메뉴 건너뛰기




Volumn 389, Issue 2, 2005, Pages 569-576

Structure-activity studies with high-affinity inhibitors of pyroglutamyl-peptidase II

Author keywords

Pyroglutamyl peptidase II (PPII); Pyroglutamyl peptidase II inhibitor; Thyrotropin releasing hormone (TRH); Thyrotropin releasing hormone degrading ectoenzyme (TRH DE); Thyrotropin releasing hormone degrading ectoenzyme inhibitor

Indexed keywords

AMINO ACIDS; CHEMICAL MODIFICATION; ENZYME KINETICS; HORMONES; SYNTHESIS (CHEMICAL);

EID: 22544440278     PISSN: 02646021     EISSN: None     Source Type: Journal    
DOI: 10.1042/BJ20041722     Document Type: Article
Times cited : (10)

References (50)
  • 1
    • 0018459284 scopus 로고
    • Mechanisms of inactivation of hypothalamic regulatory hormones
    • Griffiths, E. C. and Kelly, J. A. (1979) Mechanisms of inactivation of hypothalamic regulatory hormones. Mol. Cell. Endocrinol. 14, 3-17
    • (1979) Mol. Cell. Endocrinol. , vol.14 , pp. 3-17
    • Griffiths, E.C.1    Kelly, J.A.2
  • 2
    • 0002596215 scopus 로고
    • What are ectoenzymes?
    • (Kenny, A.J. and Turner, T. eds.), Elsevier Science Publishers, New York
    • Kenny, A. J. and Turner, T. (1987) What are ectoenzymes? In Mammalian Ectoenzymes (Kenny, A.J. and Turner, T. eds.), pp. 1-13, Elsevier Science Publishers, New York
    • (1987) Mammalian Ectoenzymes , pp. 1-13
    • Kenny, A.J.1    Turner, T.2
  • 3
    • 0002854686 scopus 로고
    • Neuropeptide inactivation by peptidases
    • (O'Cuinn, G., ed.), CRC Press, Boca Raton
    • O'Cuinn, G., O'Connor, B., Gilmartin, L. and Smyth, M. (1995) Neuropeptide inactivation by peptidases. In Metabolism of Brain Peptides (O'Cuinn, G., ed.), pp. 99-157, CRC Press, Boca Raton
    • (1995) Metabolism of Brain Peptides , pp. 99-157
    • O'Cuinn, G.1    O'Connor, B.2    Gilmartin, L.3    Smyth, M.4
  • 4
    • 0030219801 scopus 로고    scopus 로고
    • Ectoenzymes as sites of peptide regulation
    • Konkoy, C. S. and Davis, T. P. (1996) Ectoenzymes as sites of peptide regulation. Trends Pharmacol. Sci. 17, 288-294
    • (1996) Trends Pharmacol. Sci. , vol.17 , pp. 288-294
    • Konkoy, C.S.1    Davis, T.P.2
  • 5
    • 0006010908 scopus 로고    scopus 로고
    • Neuropeptide inactivation in the CNS
    • (Kenny, A. J. and Boustead, C. M., eds.), BIOS Scientific Publishers, Oxford
    • Turner, A. J. (1997) Neuropeptide inactivation in the CNS. In Cell-Surface Peptidases in Health and Disease (Kenny, A. J. and Boustead, C. M., eds.), pp. 275-310, BIOS Scientific Publishers, Oxford
