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Volumn 53, Issue 22, 2010, Pages 8059-8071

Disulfide cyclized tripeptide analogues of angiotensin IV as potent and selective inhibitors of insulin-regulated aminopeptidase (IRAP)

Author keywords

[No Author keywords available]

Indexed keywords

AMINOPEPTIDASE; ANGIOTENSIN II [3-8]; DISULFIDE; INSULIN REGULATED AMINOPEPTIDASE; INSULIN REGULATED AMINOPEPTIDASE INHIBITOR; PEPTIDE HYDROLASE INHIBITOR; PHENYLACETIC ACID; TRIPEPTIDE DERIVATIVE; UNCLASSIFIED DRUG;

EID: 78649500321     PISSN: 00222623     EISSN: 15204804     Source Type: Journal    
DOI: 10.1021/jm100793t     Document Type: Article
Times cited : (54)

References (86)
  • 3
    • 0037146905 scopus 로고    scopus 로고
    • Neuroprotection by memantine against neurodegeneration induced by beta-amyloid(1-40)
    • Miguel-Hidalgo, J. J.; Alvarez, X. A.; Cacabelos, R.; Quack, G. Neuroprotection by memantine against neurodegeneration induced by beta-amyloid(1-40) Brain Res. 2002, 958, 210-221
    • (2002) Brain Res. , vol.958 , pp. 210-221
    • Miguel-Hidalgo, J.J.1    Alvarez, X.A.2    Cacabelos, R.3    Quack, G.4
  • 4
    • 42749100518 scopus 로고    scopus 로고
    • Cholinesterase inhibitors for Alzheimer's disease
    • CD005593
    • Birks, J. Cholinesterase inhibitors for Alzheimer's disease. Cochrane Database Syst. Rev. 2006, CD005593.
    • (2006) Cochrane Database Syst. Rev.
    • Birks, J.1
  • 5
  • 6
    • 30344479822 scopus 로고    scopus 로고
    • Pharmacological strategies for the prevention of Alzheimer's disease
    • Doraiswamy, P. M.; Xiong, G. L. Pharmacological strategies for the prevention of Alzheimer's disease Expert Opin. Pharmacother. 2006, 7, 1-10
    • (2006) Expert Opin. Pharmacother. , vol.7 , pp. 1-10
    • Doraiswamy, P.M.1    Xiong, G.L.2
  • 7
    • 41049111771 scopus 로고    scopus 로고
    • Effectiveness of cholinesterase inhibitors and memantine for treating dementia: Evidence review for a clinical practice guideline
    • Raina, P.; Santaguida, P.; Ismaila, A.; Patterson, C.; Cowan, D.; Levine, M.; Booker, L.; Oremus, M. Effectiveness of cholinesterase inhibitors and memantine for treating dementia: evidence review for a clinical practice guideline Ann. Intern. Med. 2008, 148, 379-397
    • (2008) Ann. Intern. Med. , vol.148 , pp. 379-397
    • Raina, P.1    Santaguida, P.2    Ismaila, A.3    Patterson, C.4    Cowan, D.5    Levine, M.6    Booker, L.7    Oremus, M.8
  • 8
    • 0033911108 scopus 로고    scopus 로고
    • Sustained improvements in patients with dementia of Alzheimer's type (DAT) 6 months after termination of Cerebrolysin therapy
    • Ruther, E.; Ritter, R.; Apecechea, M.; Freytag, S.; Gmeinbauer, R.; Windisch, M. Sustained improvements in patients with dementia of Alzheimer's type (DAT) 6 months after termination of Cerebrolysin therapy J. Neural Transm. 2000, 107, 815-829
    • (2000) J. Neural Transm. , vol.107 , pp. 815-829
    • Ruther, E.1    Ritter, R.2    Apecechea, M.3    Freytag, S.4    Gmeinbauer, R.5    Windisch, M.6
  • 9
    • 34648845315 scopus 로고    scopus 로고
    • Prospects for Antioxidant Therapy in Mild Cognitive Impairment and Alzheimer'S Disease
    • In;, Eds.; Elsevier B.V.: Amsterdam
    • Nunomura, A.; Perry, G.; Smith, M. A. Prospects for Antioxidant Therapy in Mild Cognitive Impairment and Alzheimer'S Disease. In Oxidative Stress and Neurodegenerative Disorders; Qureshi, G. A.; Parvez, S. H., Eds.; Elsevier B.V.: Amsterdam, 2007; pp 451 - 466.
