. 3434-3438
    • Drucker, D.J.1    Philippe, J.2    Mojsov, S.3    Chick, W.L.4    Habener, J.F.5
  • 13
    • 0035081369 scopus 로고    scopus 로고
    • No reactive hypoglycaemia in type 2 diabetic patients after subcutaneous administration of GLP-1 and intravenous glucose
    • Vilsbøll T., Krarup T., Madsbad S., and Holst J. No reactive hypoglycaemia in type 2 diabetic patients after subcutaneous administration of GLP-1 and intravenous glucose. Diabet. Med. 18 (2001) 144-149
    • (2001) Diabet. Med. , vol.18 , pp. 144-149
    • Vilsbøll, T.1    Krarup, T.2    Madsbad, S.3    Holst, J.4
  • 14
    • 0034880691 scopus 로고    scopus 로고
    • Determinants of the effectiveness of glucagon-like peptide-1 in type 2 diabetes
    • Toft-Nielsen M., Madsbad S., and Holst J. Determinants of the effectiveness of glucagon-like peptide-1 in type 2 diabetes. J. Clin. Endocrinol. Metab. 86 (2001) 3853-3860
    • (2001) J. Clin. Endocrinol. Metab. , vol.86 , pp. 3853-3860
    • Toft-Nielsen, M.1    Madsbad, S.2    Holst, J.3
  • 15
    • 0037045845 scopus 로고    scopus 로고
    • Effect of 6-week course of glucagon-like peptide 1 on glycaemic control, insulin sensitivity, and beta-cell function in type 2 diabetes: a parallel-group study
    • Zander M., Madsbad S., Madsen J., and Holst J. Effect of 6-week course of glucagon-like peptide 1 on glycaemic control, insulin sensitivity, and beta-cell function in type 2 diabetes: a parallel-group study. Lancet 359 (2002) 824-830
    • (2002) Lancet , vol.359 , pp. 824-830
    • Zander, M.1    Madsbad, S.2    Madsen, J.3    Holst, J.4
  • 16
    • 3843121153 scopus 로고    scopus 로고
    • Glucagon-like peptide-1: The basis of treatment for type 2 diabetes
    • Knudsen L.B. Glucagon-like peptide-1: The basis of treatment for type 2 diabetes. J. Med. Chem. 47 (2004) 4128-4134
    • (2004) J. Med. Chem. , vol.47 , pp. 4128-4134
    • Knudsen, L.B.1
  • 18
    • 0033304603 scopus 로고    scopus 로고
    • The glucagon-like peptides
    • Kieffer T.J., and Habener J.F. The glucagon-like peptides. Endocr. Rev. 20 (1999) 876-913
    • (1999) Endocr. Rev. , vol.20 , pp. 876-913
    • Kieffer, T.J.1    Habener, J.F.2
  • 19
    • 22844444149 scopus 로고    scopus 로고
    • Mitogenomic perspectives on the origin and phylogeny of living amphibians
    • Zhang P., Zhou H., Chen Y.Q., Liu Y.F., and Qu L.H. Mitogenomic perspectives on the origin and phylogeny of living amphibians. Syst. Biol. 54 (2005) 391-400
    • (2005) Syst. Biol. , vol.54 , pp. 391-400
    • Zhang, P.1    Zhou, H.2    Chen, Y.Q.3    Liu, Y.F.4    Qu, L.H.5
  • 21
    • 0031730458 scopus 로고    scopus 로고
    • Purification and characterization of insulin, glucagon, and two glucagon-like peptides with insulin-releasing activity from the pancreas of the toad, Bufo marinus
    • Conlon J., Abdel-Wahab Y., O'Harte F., Nielsen P., and Whittaker J. Purification and characterization of insulin, glucagon, and two glucagon-like peptides with insulin-releasing activity from the pancreas of the toad, Bufo marinus. Endocrinology 139 (1998) 3442-3448
    • (1998) Endocrinology , vol.139 , pp. 3442-3448
    • Conlon, J.1    Abdel-Wahab, Y.2    O'Harte, F.3    Nielsen, P.4    Whittaker, J.5