    • (1997) Cell-Surface Peptidases in Health and Disease , pp. 275-310
    • Turner, A.J.1
  • 6
    • 0023790922 scopus 로고
    • The narrow specificity pyroglutamate aminopeptidase degrading TRH in rat brain is an ectoenzyme
    • Charli, J. L., Cruz, C., Vargas, M. A. and Joseph-Bravo, P. (1988) The narrow specificity pyroglutamate aminopeptidase degrading TRH in rat brain is an ectoenzyme. Neurochem. Int. 13, 237-242
    • (1988) Neurochem. Int. , vol.13 , pp. 237-242
    • Charli, J.L.1    Cruz, C.2    Vargas, M.A.3    Joseph-Bravo, P.4
  • 7
    • 0025098194 scopus 로고
    • Degradation of thyrotropin-releasing hormone-degrading ectoenzyme and luteinising hormone-releasing hormone by enzymes of brain tissue
    • O'Cuinn, G., O'Connor, B. and Elmore, M. (1990) Degradation of thyrotropin-releasing hormone-degrading ectoenzyme and luteinising hormone-releasing hormone by enzymes of brain tissue. J. Neurochem. 54, 1-13
    • (1990) J. Neurochem. , vol.54 , pp. 1-13
    • O'Cuinn, G.1    O'Connor, B.2    Elmore, M.3
  • 9
    • 0034596063 scopus 로고    scopus 로고
    • Kinetic investigation of the specificity of porcine brain thyrotropin-releasing hormone-degrading ectoenzyme for thyrotropin-releasing hormone-like peptides
    • Kelly, J. A., Slator, G. R., Tipton, K. F., Williams, C. H. and Bauer, K. (2000) Kinetic investigation of the specificity of porcine brain thyrotropin-releasing hormone-degrading ectoenzyme for thyrotropin-releasing hormone-like peptides. J. Biol. Chem. 275, 16746-16751
    • (2000) J. Biol. Chem. , vol.275 , pp. 16746-16751
    • Kelly, J.A.1    Slator, G.R.2    Tipton, K.F.3    Williams, C.H.4    Bauer, K.5
  • 10
    • 0032424256 scopus 로고    scopus 로고
    • Pyroglutamyl peptidase: An overview of the three known enzymatic forms
    • Cummins, P. M. and O'Connor, B. (1998) Pyroglutamyl peptidase: an overview of the three known enzymatic forms. Biochim. Biophys. Acta 1429, 1-17
    • (1998) Biochim. Biophys. Acta , vol.1429 , pp. 1-17
    • Cummins, P.M.1    O'Connor, B.2
  • 11
    • 0002621068 scopus 로고    scopus 로고
    • The chemistry and pharmacology of cell-surface peptidase inhibitors
    • (Kenny, A. J. and Boustead, C. M., eds.), BIOS Scientific Publishers, Oxford, U.K.
    • Beaumont, A., Fournié-Zaluski, M.-C., Noble, F., Maldonado, R. and Roques, B. P. (1997) The chemistry and pharmacology of cell-surface peptidase inhibitors. In Cell-Surface Peptidases in Health and Disease (Kenny, A. J. and Boustead, C. M., eds.), pp. 59-78, BIOS Scientific Publishers, Oxford, U.K.