    • (2007) Oxidative Stress and Neurodegenerative Disorders , pp. 451-466
    • Nunomura, A.1    Perry, G.2    Smith, M.A.3    Qureshi, G.A.4    Parvez, S.H.5
  • 14
    • 0036833437 scopus 로고    scopus 로고
    • Therapeutic strategies for Alzheimer's disease
    • Wolfe, M. S. Therapeutic strategies for Alzheimer's disease Nat. Rev. Drug Discovery 2002, 1, 859-866
    • (2002) Nat. Rev. Drug Discovery , vol.1 , pp. 859-866
    • Wolfe, M.S.1
  • 15
    • 66149108067 scopus 로고    scopus 로고
    • 4 receptor subtype as a target for the treatment of memory dysfunction associated with Alzheimer's disease
    • 4 receptor subtype as a target for the treatment of memory dysfunction associated with Alzheimer's disease J. Renin-Angiotensin-Aldosterone Syst. 2008, 9, 226-237
    • (2008) J. Renin-Angiotensin-Aldosterone Syst. , vol.9 , pp. 226-237
    • Wright, J.W.1    Harding, J.W.2
  • 16
    • 0024202954 scopus 로고
    • Angiotensin II-(3-8)-hexapeptide affects motor activity, performance of passive avoidance and a conditioned avoidance response in rats
    • Braszko, J. J.; Kupryszewski, G.; Witczuk, B.; Wisniewski, K. Angiotensin II-(3-8)-hexapeptide affects motor activity, performance of passive avoidance and a conditioned avoidance response in rats Neuroscience 1988, 27, 777-783
    • (1988) Neuroscience , vol.27 , pp. 777-783
    • Braszko, J.J.1    Kupryszewski, G.2    Witczuk, B.3    Wisniewski, K.4
  • 17
    • 0026081809 scopus 로고
    • The 3-7 fragment of angiotensin II is probably responsible for its psychoactive properties
    • Braszko, J. J.; Wlasienko, J.; Koziolkiewicz, W.; Janecka, A.; Wisniewski, K. The 3-7 fragment of angiotensin II is probably responsible for its psychoactive properties Brain Res. 1991, 542, 49-54
    • (1991) Brain Res. , vol.542 , pp. 49-54
    • Braszko, J.J.1    Wlasienko, J.2    Koziolkiewicz, W.3    Janecka, A.4    Wisniewski, K.5
  • 19
    • 67449101063 scopus 로고    scopus 로고
    • 4 receptor for cognitive disorders
    • 4 receptor for cognitive disorders Drug News Perspect. 2009, 22, 133-139
    • (2009) Drug News Perspect. , vol.22 , pp. 133-139
    • Hallberg, M.1
  • 22
    • 19944397128 scopus 로고    scopus 로고
    • Distribution and cellular localization of insulin-regulated aminopeptidase in the rat central nervous system
    • Fernando, R. N.; Larm, J.; Albiston, A. L.; Chai, S. Y. Distribution and cellular localization of insulin-regulated aminopeptidase in the rat central nervous system J. Comp. Neurol. 2005, 487, 372-390
    • (2005) J. Comp. Neurol. , vol.487 , pp. 372-390
    • Fernando, R.N.1    Larm, J.2    Albiston, A.L.3    Chai, S.Y.4
  • 25
    • 0028817838 scopus 로고
    • Cloning and characterization of a novel insulin-regulated membrane aminopeptidase from Glut4 vesicles
    • Keller, S. R.; Scott, H. M.; Mastick, C. C.; Aebersold, R.; Lienhard, G. E. Cloning and characterization of a novel insulin-regulated membrane aminopeptidase from Glut4 vesicles J. Biol. Chem. 1995, 270, 23612-23618
    • (1995) J. Biol. Chem. , vol.270 , pp. 23612-23618
    • Keller, S.R.1    Scott, H.M.2    Mastick, C.C.3    Aebersold, R.4    Lienhard, G.E.5
  • 32
    • 33947091567 scopus 로고
    • 9-Fluorenylmethoxycarbonyl amino-protecting group
    • Carpino, L. A.; Han, G. Y. 9-Fluorenylmethoxycarbonyl amino-protecting group J. Org. Chem. 1972, 37, 3404-3409
    • (1972) J. Org. Chem. , vol.37 , pp. 3404-3409