  • 22
    • 0034712819 scopus 로고    scopus 로고
    • Proglucagon cDNAs from the leopard frog, Rana pipiens, encode two GLP-1-like peptides
    • Irwin D., and Sivarajah P. Proglucagon cDNAs from the leopard frog, Rana pipiens, encode two GLP-1-like peptides. Mol. Cell. Endocrinol. 162 (2000) 17-24
    • (2000) Mol. Cell. Endocrinol. , vol.162 , pp. 17-24
    • Irwin, D.1    Sivarajah, P.2
  • 23
    • 0035169502 scopus 로고    scopus 로고
    • Identification of a proglucagon cDNA from Rana tigrina rugulosa that encodes two GLP-1s and that is alternatively spliced in a tissue-specific manner
    • Yeung M., and Chow B. Identification of a proglucagon cDNA from Rana tigrina rugulosa that encodes two GLP-1s and that is alternatively spliced in a tissue-specific manner. Gen. Com. Endocrinol. 124 (2001) 144-151
    • (2001) Gen. Com. Endocrinol. , vol.124 , pp. 144-151
    • Yeung, M.1    Chow, B.2
  • 24
    • 0031040794 scopus 로고    scopus 로고
    • Tissue-specific expression of unique mRNAs that encode proglucagon-derived peptides or Exendin-4 in the lizard
    • Chen Y.E., and Drucker D.J. Tissue-specific expression of unique mRNAs that encode proglucagon-derived peptides or Exendin-4 in the lizard. J. Biol. Chem. 272 (1997) 4108-4115
    • (1997) J. Biol. Chem. , vol.272 , pp. 4108-4115
    • Chen, Y.E.1    Drucker, D.J.2
  • 25
    • 0026648961 scopus 로고
    • Isolation and characterization of Exendin-4, and Exendin-3 analogouge, from Heloderma suspectum
    • Eng J., Kleinman W.A., Singh L., Singh G., and Raufman J.-P. Isolation and characterization of Exendin-4, and Exendin-3 analogouge, from Heloderma suspectum. J. Biol. Chem. 267 (1992) 7402-7405
    • (1992) J. Biol. Chem. , vol.267 , pp. 7402-7405
    • Eng, J.1    Kleinman, W.A.2    Singh, L.3    Singh, G.4    Raufman, J.-P.5
  • 26
    • 0032540385 scopus 로고    scopus 로고
    • Molecular cloning of the helodermin and exendin-4 cDNAs in the lizard. Relationship to vasoactive intestinal polypeptide/pituitary adenylate cyclase activating polypeptide and glucagon-like peptide 1 and evidence against the existence of mammalian homologues
    • Pohl M., and Wank S. Molecular cloning of the helodermin and exendin-4 cDNAs in the lizard. Relationship to vasoactive intestinal polypeptide/pituitary adenylate cyclase activating polypeptide and glucagon-like peptide 1 and evidence against the existence of mammalian homologues. J. Biol. Chem. 273 (1998) 9778-9784
    • (1998) J. Biol. Chem. , vol.273 , pp. 9778-9784
    • Pohl, M.1    Wank, S.2
  • 27
    • 0027215348 scopus 로고
    • Dipeptidyl-peptidase IV hydrolyses gastric inhibitory polypeptide, glucagon-like peptide-1(7-36)amide, peptide histidine methionine and is responsible for their degradation in human serum
    • Mentlein R., Gallwitz B., and Schmidt W. Dipeptidyl-peptidase IV hydrolyses gastric inhibitory polypeptide, glucagon-like peptide-1(7-36)amide, peptide histidine methionine and is responsible for their degradation in human serum. Eur. J. Biochem. 214 (1993) 829-835
    • (1993) Eur. J. Biochem. , vol.214 , pp. 829-835
    • Mentlein, R.1    Gallwitz, B.2    Schmidt, W.3
  • 28
