메뉴 건너뛰기




Volumn 10, Issue 1, 2006, Pages 9-16

Hinge peptide combinatorial libraries for inhibitors of botulinum neurotoxins and saxitoxin: Deconvolution strategy

Author keywords

Botulinum neurotoxin; Combinatorial; Deconvolution strategy; Hinge peptide libraries; Saxitoxin

Indexed keywords

4 AMINOBUTYRIC ACID; AMINO ACID; BOTULINUM TOXIN A; BOTULINUM TOXIN B; CAPTOPRIL; OUABAIN; PEPTIDE; PROTEINASE; SAXITOXIN; UNCLASSIFIED DRUG; VERATRIDINE; ZINC PROTEASE;

EID: 30744431863     PISSN: 13811991     EISSN: None     Source Type: Journal    
DOI: 10.1007/s11030-006-1394-2     Document Type: Article
Times cited : (12)

References (20)
  • 1
    • 0026419319 scopus 로고
    • Generation and use of synthetic peptide combinatorial libraries for basic research and drug discovery
    • Houghten, R.A., Pinilla, C., Blondelle, S.E., Appel, J.R., Dooley, C.T. and Cuervo, J.H., Generation and use of synthetic peptide combinatorial libraries for basic research and drug discovery, Nature, 354 (1991) 84-86.
    • (1991) Nature , vol.354 , pp. 84-86
    • Houghten, R.A.1    Pinilla, C.2    Blondelle, S.E.3    Appel, J.R.4    Dooley, C.T.5    Cuervo, J.H.6
  • 2
    • 0032500530 scopus 로고    scopus 로고
    • Identification of inhibitors of prohormone convertases 1 and 2 using a peptide combinatorial library
    • Apletalina, E., Appel, J., Lamango, N.S., Houghten, R.A. and Lindberg I., Identification of inhibitors of prohormone convertases 1 and 2 using a peptide combinatorial library, J. Biol. Chem., 273 (1998) 26589-26595.
    • (1998) J. Biol. Chem. , vol.273 , pp. 26589-26595
    • Apletalina, E.1    Appel, J.2    Lamango, N.S.3    Houghten, R.A.4    Lindberg, I.5
  • 3
    • 0036245078 scopus 로고    scopus 로고
    • Identification of novel hexapeptides bioactive against phytopathogenic fungi through screening of a synthetic peptide combinatorial library
    • Lopez-Garcia, B., Perez-Paya, E. and Marcos, J.F., Identification of novel hexapeptides bioactive against phytopathogenic fungi through screening of a synthetic peptide combinatorial library, Appl. Environ. Microbiol., 68 (2002) 2453-2460.
    • (2002) Appl. Environ. Microbiol. , vol.68 , pp. 2453-2460
    • Lopez-Garcia, B.1    Perez-Paya, E.2    Marcos, J.F.3
  • 4
    • 0037238058 scopus 로고    scopus 로고
    • Combinatorial peptide library methods for immunobiology research
    • Liu, R., Enstrom, A.M. and Lam, K.S., Combinatorial peptide library methods for immunobiology research, Exp. Hematol., 31 (2003) 11-30.
    • (2003) Exp. Hematol. , vol.31 , pp. 11-30
    • Liu, R.1    Enstrom, A.M.2    Lam, K.S.3
  • 6
    • 0028293066 scopus 로고
    • Designing peptide mimetics
    • Moore, G.J., Designing peptide mimetics, Trends Pharmacol. Sci., 15 (1994) 124-129.
    • (1994) Trends Pharmacol. Sci. , vol.15 , pp. 124-129
    • Moore, G.J.1
  • 7
    • 0037258549 scopus 로고    scopus 로고
    • Discovery and design of novel inhibitors of botulinum neurotoxin A: Targeted "hinge" peptide libraries
    • Hayden, J., Pires, J., Roy, S., Hamilton, M. and Moore, G.J., Discovery and design of novel inhibitors of botulinum neurotoxin A: targeted "hinge" peptide libraries, J. Appl. Toxicol. 23 (2003) 1-7.
    • (2003) J. Appl. Toxicol. , vol.23 , pp. 1-7
    • Hayden, J.1    Pires, J.2    Roy, S.3    Hamilton, M.4    Moore, G.J.5
  • 8
    • 0031393804 scopus 로고    scopus 로고
    • "Hinge" peptide libraries in basic research and drug development: Application to breast cancer and multiple sclerosis
    • Moore, G.J., "Hinge" peptide libraries in basic research and drug development: application to breast cancer and multiple sclerosis, Drug Devel. Res., 42 (1997) 157-163.
    • (1997) Drug Devel. Res. , vol.42 , pp. 157-163
    • Moore, G.J.1
  • 9
    • 0027052983 scopus 로고
    • Rapid identification of high affinity peptide ligands using positional scanning synthetic peptide combinatorial libraries
    • Pinilla, C., Appel, J.R., Blanc, P. and Houghten, R.A., Rapid identification of high affinity peptide ligands using positional scanning synthetic peptide combinatorial libraries, Biotechniques, 13 (1992) 901-905.
    • (1992) Biotechniques , vol.13 , pp. 901-905
    • Pinilla, C.1    Appel, J.R.2    Blanc, P.3    Houghten, R.A.4
  • 11
    • 0033887403 scopus 로고    scopus 로고
    • Cocrystal structure of synaptobrevin-II bound to botulinum neurotoxin type B at 2.0 Angstroms resolution
    • Hanson, M.A. and Stevens, R.C., Cocrystal structure of synaptobrevin-II bound to botulinum neurotoxin type B at 2.0 Angstroms resolution, Nature Struct. Biol., 7 (2000) 687-693.