    • Carpino, L.A.1    Han, G.Y.2
  • 33
    • 0036830576 scopus 로고    scopus 로고
    • Practical protocols for stepwise solid-phase synthesis of cysteine-containing peptides
    • Angell, Y. M.; Alsina, J.; Albericio, F.; Barany, G. Practical protocols for stepwise solid-phase synthesis of cysteine-containing peptides J. Pept. Res. 2002, 60, 292-299
    • (2002) J. Pept. Res. , vol.60 , pp. 292-299
    • Angell, Y.M.1    Alsina, J.2    Albericio, F.3    Barany, G.4
  • 34
    • 0000443850 scopus 로고    scopus 로고
    • Reactions of thiols with sulfoxides. II. Kinetics and mechanistic implications
    • Wallace, T. J.; Mahon, J. J. Reactions of thiols with sulfoxides. II. Kinetics and mechanistic implications J. Am. Chem. Soc. 2002, 86, 4099-4103
    • (2002) J. Am. Chem. Soc. , vol.86 , pp. 4099-4103
    • Wallace, T.J.1    Mahon, J.J.2
  • 35
    • 0026099676 scopus 로고
    • Application of dimethylsulphoxide(DMSO)/trifluoroacetic acid(TFA) oxidation to the synthesis of cystine-containing peptide
    • Otaka, A.; Koide, T.; Shide, A.; Fujii, N. Application of dimethylsulphoxide(DMSO)/trifluoroacetic acid(TFA) oxidation to the synthesis of cystine-containing peptide Tetrahedron Lett. 1991, 32, 1223-1226
    • (1991) Tetrahedron Lett. , vol.32 , pp. 1223-1226
    • Otaka, A.1    Koide, T.2    Shide, A.3    Fujii, N.4
  • 36
    • 12044255356 scopus 로고    scopus 로고
    • Disulfide bond formation in peptides by dimethyl sulfoxide. Scope and applications
    • Tam, J. P.; Wu, C. R.; Liu, W.; Zhang, J. W. Disulfide bond formation in peptides by dimethyl sulfoxide. Scope and applications J. Am. Chem. Soc. 2002, 113, 6657-6662
    • (2002) J. Am. Chem. Soc. , vol.113 , pp. 6657-6662
    • Tam, J.P.1    Wu, C.R.2    Liu, W.3    Zhang, J.W.4
  • 37
    • 0032474786 scopus 로고    scopus 로고
    • Preparation of amides from acids and resin bound azides: Suppression of intramolecular lactam formation
    • Tang, Z. L.; Pelletier, J. C. Preparation of amides from acids and resin bound azides: suppression of intramolecular lactam formation Tetrahedron Lett. 1998, 39, 4773-4776
    • (1998) Tetrahedron Lett. , vol.39 , pp. 4773-4776
    • Tang, Z.L.1    Pelletier, J.C.2
  • 38
    • 33751185559 scopus 로고    scopus 로고
    • Microwave heating for solid-phase peptide synthesis: General evaluation and application to 15-mer phosphopeptides
    • Brandt, M.; Gammeltoft, S.; Jensen, K. Microwave heating for solid-phase peptide synthesis: general evaluation and application to 15-mer phosphopeptides Int. J. Pept. Res. Ther. 2006, 12, 349-357
    • (2006) Int. J. Pept. Res. Ther. , vol.12 , pp. 349-357
    • Brandt, M.1    Gammeltoft, S.2    Jensen, K.3
  • 39
    • 0035903957 scopus 로고    scopus 로고
    • A useful and sensitive color test to monitor aldehydes on solid-phase
    • Vázquez, J.; Albericio, F. A useful and sensitive color test to monitor aldehydes on solid-phase Tetrahedron Lett. 2001, 42, 6691-6693
    • (2001) Tetrahedron Lett. , vol.42 , pp. 6691-6693
    • Vázquez, J.1    Albericio, F.2
  • 41
    • 0029330768 scopus 로고
    • Detection of secondary amines on solid phase
    • Vojkovsky, T. Detection of secondary amines on solid phase Pept. Res. 1995, 8, 236-237
    • (1995) Pept. Res. , vol.8 , pp. 236-237
    • Vojkovsky, T.1
  • 42
    • 0033612194 scopus 로고    scopus 로고
    • A test of the single-conformation hypothesis in the analysis of NMR data for small polar molecules: A force field comparison