    • 0029118049 scopus 로고
    • Degradation of glucose-dependent insulinotropic polypeptide and truncated glucagon-like peptide 1 in vitro and in vivo by dipeptidyl peptidase IV
    • Kieffer T., McIntosh C., and Pederson R. Degradation of glucose-dependent insulinotropic polypeptide and truncated glucagon-like peptide 1 in vitro and in vivo by dipeptidyl peptidase IV. Endocrinology 136 (1995) 3585-3596
    • (1995) Endocrinology , vol.136 , pp. 3585-3596
    • Kieffer, T.1    McIntosh, C.2    Pederson, R.3
  • 29
    • 0032908654 scopus 로고    scopus 로고
    • Glucose-lowering and insulin-sensitizing actions of exendin-4: studies in obese diabetic (ob/ob, db/db) mice, diabetic fatty Zucker rats, and diabetic rhesus monkeys (Macaca mulatta)
    • Young A.A., Gedulin B.R., Bhavsar S., Bodkin N., Jodka C., Hansen B., and Denaro M. Glucose-lowering and insulin-sensitizing actions of exendin-4: studies in obese diabetic (ob/ob, db/db) mice, diabetic fatty Zucker rats, and diabetic rhesus monkeys (Macaca mulatta). Diabetes 48 (1999) 1026-1034
    • (1999) Diabetes , vol.48 , pp. 1026-1034
    • Young, A.A.1    Gedulin, B.R.2    Bhavsar, S.3    Bodkin, N.4    Jodka, C.5    Hansen, B.6    Denaro, M.7
  • 30
    • 31844435709 scopus 로고    scopus 로고
    • Early evolution of the venom system in lizards and snakes
    • Fry B., Vidal N., Norman J., Vonk F., Scheib H., Ramjan S., et al. Early evolution of the venom system in lizards and snakes. Nature 439 (2006) 584-588
    • (2006) Nature , vol.439 , pp. 584-588
    • Fry, B.1    Vidal, N.2    Norman, J.3    Vonk, F.4    Scheib, H.5    Ramjan, S.6
  • 32
    • 0036936650 scopus 로고    scopus 로고
    • Comparative peptidomics of the endocrine pancreas: islet hormones from the clawed frog Xenopus laevis and the red-bellied newt Cynops pyrrhogaster
    • Conlon J., Kim J., Johansson A., and Kikuyama S. Comparative peptidomics of the endocrine pancreas: islet hormones from the clawed frog Xenopus laevis and the red-bellied newt Cynops pyrrhogaster. J. Endocrinol. 175 (2002) 777-869
    • (2002) J. Endocrinol. , vol.175 , pp. 777-869
    • Conlon, J.1    Kim, J.2    Johansson, A.3    Kikuyama, S.4
  • 33
    • 33744997617 scopus 로고    scopus 로고
    • Immunogenicity of xenopeptide hormone therapies
    • Schnabel C.A., Fineberg S.E., and Kim D.D. Immunogenicity of xenopeptide hormone therapies. Peptides 27 (2006) 1902-1910
    • (2006) Peptides , vol.27 , pp. 1902-1910
    • Schnabel, C.A.1    Fineberg, S.E.2    Kim, D.D.3
  • 35
    • 33845377127 scopus 로고
    • Estimation of effective inter-residue contact energies from protein crystal structures: quasi-chemical approximation
    • Miyazawa S., and Jernigan R.L. Estimation of effective inter-residue contact energies from protein crystal structures: quasi-chemical approximation. Macromolecules 18 (1985) 534-552
    • (1985) Macromolecules , vol.18 , pp. 534-552
    • Miyazawa, S.1    Jernigan, R.L.2
  • 36
    • 33750180978 scopus 로고    scopus 로고
    • Rastogi, S., Reuter, N. & Liberles, D. A. (2006). Evaluation of models for the evolution of protein sequences and functions under structural constraint. Biophys. Chem. In the press.