    • (1997) Cell-Surface Peptidases in Health and Disease , pp. 59-78
    • Beaumont, A.1    Fournié-Zaluski, M.-C.2    Noble, F.3    Maldonado, R.4    Roques, B.P.5
  • 12
    • 0034387741 scopus 로고    scopus 로고
    • Novel approaches to targeting neuropeptide systems
    • Roques, B. P. (2000) Novel approaches to targeting neuropeptide systems. Trends Pharmacol. Sci. 21, 475-483
    • (2000) Trends Pharmacol. Sci. , vol.21 , pp. 475-483
    • Roques, B.P.1
  • 13
    • 0032828165 scopus 로고    scopus 로고
    • Design of angiotensin converting enzyme inhibitors
    • Cushman, D. W. and Ondetti, M. A. (1999) Design of angiotensin converting enzyme inhibitors. Nat. Med. 5, 1110-1112
    • (1999) Nat. Med. , vol.5 , pp. 1110-1112
    • Cushman, D.W.1    Ondetti, M.A.2
  • 15
    • 0026540898 scopus 로고
    • Pharmacological strategies in CNS trauma
    • Faden, A. I. and Salzman, S. (1992) Pharmacological strategies in CNS trauma. Trends Pharmacol. Sci. 13, 29-35
    • (1992) Trends Pharmacol. Sci. , vol.13 , pp. 29-35
    • Faden, A.I.1    Salzman, S.2
  • 16
    • 0032571346 scopus 로고    scopus 로고
    • An update on the CNS actions of TRH and its analogs
    • Horita, A. (1998) An update on the CNS actions of TRH and its analogs. Life Sci. 62, 1443-1448
    • (1998) Life Sci. , vol.62 , pp. 1443-1448
    • Horita, A.1
  • 17
    • 0029433870 scopus 로고
    • Thyrotropin-releasing hormone: Basis and potential for its therapeutic use
    • Kelly, J. A. (1995) Thyrotropin-releasing hormone: basis and potential for its therapeutic use. Essays Biochem. 30, 133-149
    • (1995) Essays Biochem. , vol.30 , pp. 133-149
    • Kelly, J.A.1
  • 18
    • 0000562053 scopus 로고
    • Thyrotropin-releasing hormone: Focus on basic neurobiology
    • (Bloom, F. E. and Kupfer, D. J., eds.), Raven Press, New York
    • Mason, G., Garbutt, J. and Prange, A. J. (1995) Thyrotropin-releasing hormone: focus on basic neurobiology. In Psychopharmacology: the Fourth Generation of Progress (Bloom, F. E. and Kupfer, D. J., eds.), pp. 495-503, Raven Press, New York
    • (1995) Psychopharmacology: The Fourth Generation of Progress , pp. 495-503
    • Mason, G.1    Garbutt, J.2    Prange, A.J.3
  • 19
    • 0033305169 scopus 로고    scopus 로고
    • The biology of pro-thyrotropin-releasing hormone-derived peptides
    • Nillni, E. A. and Sevarino, K. A. (1999) The biology of pro-thyrotropin-releasing hormone-derived peptides. Endocr. Rev. 20, 599-648
    • (1999) Endocr. Rev. , vol.20 , pp. 599-648
    • Nillni, E.A.1    Sevarino, K.A.2
  • 20
    • 0034730476 scopus 로고    scopus 로고
    • Antidepressants: Past, present and future
    • Vetulani, J. and Nalepa, I. (2000) Antidepressants: past, present and future. Eur. J. Pharmacol. 405, 351-363
    • (2000) Eur. J. Pharmacol. , vol.405 , pp. 351-363
    • Vetulani, J.1    Nalepa, I.2
  • 21
    • 0034812679 scopus 로고    scopus 로고
    • CSF thyrotropin-releasing hormone concentrations differ in patients with schizoaffective disorder from patients with schizophrenia or mood disorders
    • Sharma, R. P., Martis, B., Rosen, C., Jonalagadda, J., Nemeroff, C. B. and Bissette, G. (2001) CSF thyrotropin-releasing hormone concentrations differ in patients with schizoaffective disorder from patients with schizophrenia or mood disorders. J. Psychiatr. Res. 35, 287-291