    • Nevins, N.; Cicero, D.; Snyder, J. P. A test of the single-conformation hypothesis in the analysis of NMR data for small polar molecules: a force field comparison J. Org. Chem. 1999, 64, 3979-3986
    • (1999) J. Org. Chem. , vol.64 , pp. 3979-3986
    • Nevins, N.1    Cicero, D.2    Snyder, J.P.3
  • 43
    • 0030636935 scopus 로고    scopus 로고
    • Application of a genetic algorithm in the conformational analysis of methylene-acetal-linked thymine dimers in DNA: Comparison with distance geometry calculations
    • Beckers, M. L.; Buydens, L. M.; Pikkemaat, J. A.; Altona, C. Application of a genetic algorithm in the conformational analysis of methylene-acetal-linked thymine dimers in DNA: comparison with distance geometry calculations J. Biomol. NMR 1997, 9, 25-34
    • (1997) J. Biomol. NMR , vol.9 , pp. 25-34
    • Beckers, M.L.1    Buydens, L.M.2    Pikkemaat, J.A.3    Altona, C.4
  • 44
    • 0027384192 scopus 로고
    • Conformational backbone dynamics of the cyclic decapeptide antamanide. Application of a new multiconformational search algorithm based on NMR data
    • Blackledge, M. J.; Bruschweiler, R.; Griesinger, C.; Schmidt, J. M.; Xu, P.; Ernst, R. R. Conformational backbone dynamics of the cyclic decapeptide antamanide. Application of a new multiconformational search algorithm based on NMR data Biochemistry 1993, 32, 10960-10974
    • (1993) Biochemistry , vol.32 , pp. 10960-10974
    • Blackledge, M.J.1    Bruschweiler, R.2    Griesinger, C.3    Schmidt, J.M.4    Xu, P.5    Ernst, R.R.6
  • 45
    • 0026159294 scopus 로고
    • Multi-conformational peptide dynamics derived from NMR data: A new search algorithm and its application to antamanide
    • Bruschweiler, R.; Blackledge, M.; Ernst, R. R. Multi-conformational peptide dynamics derived from NMR data: a new search algorithm and its application to antamanide J. Biomol. NMR 1991, 1, 3-11
    • (1991) J. Biomol. NMR , vol.1 , pp. 3-11
    • Bruschweiler, R.1    Blackledge, M.2    Ernst, R.R.3
  • 46
    • 0000457461 scopus 로고
    • Elucidation of solution structures by conformer population analysis of NOE data
    • Landis, C.; Allured, V. S. Elucidation of solution structures by conformer population analysis of NOE data J. Am. Chem. Soc. 1991, 113, 9493-9499
    • (1991) J. Am. Chem. Soc. , vol.113 , pp. 9493-9499
    • Landis, C.1    Allured, V.S.2
  • 47
    • 0028793933 scopus 로고
    • NMR analysis of molecular flexibility in solution: A new method for the study of complex distributions of rapidly exchanging conformations. Application to a 13-residue peptide with an 8-residue loop
    • Cicero, D. O.; Barbato, G.; Bazzo, R. NMR analysis of molecular flexibility in solution: a new method for the study of complex distributions of rapidly exchanging conformations. Application to a 13-residue peptide with an 8-residue loop J. Am. Chem. Soc. 1995, 117, 1027-1033
    • (1995) J. Am. Chem. Soc. , vol.117 , pp. 1027-1033
    • Cicero, D.O.1    Barbato, G.2    Bazzo, R.3
  • 48
    • 0001843949 scopus 로고    scopus 로고
    • FINGAR, a new genetic algorithm-based method for fitting NMR data
    • Pearlman, D. A. FINGAR, a new genetic algorithm-based method for fitting NMR data J. Biomol. NMR 1996, 8, 49-66
    • (1996) J. Biomol. NMR , vol.8 , pp. 49-66
    • Pearlman, D.A.1
  • 49
    • 0029099201 scopus 로고