  • 37
    • 0029830703 scopus 로고    scopus 로고
    • Investigation of glucose-dependent insulinotropic polypeptide-(1-42) and glucagon-like peptide-1-(7-36) degradation in vitro by dipeptidyl peptidase IV using matrix-assisted laser desorption/ionization-time of flight mass spectrometry. A novel kinetic approach
    • Pauly R.P., Rosche F., Wermann M., McIntosh C.H., Pederson R.A., and Demuth H.U. Investigation of glucose-dependent insulinotropic polypeptide-(1-42) and glucagon-like peptide-1-(7-36) degradation in vitro by dipeptidyl peptidase IV using matrix-assisted laser desorption/ionization-time of flight mass spectrometry. A novel kinetic approach. J. Biol. Chem. 27 (1996) 23222-23229
    • (1996) J. Biol. Chem. , vol.27 , pp. 23222-23229
    • Pauly, R.P.1    Rosche, F.2    Wermann, M.3    McIntosh, C.H.4    Pederson, R.A.5    Demuth, H.U.6
  • 38
    • 0038798661 scopus 로고    scopus 로고
    • The importance of the nine-amino acid C-terminal sequence of exendin-4 for binding to the GLP-1 receptor and for biological activity
    • Doyle M., Theodorakis M., Holloway H., Bernier M., Greig N., and Egan J. The importance of the nine-amino acid C-terminal sequence of exendin-4 for binding to the GLP-1 receptor and for biological activity. Reg. Pept. 114 (2003) 153-158
    • (2003) Reg. Pept. , vol.114 , pp. 153-158
    • Doyle, M.1    Theodorakis, M.2    Holloway, H.3    Bernier, M.4    Greig, N.5    Egan, J.6
  • 39
    • 0031782440 scopus 로고    scopus 로고
    • Dipeptidyl peptidase IV resistant analogues of glucagon-like peptide-1 which have extended metabolic stability and improved biological activity
    • Deacon C., Knudsen L., Madsen K., Wiberg F., Jacobsen O., and Holst J.J. Dipeptidyl peptidase IV resistant analogues of glucagon-like peptide-1 which have extended metabolic stability and improved biological activity. Diabetologia 41 (1998) 271-278
    • (1998) Diabetologia , vol.41 , pp. 271-278
    • Deacon, C.1    Knudsen, L.2    Madsen, K.3    Wiberg, F.4    Jacobsen, O.5    Holst, J.J.6
  • 40
    • 0034806376 scopus 로고    scopus 로고
    • Insertion of an N-terminal 6-aminohexanoic acid after the 7 amino acid position of glucagon-like peptide-1 produces a long-acting hypoglycemic agent
    • Doyle M., Greig N., Holloway H., Betkey J., Bernier M., and Egan J. Insertion of an N-terminal 6-aminohexanoic acid after the 7 amino acid position of glucagon-like peptide-1 produces a long-acting hypoglycemic agent. Endocrinology 142 (2001) 4462-4468
    • (2001) Endocrinology , vol.142 , pp. 4462-4468
    • Doyle, M.1    Greig, N.2    Holloway, H.3    Betkey, J.4    Bernier, M.5    Egan, J.6
  • 42
    • 0035029534 scopus 로고    scopus 로고
    • Maximum likelihood phylogenetic analysis under a covarion-like model
    • Galtier N. Maximum likelihood phylogenetic analysis under a covarion-like model. Mol. Biol. Evol. 18 (2001) 866-873
    • (2001) Mol. Biol. Evol. , vol.18 , pp. 866-873
    • Galtier, N.1
  • 43
    • 0036134757 scopus 로고    scopus 로고
    • Heterotachy, an important process of protein evolution
    • Lopez P., Casane D., and Philippe H. Heterotachy, an important process of protein evolution. Mol. Biol. Evol. 19 (2002) 1-7
    • (2002) Mol. Biol. Evol. , vol.19 , pp. 1-7
    • Lopez, P.1    Casane, D.2    Philippe, H.3
  • 44
    • 21044435697 scopus 로고    scopus 로고
    • Sign epistasis and genetic constraint on evolutionary trajectories
    • Weinreich D.M., Watson R.A., and Chao L. Sign epistasis and genetic constraint on evolutionary trajectories. Evolution 59 (2005) 1165-1174
    • (2005) Evolution , vol.59 , pp. 1165-1174
    • Weinreich, D.M.1    Watson, R.A.2    Chao, L.3
  • 45
    • 0028922906 scopus 로고
    • Testing the covarion hypothesis of molecular evolution