    • (2000) Nature Struct. Biol. , vol.7 , pp. 687-693
    • Hanson, M.A.1    Stevens, R.C.2
  • 12
    • 0037132540 scopus 로고    scopus 로고
    • A high affinity competitive inhibitor of type a botulinum neurotoxin protease activity
    • Schmidt, J.J. and Stafford, R.G., A high affinity competitive inhibitor of type A botulinum neurotoxin protease activity, FEBS Lett., 18 (2002) 423-426.
    • (2002) FEBS Lett. , vol.18 , pp. 423-426
    • Schmidt, J.J.1    Stafford, R.G.2
  • 13
    • 0035870840 scopus 로고    scopus 로고
    • High-throughput fluorogenic assay for determination of botulinum type B neurotoxin protease activity
    • Anne, C., Cornille, F., Lenoir, C. and Roques, B.P., High-throughput fluorogenic assay for determination of botulinum type B neurotoxin protease activity, Anal. Biochem., 291 (2001) 253-261.
    • (2001) Anal. Biochem. , vol.291 , pp. 253-261
    • Anne, C.1    Cornille, F.2    Lenoir, C.3    Roques, B.P.4
  • 14
    • 0026548114 scopus 로고
    • Properties and use of botulinum toxin and other microbial neurotoxins in medicine
    • Schantz, E.J. and Johnson, E.A,. Properties and use of botulinum toxin and other microbial neurotoxins in medicine, Microbiol. Rev., 56 (1992) 80-99.
    • (1992) Microbiol. Rev. , vol.56 , pp. 80-99
    • Schantz, E.J.1    Johnson, E.A.2
  • 15
    • 0027521670 scopus 로고
    • Tetrazolium-based cell bioassay for neurotoxins active on voltage-sensitive sodium channels: Semiautomated assay for saxitoxins, brevetoxins, and ciguatoxins
    • Manger, R.L., Leja, L.S., Lee, S.Y., Hungerford, J.M. and Wekell, M.M., Tetrazolium-based cell bioassay for neurotoxins active on voltage-sensitive sodium channels: Semiautomated assay for saxitoxins, brevetoxins, and ciguatoxins, Anal. Biochem., 14 (1993) 190-194.
    • (1993) Anal. Biochem. , vol.14 , pp. 190-194
    • Manger, R.L.1    Leja, L.S.2    Lee, S.Y.3    Hungerford, J.M.4    Wekell, M.M.5
  • 16
    • 0033368312 scopus 로고    scopus 로고
    • A natural peptide, inhibits botulinum neurotoxin B activity in vitro
    • Garcia, G.E., Moorad, D.R., Gordon, R.K. and Buforin, I., A natural peptide, inhibits botulinum neurotoxin B activity in vitro, J. Appl. Toxicol., 19(S-1) (1999) S19-S22.
    • (1999) J. Appl. Toxicol. , vol.19 , Issue.S-1
    • Garcia, G.E.1    Moorad, D.R.2    Gordon, R.K.3    Buforin, I.4
  • 17
    • 0029041265 scopus 로고
    • Peptidyl dipeptidase A: AngiotensinI-converting enzyme
    • Corvol, P., Williams, T.A. and Soubrier, F., Peptidyl dipeptidase A: AngiotensinI-converting enzyme, Methods Enzymol., 248 (1995) 283-305.
    • (1995) Methods Enzymol. , vol.248 , pp. 283-305
    • Corvol, P.1    Williams, T.A.2    Soubrier, F.3
  • 18
    • 0030981239 scopus 로고    scopus 로고
    • Substrate dependence of angiotensin I-converting enzyme inhibition: Captopril displays a partial selectivity for inhibition of N-acetyl-seryl- aspartyl-lysyl-proline hydrolysis compared with that of angiotensin I
    • Michaud, A., Williams, T.A., Chauvet, M.T. and Corvol, P., Substrate dependence of angiotensin I-converting enzyme inhibition: Captopril displays a partial selectivity for inhibition of N-acetyl-seryl-aspartyl-lysyl-proline hydrolysis compared with that of angiotensin I, Mol. Pharmacol., 51 (1997) 1070-1076.
    • (1997) Mol. Pharmacol. , vol.51 , pp. 1070-1076
    • Michaud, A.1    Williams, T.A.2    Chauvet, M.T.3    Corvol, P.4
  • 19
    • 0028558884 scopus 로고
    • Differences in the protease activities of tetanus and botulinum B toxins revealed by the cleavage of vesicle-associated membrane protein and various sized fragments
    • Foran, P., Shone, C.C. and Dolly, J.O., Differences in the protease activities of tetanus and botulinum B toxins revealed by the cleavage of vesicle-associated membrane protein and various sized fragments, Biochemistry, 33 (1994) 15365-15374.
    • (1994) Biochemistry , vol.33 , pp. 15365-15374
    • Foran, P.1    Shone, C.C.2    Dolly, J.O.3
  • 20
    • 0036393768 scopus 로고    scopus 로고
    • Discovery of nonpeptide, peptidomimetic peptidase inhibitors that target alternate enzyme active site conformations
    • Rich, D.H., Bursavich, M.G. and Estiarte, M.A., Discovery of nonpeptide, peptidomimetic peptidase inhibitors that target alternate enzyme active site conformations, Biopolymers, 66 (2002) 115-125.
    • (2002) Biopolymers , vol.66 , pp. 115-125
    • Rich, D.H.1    Bursavich, M.G.2    Estiarte, M.A.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.