    • Generating multiple conformations of flexible peptides in solution on the basis of NMR nuclear Overhauser effect data: Application to desmopressin
    • Wang, J.; Hodges, R. S.; Sykes, B. D. Generating multiple conformations of flexible peptides in solution on the basis of NMR nuclear Overhauser effect data: application to desmopressin J. Am. Chem. Soc. 1995, 117, 8627-8634
    • (1995) J. Am. Chem. Soc. , vol.117 , pp. 8627-8634
    • Wang, J.1    Hodges, R.S.2    Sykes, B.D.3
  • 51
    • 35148813913 scopus 로고    scopus 로고
    • Determination of relative configuration in organic compounds by NMR spectroscopy and computational methods
    • Bifulco, G.; Dambruoso, P.; Gomez-Paloma, L.; Riccio, R. Determination of relative configuration in organic compounds by NMR spectroscopy and computational methods Chem. Rev. 2007, 107, 3744-3779
    • (2007) Chem. Rev. , vol.107 , pp. 3744-3779
    • Bifulco, G.1    Dambruoso, P.2    Gomez-Paloma, L.3    Riccio, R.4
  • 52
    • 0033525048 scopus 로고    scopus 로고
    • Stereochemical determination of acyclic structures based on carbon-proton spin-coupling constants. A method of configuration analysis for natural products
    • Matsumori, N.; Kaneno, D.; Murata, M.; Nakamura, H.; Tachibana, K. Stereochemical determination of acyclic structures based on carbon-proton spin-coupling constants. A method of configuration analysis for natural products J. Org. Chem. 1999, 64, 866-876
    • (1999) J. Org. Chem. , vol.64 , pp. 866-876
    • Matsumori, N.1    Kaneno, D.2    Murata, M.3    Nakamura, H.4    Tachibana, K.5
  • 53
    • 45549091464 scopus 로고    scopus 로고
    • Simultaneous determination of the conformation and relative configuration of archazolide A by using nuclear Overhauser effects, J couplings, and residual dipolar couplings
    • Farès, C.; Hassfeld, J.; Menche, D.; Carlomagno, T. Simultaneous determination of the conformation and relative configuration of archazolide A by using nuclear Overhauser effects, J couplings, and residual dipolar couplings Angew. Chem., Int. Ed. 2008, 47, 3722-3726
    • (2008) Angew. Chem., Int. Ed. , vol.47 , pp. 3722-3726
    • Farès, C.1    Hassfeld, J.2    Menche, D.3    Carlomagno, T.4
  • 54
    • 64349102959 scopus 로고    scopus 로고
    • Residual dipolar couplings of freely rotating groups in small molecules. Stereochemical assignment and side-chain conformation of 8-phenylmenthol
    • Sanchez-Pedregal, V. M.; Santamaria-Fernandez, R.; Navarro-Vazquez, A. Residual dipolar couplings of freely rotating groups in small molecules. Stereochemical assignment and side-chain conformation of 8-phenylmenthol Org. Lett. 2009, 11, 1471-1474
    • (2009) Org. Lett. , vol.11 , pp. 1471-1474
    • Sanchez-Pedregal, V.M.1    Santamaria-Fernandez, R.2    Navarro-Vazquez, A.3
  • 55
    • 6344229751 scopus 로고    scopus 로고
    • Simultaneous assignment of all diastereotopic protons in strychnine using RDCs: PELG as alignment medium for organic molecules
    • Thiele, C. M. Simultaneous assignment of all diastereotopic protons in strychnine using RDCs: PELG as alignment medium for organic molecules J. Org. Chem. 2004, 69, 7403-7413
    • (2004) J. Org. Chem. , vol.69 , pp. 7403-7413
    • Thiele, C.M.1
  • 56
    • 56749185636 scopus 로고    scopus 로고
    • Residual dipolar couplings (RDCs) in organic structure determination
    • Thiele, C. M. Residual dipolar couplings (RDCs) in organic structure determination Eur. J. Org. Chem. 2008, 5673-5685