    • Miyamoto M.M., and Fitch W.M. Testing the covarion hypothesis of molecular evolution. Mol. Biol. Evol. 12 (1995) 503-513
    • (1995) Mol. Biol. Evol. , vol.12 , pp. 503-513
    • Miyamoto, M.M.1    Fitch, W.M.2
  • 46
    • 19944373422 scopus 로고    scopus 로고
    • Tertiary windowing to detect positive diversifying selection
    • Berglund A.C., Wallner B., Elofsson A., and Liberles D.A. Tertiary windowing to detect positive diversifying selection. J. Mol. Evol. 60 (2005) 499-504
    • (2005) J. Mol. Evol. , vol.60 , pp. 499-504
    • Berglund, A.C.1    Wallner, B.2    Elofsson, A.3    Liberles, D.A.4
  • 47
    • 23944476399 scopus 로고    scopus 로고
    • A model based approach for detecting coevolving positions in a molecule
    • Dutheil J., Pupko T., Jean-Marie A., and Galtier N. A model based approach for detecting coevolving positions in a molecule. Mol. Biol. Evol. 22 (2005) 1919-1928
    • (2005) Mol. Biol. Evol. , vol.22 , pp. 1919-1928
    • Dutheil, J.1    Pupko, T.2    Jean-Marie, A.3    Galtier, N.4
  • 48
    • 30744435826 scopus 로고    scopus 로고
    • An evolutionary space-time model with varying among-site dependencies
    • Stern A., and Pupko T. An evolutionary space-time model with varying among-site dependencies. Mol. Biol. Evol. 23 (2006) 392-400
    • (2006) Mol. Biol. Evol. , vol.23 , pp. 392-400
    • Stern, A.1    Pupko, T.2
  • 49
    • 33747239595 scopus 로고    scopus 로고
    • A systematic search for positive selection in higher plants (Embryophytes)
    • Roth C., and Liberles D.A. A systematic search for positive selection in higher plants (Embryophytes). BMC Plant Biology 6 (2006) 12
    • (2006) BMC Plant Biology , vol.6 , pp. 12
    • Roth, C.1    Liberles, D.A.2
  • 50
    • 0033582946 scopus 로고    scopus 로고
    • Coevolving protein residues: maximum likelihood identification and relationship to structure
    • Pollock D.D., Taylor W.R., and Goldman N. Coevolving protein residues: maximum likelihood identification and relationship to structure. J. Mol. Biol. 287 (1999) 187-198
    • (1999) J. Mol. Biol. , vol.287 , pp. 187-198
    • Pollock, D.D.1    Taylor, W.R.2    Goldman, N.3
  • 51
    • 0035818410 scopus 로고    scopus 로고
    • Exendin-4 and glucagon-like-peptide-1: NMR structural comparisons in the solution and micelle-associated states
    • Neidigh J.W., Fesinmeyer R.M., Prickett K.S., and Andersen N.H. Exendin-4 and glucagon-like-peptide-1: NMR structural comparisons in the solution and micelle-associated states. Biochemistry 40 (2001) 13188-13200
    • (2001) Biochemistry , vol.40 , pp. 13188-13200
    • Neidigh, J.W.1    Fesinmeyer, R.M.2    Prickett, K.S.3    Andersen, N.H.4
  • 52
    • 0008739778 scopus 로고    scopus 로고
    • Structure and folding of glucagon-like peptide-1-(7-36)-amide in trifluoroethanol studied by NMR Magn
    • Chang X., Keller D., Bjorn S., and Led J.J. Structure and folding of glucagon-like peptide-1-(7-36)-amide in trifluoroethanol studied by NMR Magn. Reson. Chem. 39 (2001) 477-483
    • (2001) Reson. Chem. , vol.39 , pp. 477-483
    • Chang, X.1    Keller, D.2    Bjorn, S.3    Led, J.J.4
  • 53
    • 0029111540 scopus 로고
    • Characterisation of the processing by human neutral endopeptidase 24.11 of GLP-1(7-36) amide and comparison of the substrate specificity of the enzyme for other glucagon-like peptides
    • Hupe-Sodmann K., McGregor G.P., Bridenbaugh R., Goke R., Goke B., Thole H., et al. Characterisation of the processing by human neutral endopeptidase 24.11 of GLP-1(7-36) amide and comparison of the substrate specificity of the enzyme for other glucagon-like peptides. Regul. Pept. 58 (1995) 149-156
    • (1995) Regul. Pept. , vol.58 , pp. 149-156