    • (2001) J. Psychiatr. Res. , vol.35 , pp. 287-291
    • Sharma, R.P.1    Martis, B.2    Rosen, C.3    Jonalagadda, J.4    Nemeroff, C.B.5    Bissette, G.6
  • 22
    • 0037110654 scopus 로고    scopus 로고
    • Lithium modulates expression of TRH receptors and TRH-related peptides in rat brain
    • Sattin, A., Senanayake, S. S. and Pekary, A. E. (2002) Lithium modulates expression of TRH receptors and TRH-related peptides in rat brain. Neuroscience 115, 263-273
    • (2002) Neuroscience , vol.115 , pp. 263-273
    • Sattin, A.1    Senanayake, S.S.2    Pekary, A.E.3
  • 23
    • 0036163653 scopus 로고    scopus 로고
    • Thyrotropin-releasing hormone in the treatment of intractable epilepsy
    • Kubek, M. J. and Garg, B. P. (2002) Thyrotropin-releasing hormone in the treatment of intractable epilepsy. Pediatr. Neurol. 26, 9-17
    • (2002) Pediatr. Neurol. , vol.26 , pp. 9-17
    • Kubek, M.J.1    Garg, B.P.2
  • 24
    • 0037405712 scopus 로고    scopus 로고
    • The thyrotropin-releasing hormone (TRH) hypothesis of homeostatic regulation: Implications for TRH-based therapeutics
    • Gary, K. A., Sevarino, K. A., Yarbrough, G. G., Prange, Jr, A. J. and Winokur, A. (2003) The thyrotropin-releasing hormone (TRH) hypothesis of homeostatic regulation: implications for TRH-based therapeutics. J. Pharmacol. Exp. Ther. 305, 410-416
    • (2003) J. Pharmacol. Exp. Ther. , vol.305 , pp. 410-416
    • Gary, K.A.1    Sevarino, K.A.2    Yarbrough, G.G.3    Prange Jr., A.J.4    Winokur, A.5
  • 25
    • 0028111423 scopus 로고
    • Cloning of a cDNA encoding an ectoenzyme that degrades thyrotropin-releasing hormone
    • Schauder, B., Schomburg, L., Kohrle, J. and Bauer, K. (1994) Cloning of a cDNA encoding an ectoenzyme that degrades thyrotropin-releasing hormone. Proc. Natl. Acad. Sci. U.S.A. 91, 9534-9538
    • (1994) Proc. Natl. Acad. Sci. U.S.A. , vol.91 , pp. 9534-9538
    • Schauder, B.1    Schomburg, L.2    Kohrle, J.3    Bauer, K.4
  • 26
    • 0035822653 scopus 로고    scopus 로고
    • Mutational analysis of the thyrotropin-releasing hormone-degrading ectoenzyme: Similarities and differences with other members of the M1 family of aminopeptidases and thermolysin
    • Papadopoulas, T., Kelly, J. A. and Bauer, K. (2001) Mutational analysis of the thyrotropin-releasing hormone-degrading ectoenzyme: similarities and differences with other members of the M1 family of aminopeptidases and thermolysin. Biochemistry 40, 9347-9355
    • (2001) Biochemistry , vol.40 , pp. 9347-9355
    • Papadopoulas, T.1    Kelly, J.A.2    Bauer, K.3
  • 27
    • 0037047301 scopus 로고    scopus 로고
    • Contribution of molecular modeling and site-directed mutagenesis to the identification of two structural residues, Arg-220 and Asp-227, in aminopeptidase A
    • Rozenfeld, R., Iturrioz, X., Maigret, B. and Llorens-Cortes, C. (2002) Contribution of molecular modeling and site-directed mutagenesis to the identification of two structural residues, Arg-220 and Asp-227, in aminopeptidase A. J. Biol. Chem. 277, 29242-29252
    • (2002) J. Biol. Chem. , vol.277 , pp. 29242-29252
    • Rozenfeld, R.1    Iturrioz, X.2    Maigret, B.3    Llorens-Cortes, C.4
  • 28
    • 0024443859 scopus 로고
    • Inhibitors of TRH-degrading enzymes