    • (2008) Eur. J. Org. Chem. , pp. 5673-5685
    • Thiele, C.M.1
  • 65
    • 0022895350 scopus 로고
    • Regulatory peptide metabolism at cell surfaces: The key role of endopeptidase-24.11
    • Kenny, A. J. Regulatory peptide metabolism at cell surfaces: the key role of endopeptidase-24.11 Biomed. Biochim. Acta 1986, 45, 1503-1513
    • (1986) Biomed. Biochim. Acta , vol.45 , pp. 1503-1513
    • Kenny, A.J.1
  • 66
    • 0022922648 scopus 로고
    • Characterization of three aminopeptidases purified from maternal serum
    • Lalu, K.; Lampelo, S.; Vanha-Perttula, T. Characterization of three aminopeptidases purified from maternal serum Biochim. Biophys. Acta 1986, 873, 190-197
    • (1986) Biochim. Biophys. Acta , vol.873 , pp. 190-197
    • Lalu, K.1    Lampelo, S.2    Vanha-Perttula, T.3
  • 67
    • 0035173732 scopus 로고    scopus 로고
    • Mutational analysis of the active site of human insulin-regulated aminopeptidase
    • Laustsen, P. G.; Vang, S.; Kristensen, T. Mutational analysis of the active site of human insulin-regulated aminopeptidase Eur. J. Biochem. 2001, 268, 98-104
    • (2001) Eur. J. Biochem. , vol.268 , pp. 98-104
    • Laustsen, P.G.1    Vang, S.2    Kristensen, T.3
  • 69
    • 0343320717 scopus 로고
    • Coordinating properties of the amide bond. Stability and structure of metal ion complexes of peptides and related ligands
    • Sigel, H.; Martin, R. B. Coordinating properties of the amide bond. Stability and structure of metal ion complexes of peptides and related ligands Chem. Rev. 1982, 82, 385-426
    • (1982) Chem. Rev. , vol.82 , pp. 385-426
    • Sigel, H.1    Martin, R.B.2
  • 70
    • 44949104409 scopus 로고    scopus 로고
    • Identification of modulating residues defining the catalytic cleft of insulin-regulated aminopeptidase
    • Ye, S.; Chai, S. Y.; Lew, R. A.; Ascher, D. B.; Morton, C. J.; Parker, M. W.; Albiston, A. L. Identification of modulating residues defining the catalytic cleft of insulin-regulated aminopeptidase Biochem. Cell Biol. 2008, 86, 251-261
    • (2008) Biochem. Cell Biol. , vol.86 , pp. 251-261
    • Ye, S.1    Chai, S.Y.2    Lew, R.A.3    Ascher, D.B.4    Morton, C.J.5    Parker, M.W.6    Albiston, A.L.7
  • 71
    • 51849151991 scopus 로고    scopus 로고
    • Structure-based dissection of the active site chemistry of leukotriene A4 hydrolase: Implications for M1 aminopeptidases and inhibitor design
    • Tholander, F.; Muroya, A.; Roques, B. P.; Fournie-Zaluski, M. C.; Thunnissen, M. M.; Haeggstrom, J. Z. Structure-based dissection of the active site chemistry of leukotriene A4 hydrolase: implications for M1 aminopeptidases and inhibitor design Chem. Biol. 2008, 15, 920-929
    • (2008) Chem. Biol. , vol.15 , pp. 920-929
    • Tholander, F.1    Muroya, A.2    Roques, B.P.3    Fournie-Zaluski, M.C.4    Thunnissen, M.M.5    Haeggstrom, J.Z.6
  • 72
    • 33845954688 scopus 로고    scopus 로고
    • Crystal structure of aminopeptidase N (proteobacteria alanyl aminopeptidase) from Escherichia coli and conformational change of methionine 260 involved in substrate recognition
    • Ito, K.; Nakajima, Y.; Onohara, Y.; Takeo, M.; Nakashima, K.; Matsubara, F.; Ito, T.; Yoshimoto, T. Crystal structure of aminopeptidase N (proteobacteria alanyl aminopeptidase) from Escherichia coli and conformational change of methionine 260 involved in substrate recognition J. Biol. Chem. 2006, 281, 33664-33676
    • (2006) J. Biol. Chem. , vol.281 , pp. 33664-33676