    • Hupe-Sodmann, K.1    McGregor, G.P.2    Bridenbaugh, R.3    Goke, R.4    Goke, B.5    Thole, H.6
  • 54
    • 4143138571 scopus 로고    scopus 로고
    • Neutral endopeptidase 24.11 is important for the degradation of both endogenous and exogenous glucagon in anesthetized pigs
    • Trebbien R., Klarskov L., Olesen M., Holst J.J., Carr R.D., and Deacon C.F. Neutral endopeptidase 24.11 is important for the degradation of both endogenous and exogenous glucagon in anesthetized pigs. Am. J. Physiol. Endocrinol. Metab. 287 (2004) E431-E438
    • (2004) Am. J. Physiol. Endocrinol. Metab. , vol.287
    • Trebbien, R.1    Klarskov, L.2    Olesen, M.3    Holst, J.J.4    Carr, R.D.5    Deacon, C.F.6
  • 55
    • 24944436267 scopus 로고    scopus 로고
    • Neutral endopeptidase 24.11 and dipeptidyl peptidase IV are both mediators of the degradation of glucagon-like peptide 1 in the anaesthetised pig
    • Plamboeck A., Holst J.J., Carr R.D., and Deacon C.F. Neutral endopeptidase 24.11 and dipeptidyl peptidase IV are both mediators of the degradation of glucagon-like peptide 1 in the anaesthetised pig. Diabetologia 48 (2005) 1882-1890
    • (2005) Diabetologia , vol.48 , pp. 1882-1890
    • Plamboeck, A.1    Holst, J.J.2    Carr, R.D.3    Deacon, C.F.4
  • 56
    • 0029921021 scopus 로고    scopus 로고
    • Isolation and structural characterization of proglucagon-derived peptides, pancreatic polypeptide, and somatostatin from the urodele Amphiuma tridactylum
    • Cavanaugh E., Nielsen P., and Conlon J. Isolation and structural characterization of proglucagon-derived peptides, pancreatic polypeptide, and somatostatin from the urodele Amphiuma tridactylum. Gen. Comp. Endocrinol. 101 (1996) 12-20
    • (1996) Gen. Comp. Endocrinol. , vol.101 , pp. 12-20
    • Cavanaugh, E.1    Nielsen, P.2    Conlon, J.3
  • 57
    • 0032991760 scopus 로고    scopus 로고
    • Insulin and proglucagonderived peptides from the horned frog, Ceratophrys ornata (anura:leptodactylidae)
    • White A., Secor S., and Conlon J. Insulin and proglucagonderived peptides from the horned frog, Ceratophrys ornata (anura:leptodactylidae). Gen. Comp. Endocrinol. 115 (1999) 143-154
    • (1999) Gen. Comp. Endocrinol. , vol.115 , pp. 143-154
    • White, A.1    Secor, S.2    Conlon, J.3
  • 58
    • 0025342757 scopus 로고
    • Nucleotide sequence determination of chicken glucagon precursor cDNA. Chicken preproglucagon does not contain glucagon-like peptide II
    • Hasegawa S., Terazono K., Nata K., Takada T., Yamamoto H., and Okamoto H. Nucleotide sequence determination of chicken glucagon precursor cDNA. Chicken preproglucagon does not contain glucagon-like peptide II. FEBS Letters 264 (1990) 117-120
    • (1990) FEBS Letters , vol.264 , pp. 117-120
    • Hasegawa, S.1    Terazono, K.2    Nata, K.3    Takada, T.4    Yamamoto, H.5    Okamoto, H.6
  • 59
    • 0024359370 scopus 로고
    • Complete sequences of glucagon-like peptide-1 from human and pig small intestine
    • Ørskov C., Bersani M., Johnsen A., Hojrup P., and Holst J. Complete sequences of glucagon-like peptide-1 from human and pig small intestine. J. Biol. Chem. 264 (1989) 12826-12829
    • (1989) J. Biol. Chem. , vol.264 , pp. 12826-12829
    • Ørskov, C.1    Bersani, M.2    Johnsen, A.3    Hojrup, P.4    Holst, J.5
  • 60
    • 0033890622 scopus 로고    scopus 로고
    • Islet hormones from the african bullfrog Pyxicephalus adspersus (anura:ranidae): structural characterization and phylogenetic implications
    • Conlon J., White A., and Platz J. Islet hormones from the african bullfrog Pyxicephalus adspersus (anura:ranidae): structural characterization and phylogenetic implications. Gen. Comp. Endocrinol. 119 (2000) 85-94
    • (2000) Gen. Comp. Endocrinol. , vol.119 , pp. 85-94