    • Wilk, S. (1989) Inhibitors of TRH-degrading enzymes. Ann. N.Y. Acad. Sci. 553, 252-264
    • (1989) Ann. N.Y. Acad. Sci. , vol.553 , pp. 252-264
    • Wilk, S.1
  • 29
    • 0024384817 scopus 로고
    • Pyroglutamyl peptidase II inhibition specifically increases the recovery of TRH released from rat brain slices
    • Charli, J.-L., Mendez, M., Vargas, M.-A., Cisneros, M., Assai, M., Joseph-Bravo, P. and Wilk, S. (1989) Pyroglutamyl peptidase II inhibition specifically increases the recovery of TRH released from rat brain slices. Neuropeptides 14, 191-196
    • (1989) Neuropeptides , vol.14 , pp. 191-196
    • Charli, J.-L.1    Mendez, M.2    Vargas, M.-A.3    Cisneros, M.4    Assai, M.5    Joseph-Bravo, P.6    Wilk, S.7
  • 30
    • 22544458877 scopus 로고    scopus 로고
    • Effects of thyrotropin-releasing hormone-degrading ectoenzyme inhibitors on thyrotropin-releasing hormone actions in vivo
    • Kelly, J. A., Bennett, G. W., Beckett, S., Slator, G. R., Roe, C. H., O'Loinsigh, E. D. and O'Boyle, K. M. (2000) Effects of thyrotropin-releasing hormone-degrading ectoenzyme inhibitors on thyrotropin-releasing hormone actions in vivo. Br. J. Pharmacol. 133, 187P
    • (2000) Br. J. Pharmacol. , vol.133
    • Kelly, J.A.1    Bennett, G.W.2    Beckett, S.3    Slator, G.R.4    Roe, C.H.5    O'Loinsigh, E.D.6    O'Boyle, K.M.7
  • 31
    • 0242317260 scopus 로고    scopus 로고
    • Purification of a specific inhibitor of pyroglutamyl aminopeptidase II from the marine annelide Hermodice carunculata: In vivo effects in rodent brain
    • Pascual, I., Gil-Parrado, S., Cisneros, M., Joseph-Bravo, P., Diaz, J., Possani, L. D., Charli, J. L. and Chavez, M. (2004) Purification of a specific inhibitor of pyroglutamyl aminopeptidase II from the marine annelide Hermodice carunculata: in vivo effects in rodent brain. Int. J. Biochem. Cell Biol. 36, 138-152
    • (2004) Int. J. Biochem. Cell Biol. , vol.36 , pp. 138-152
    • Pascual, I.1    Gil-Parrado, S.2    Cisneros, M.3    Joseph-Bravo, P.4    Diaz, J.5    Possani, L.D.6    Charli, J.L.7    Chavez, M.8
  • 32
    • 0024389791 scopus 로고
    • Pyroglutamyl peptidase II, a thyrotropin releasing hormone degrading enzyme: Purification and substrate specificity studies of the rabbit brain enzyme
    • Wilk, S. and Wilk, E. K. (1989) Pyroglutamyl peptidase II, a thyrotropin releasing hormone degrading enzyme: purification and substrate specificity studies of the rabbit brain enzyme. Neurochem. Int. 15, 81-89
    • (1989) Neurochem. Int. , vol.15 , pp. 81-89
    • Wilk, S.1    Wilk, E.K.2
  • 33
    • 0021864722 scopus 로고
    • Purification of and kinetic studies on a narrow specificity synaptosomal membrane pyroglutamate aminopeptidase from guinea-pig brain
    • O'Connor, B. and O'Cuinn, G. (1985) Purification of and kinetic studies on a narrow specificity synaptosomal membrane pyroglutamate aminopeptidase from guinea-pig brain. Eur. J. Biochem. 150, 47-52
    • (1985) Eur. J. Biochem. , vol.150 , pp. 47-52
    • O'Connor, B.1    O'Cuinn, G.2
  • 34
    • 0025100971 scopus 로고
    • Further characterisation of the substrate specificity of a TRH hydrolysing pyroglutamate aminopeptidase from guinea-pig brain
    • Elmore, M. A., Griffiths, E. C., O'Connor, B. and O'Cuinn, G. (1990) Further characterisation of the substrate specificity of a TRH hydrolysing pyroglutamate aminopeptidase from guinea-pig brain. Neuropeptides 15, 31-36