    • Ito, K.1    Nakajima, Y.2    Onohara, Y.3    Takeo, M.4    Nakashima, K.5    Matsubara, F.6    Ito, T.7    Yoshimoto, T.8
  • 73
    • 34047182553 scopus 로고    scopus 로고
    • Insulin-regulated aminopeptidase: Analysis of peptide substrate and inhibitor binding to the catalytic domain
    • Ye, S.; Chai, S. Y.; Lew, R. A.; Albiston, A. L. Insulin-regulated aminopeptidase: analysis of peptide substrate and inhibitor binding to the catalytic domain Biol. Chem. 2007, 388, 399-403
    • (2007) Biol. Chem. , vol.388 , pp. 399-403
    • Ye, S.1    Chai, S.Y.2    Lew, R.A.3    Albiston, A.L.4
  • 75
    • 0000224864 scopus 로고
    • Elucidation of chemical exchange networks by two-dimensional NMR spectroscopy: The heptamethylbenzenonium ion
    • Meier, B. H.; Ernst, R. R. Elucidation of chemical exchange networks by two-dimensional NMR spectroscopy: the heptamethylbenzenonium ion J. Am. Chem. Soc. 1979, 101, 6441-6442
    • (1979) J. Am. Chem. Soc. , vol.101 , pp. 6441-6442
    • Meier, B.H.1    Ernst, R.R.2
  • 76
    • 0345311136 scopus 로고
    • Practical aspects of the E.COSY technique. Measurement of scalar spin-spin coupling constants in peptides
    • Griesinger, C.; Sørensen, O. W.; Ernst, R. R. Practical aspects of the E.COSY technique. Measurement of scalar spin-spin coupling constants in peptides J. Magn. Reson. 1987, 75, 474-492
    • (1987) J. Magn. Reson. , vol.75 , pp. 474-492
    • Griesinger, C.1    Sørensen, O.W.2    Ernst, R.R.3
  • 78
    • 0344778061 scopus 로고
    • Semianalytical treatment of solvation for molecular mechanics and dynamics
    • Still, W. C.; Tempczyk, A.; Hawley, R. C.; Hendrickson, T. Semianalytical treatment of solvation for molecular mechanics and dynamics J. Am. Chem. Soc. 1990, 112, 6127-6129
    • (1990) J. Am. Chem. Soc. , vol.112 , pp. 6127-6129
    • Still, W.C.1    Tempczyk, A.2    Hawley, R.C.3    Hendrickson, T.4
  • 81
    • 20444483055 scopus 로고
    • The relationship between proton-proton NMR coupling-constants and substituent electronegativities-I. An empirical generalization of the Karplus equation
    • Haasnoot, C. A. G.; Deleeuw, F. A. A. M.; Altona, C. The relationship between proton-proton NMR coupling-constants and substituent electronegativities-I. An empirical generalization of the Karplus equation Tetrahedron 1980, 36, 2783-2792
    • (1980) Tetrahedron , vol.36 , pp. 2783-2792
    • Haasnoot, C.A.G.1    Deleeuw, F.A.A.M.2    Altona, C.3
  • 82
    • 0025358427 scopus 로고
    • Biosynthesis of peptide precursors and protease inhibitors using new constitutive and inducible eukaryotic expression vectors
    • Johansen, T. E.; Scholler, M. S.; Tolstoy, S.; Schwartz, T. W. Biosynthesis of peptide precursors and protease inhibitors using new constitutive and inducible eukaryotic expression vectors FEBS Lett. 1990, 267, 289-294
    • (1990) FEBS Lett. , vol.267 , pp. 289-294
    • Johansen, T.E.1    Scholler, M.S.2    Tolstoy, S.3    Schwartz, T.W.4
  • 86
    • 78649524395 scopus 로고    scopus 로고
    • The difference in the magnitude of the SSD values for 12 and 13 originates from the nature of the SSD. Its absolute value depends on the number of used constraints. (42)
    • The difference in the magnitude of the SSD values for 12 and 13 originates from the nature of the SSD. Its absolute value depends on the number of used constraints. (42)


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