    • Conlon, J.1    White, A.2    Platz, J.3
  • 61
    • 0033783674 scopus 로고    scopus 로고
    • Characterization of insulin and atypically processed proglucagon-derived peptides from the surinam toad Pipa pipa (anura:pipidae)
    • Matutte B., and Conlon J. Characterization of insulin and atypically processed proglucagon-derived peptides from the surinam toad Pipa pipa (anura:pipidae). Peptides 21 (2000) 1355-1360
    • (2000) Peptides , vol.21 , pp. 1355-1360
    • Matutte, B.1    Conlon, J.2
  • 62
    • 0023718392 scopus 로고
    • Isolation of peptide hormones from the pancreas of the bullfrog (Rana catesbeiana). Amino acid sequences of pancreatic polypeptide, oxyntomodulin, and two glucagon-like peptides
    • Pollock H., Hamilton J., Rouse J., Ebner K., and Rawitch A. Isolation of peptide hormones from the pancreas of the bullfrog (Rana catesbeiana). Amino acid sequences of pancreatic polypeptide, oxyntomodulin, and two glucagon-like peptides. J. Biol. Chem. 263 (1988) 9746-9751
    • (1988) J. Biol. Chem. , vol.263 , pp. 9746-9751
    • Pollock, H.1    Hamilton, J.2    Rouse, J.3    Ebner, K.4    Rawitch, A.5
  • 63
    • 0000122573 scopus 로고    scopus 로고
    • PHYLIP- phylogeny interference package
    • Felsenstein J. PHYLIP- phylogeny interference package. Cladistics 5 (1998) 164-166
    • (1998) Cladistics , vol.5 , pp. 164-166
    • Felsenstein, J.1
  • 64
    • 18744382506 scopus 로고    scopus 로고
    • ProtTest: Selection of best-fit models of protein evolution
    • Abascal F., Zardoya R., and Posoda D. ProtTest: Selection of best-fit models of protein evolution. Bioinformatics 21 (2005) 2104-2105
    • (2005) Bioinformatics , vol.21 , pp. 2104-2105
    • Abascal, F.1    Zardoya, R.2    Posoda, D.3
  • 65
    • 33746433923 scopus 로고    scopus 로고
    • Optimal gene trees from sequences and species trees using a soft interpretation of parsimony
    • Berglund-Sonnhammer A.C., Steffansson P., Betts M.J., and Liberles D.A. Optimal gene trees from sequences and species trees using a soft interpretation of parsimony. J. Mol. Evol. 63 (2006) 240-250
    • (2006) J. Mol. Evol. , vol.63 , pp. 240-250
    • Berglund-Sonnhammer, A.C.1    Steffansson, P.2    Betts, M.J.3    Liberles, D.A.4
  • 66
    • 0034117082 scopus 로고    scopus 로고
    • A fast algorithm for joint reconstruction of ancestral amino-acid sequences
    • Pupko T., Pe'er I., Shamir R., and Graur D. A fast algorithm for joint reconstruction of ancestral amino-acid sequences. Mol. Biol. Evol. 17 (2000) 890-896
    • (2000) Mol. Biol. Evol. , vol.17 , pp. 890-896
    • Pupko, T.1    Pe'er, I.2    Shamir, R.3    Graur, D.4
  • 67
    • 0036677932 scopus 로고    scopus 로고
    • A branch- and -bound algorithm for the inference of ancestral amino-acid sequences when the replacement rate varies among sites: application to the evolution of five gene families
    • Pupko T., Pe'er I., Graur D., Hasegawa M., and Friedman N. A branch- and -bound algorithm for the inference of ancestral amino-acid sequences when the replacement rate varies among sites: application to the evolution of five gene families. Bioinformatics 18 (2002) 1116-1123
    • (2002) Bioinformatics , vol.18 , pp. 1116-1123
    • Pupko, T.1    Pe'er, I.2    Graur, D.3    Hasegawa, M.4    Friedman, N.5
  • 68
    • 0026691182 scopus 로고
    • The rapid generation of mutation data matrices from protein sequences
    • Jones D., Taylor W., and Thornton J. The rapid generation of mutation data matrices from protein sequences. Comput. Appl. Biosci. 8 (1992) 275-282
    • (1992) Comput. Appl. Biosci. , vol.8 , pp. 275-282
    • Jones, D.1    Taylor, W.2    Thornton, J.3


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