    • (1990) Neuropeptides , vol.15 , pp. 31-36
    • Elmore, M.A.1    Griffiths, E.C.2    O'Connor, B.3    O'Cuinn, G.4
  • 35
    • 0032546402 scopus 로고    scopus 로고
    • Study of a highly specific pyroglutamyl aminopeptidase type-II from the membrane fraction of bovine brain
    • Gallagher, S. P. and O'Connor, B. (1998) Study of a highly specific pyroglutamyl aminopeptidase type-II from the membrane fraction of bovine brain. Int. J. Biochem. Cell Biol. 30, 115-133
    • (1998) Int. J. Biochem. Cell Biol. , vol.30 , pp. 115-133
    • Gallagher, S.P.1    O'Connor, B.2
  • 36
    • 0001895193 scopus 로고
    • Solid-phase peptide synthesis
    • (Wisdom, G. B., ed.), Oxford University Press, Oxford
    • Walker, B. (1994) Solid-phase peptide synthesis. In Synthetic Antigens: A Practical Approach (Wisdom, G. B., ed.), pp. 27-81, Oxford University Press, Oxford
    • (1994) Synthetic Antigens: A Practical Approach , pp. 27-81
    • Walker, B.1
  • 37
    • 0033569951 scopus 로고    scopus 로고
    • Development of a discontinuous, quantitative HPLC assay for thyrotropin-releasing hormone-degrading ectoenzyme
    • Kelly, J. A., Slator, G. R., Tipton, K. F., Williams, C. H. and Bauer, K. (1999) Development of a discontinuous, quantitative HPLC assay for thyrotropin-releasing hormone-degrading ectoenzyme. Anal. Biochem. 274, 195-202
    • (1999) Anal. Biochem. , vol.274 , pp. 195-202
    • Kelly, J.A.1    Slator, G.R.2    Tipton, K.F.3    Williams, C.H.4    Bauer, K.5
  • 38
    • 0021341951 scopus 로고
    • The effects of 5,7-dihydroxytryptamine and p-chlorophenylalanine on thyrotropin-releasing hormone in regions of the brain and spinal cord of the rat
    • Lighton, C., Marsden, C. A. and Bennett, G. W. (1984) The effects of 5,7-dihydroxytryptamine and p-chlorophenylalanine on thyrotropin-releasing hormone in regions of the brain and spinal cord of the rat. Neuropharmacology 23, 55-60
    • (1984) Neuropharmacology , vol.23 , pp. 55-60
    • Lighton, C.1    Marsden, C.A.2    Bennett, G.W.3
  • 41
    • 0030599010 scopus 로고    scopus 로고
    • A fast flexible docking method using an incremental construction algorithm
    • Rarey, M., Kramer, B., Lengauer, T. and Klebe, G. (1996) A fast flexible docking method using an incremental construction algorithm. J. Mol. Biol. 261, 470-489
    • (1996) J. Mol. Biol. , vol.261 , pp. 470-489
    • Rarey, M.1    Kramer, B.2    Lengauer, T.3    Klebe, G.4
  • 42
    • 0028454828 scopus 로고
    • On the use of LUDI to search the Fine Chemicals Directory for ligands of proteins of known three-dimensional structure
    • Böhm, H.-J. (1994) On the use of LUDI to search the Fine Chemicals Directory for ligands of proteins of known three-dimensional structure. J. Comput. Aided Mol. Des. 8, 243-256
    • (1994) J. Comput. Aided Mol. Des. , vol.8 , pp. 243-256
    • Böhm, H.-J.1
  • 43
    • 0842332235 scopus 로고    scopus 로고
    • A practical approach to docking of zinc metalloproteinase inhibitors
    • Hu, X., Balaz, S. and Shelver, W. H. (2004) A practical approach to docking of zinc metalloproteinase inhibitors. J. Mol. Graphics Modell. 22, 293-307
    • (2004) J. Mol. Graphics Modell. , vol.22 , pp. 293-307
    • Hu, X.1    Balaz, S.2    Shelver, W.H.3
  • 44
    • 4344593122 scopus 로고    scopus 로고
    • The effect of tightly bound water molecules on the structural interpretation of ligand-derived pharmacophore models
    • Lloyd, D. G., García-Sosa, A. T., Alberts, I. L., Todorov, N. P. and Mancera, R. L. (2004) The effect of tightly bound water molecules on the structural interpretation of ligand-derived pharmacophore models. J. Comput. Aided Mol. Des. 18, 89-100
    • (2004) J. Comput. Aided Mol. Des. , vol.18 , pp. 89-100
    • Lloyd, D.G.1    García-Sosa, A.T.2    Alberts, I.L.3    Todorov, N.P.4    Mancera, R.L.5
  • 45
    • 0037059334 scopus 로고    scopus 로고
    • 4 hydrolase/aminopeptidase: Glutamate 271 is a catalytic residue with specific roles in two distinct enzyme mechanisms
    • 4 hydrolase/aminopeptidase: glutamate 271 is a catalytic residue with specific roles in two distinct enzyme mechanisms. J. Biol. Chem. 277, 1398-1404
    • (2002) J. Biol. Chem. , vol.277 , pp. 1398-1404
    • Rudberg, P.C.1    Tholander, F.2    Thunnissen, M.M.3    Haeggstrom, J.Z.4
  • 46
    • 0021933588 scopus 로고
    • Probing histidine-substrate interactions in tyrosyl-tRNA synthetase using asparagine and glutamine replacements
    • Lowe, D. M., Fersht, A. R., Wilkinson, A. J., Carter, P. and Winter, G. (1985) Probing histidine-substrate interactions in tyrosyl-tRNA synthetase using asparagine and glutamine replacements. Biochemistry 24, 5106-5109
    • (1985) Biochemistry , vol.24 , pp. 5106-5109
    • Lowe, D.M.1    Fersht, A.R.2    Wilkinson, A.J.3    Carter, P.4    Winter, G.5
  • 47
    • 0033215130 scopus 로고    scopus 로고
    • Human TRH-degrading ectoenzyme: CDNA cloning, functional expression, genomic structure and chromosomal assignment
    • Schomburg, L., Turwitt, S., Prescher, G., Lohmann, D., Horsthemke, B. and Bauer, K. (1999) Human TRH-degrading ectoenzyme: cDNA cloning, functional expression, genomic structure and chromosomal assignment. Eur. J. Biochem. 265, 415-422
    • (1999) Eur. J. Biochem. , vol.265 , pp. 415-422
    • Schomburg, L.1    Turwitt, S.2    Prescher, G.3    Lohmann, D.4    Horsthemke, B.5    Bauer, K.6
  • 48
    • 0031767267 scopus 로고    scopus 로고
    • Differences in transition state stabilization between thermolysin (EC 3.4.24.27) and neprilysin (EC 3.4.24.11)
    • Marie-Claire, C., Ruffet, E., Tiraboschi, G. and Fournié-Zaluski, M.-C. (1998) Differences in transition state stabilization between thermolysin (EC 3.4.24.27) and neprilysin (EC 3.4.24.11). FEBS Lett. 438, 215-219
    • (1998) FEBS Lett. , vol.438 , pp. 215-219
    • Marie-Claire, C.1    Ruffet, E.2    Tiraboschi, G.3    Fournié-Zaluski, M.-C.4
  • 50
    • 0037013278 scopus 로고    scopus 로고
    • The effects of modifying the surface charge on the catalytic activity of a thermolysin-like protease
    • de Kreij, A., van den Burg, B., Venema, G., Vriend, G., Eijsink, V. G. H. and Nielsen, J. E. (2002) The effects of modifying the surface charge on the catalytic activity of a thermolysin-like protease. J. Biol. Chem. 277, 15432-15438
    • (2002) J. Biol. Chem. , vol.277 , pp. 15432-15438
    • De Kreij, A.1    Van Den Burg, B.2    Venema, G.3    Vriend, G.4    Eijsink, V.G.H.5    Nielsen, J.E.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.