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Volumn 82, Issue 6, 2002, Pages 1398-1405

A novel prohormone processing site in aplysia californica: The Leu-Leu rule

Author keywords

Leucine Leucine cleavages; MALDI MS; Neuropeptides; Prohormone processing

Indexed keywords

DIAMINO ACID; EDETIC ACID; HORMONE PRECURSOR; LEUCINE; NEUROPEPTIDE; PEPTIDASE; SYNTHETIC PEPTIDE;

EID: 0036733138     PISSN: 00223042     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1471-4159.2002.01070.x     Document Type: Article
Times cited : (14)

References (20)
  • 1
    • 0017164971 scopus 로고
    • The active centers of Streptomyces griseus protease 3, α-chymotrypsin, and elastase: Enzyme-substrate interactions close to the scissile bond
    • Bauer C.-A., Thompson R. C. and Blout E. R. (1976) The active centers of Streptomyces griseus protease 3, α-chymotrypsin, and elastase: enzyme-substrate interactions close to the scissile bond. Biochemistry 15, 1296-1300.
    • (1976) Biochemistry , vol.15 , pp. 1296-1300
    • Bauer, C.-A.1    Thompson, R.C.2    Blout, E.R.3
  • 2
    • 0033933329 scopus 로고    scopus 로고
    • Biochemical evidence of specific trypsin-chymotrypsin inhibitors in the rhynchobdellid leech, Theromyzon tessulatum
    • Chopin V., Stefano G. and Salzet M. (2000) Biochemical evidence of specific trypsin-chymotrypsin inhibitors in the rhynchobdellid leech, Theromyzon tessulatum. J. Enzyme Inhib. 15, 367-379.
    • (2000) J. Enzyme Inhib. , vol.15 , pp. 367-379
    • Chopin, V.1    Stefano, G.2    Salzet, M.3
  • 5
    • 0028819586 scopus 로고
    • Angiotensinogen-like epitopes are present in the CNS of Aplysia californica and co-localize with urotensin I- and urotensin II-like immunoreactivities in the cerebral ganglia
    • Gonzalez G. C., Roger I., Gonzalez E., Martinez-Padron M., Moore G. J. and Lukowiak K. (1995) Angiotensinogen-like epitopes are present in the CNS of Aplysia californica and co-localize with urotensin I- and urotensin II-like immunoreactivities in the cerebral ganglia. Neuroreport 6, 541-544.
    • (1995) Neuroreport , vol.6 , pp. 541-544
    • Gonzalez, G.C.1    Roger, I.2    Gonzalez, E.3    Martinez-Padron, M.4    Moore, G.J.5    Lukowiak, K.6
  • 6
    • 0019452660 scopus 로고
    • Molecular cloning and characterization of cDNA sequences coding for rat relaxin
    • Hudson P., Haley J., Cronk M., Shine J. and Niall H. (1981) Molecular cloning and characterization of cDNA sequences coding for rat relaxin. Nature 291, 127-131.
    • (1981) Nature , vol.291 , pp. 127-131
    • Hudson, P.1    Haley, J.2    Cronk, M.3    Shine, J.4    Niall, H.5
  • 8
    • 0028879230 scopus 로고
    • Isolation of a renin-like enzyme from the leech Theromyzon tessulatum
    • Laurent V. and Salzet M. (1995) Isolation of a renin-like enzyme from the leech Theromyzon tessulatum. Peptides 16, 1351-1358.
    • (1995) Peptides , vol.16 , pp. 1351-1358
    • Laurent, V.1    Salzet, M.2
  • 9
    • 0033572758 scopus 로고    scopus 로고
    • In situ sequencing of peptides from biological tissues and single cells using MALDI-PSD/CID analysis
    • Li L., Garden R. W., Romanova E. V. and Sweedler J. V. (1999) In situ sequencing of peptides from biological tissues and single cells using MALDI-PSD/CID analysis. Anal. Chem. 71, 5451-5458.
    • (1999) Anal. Chem. , vol.71 , pp. 5451-5458
    • Li, L.1    Garden, R.W.2    Romanova, E.V.3    Sweedler, J.V.4
  • 10
    • 0034176654 scopus 로고    scopus 로고
    • Single-cell MALDI: A new tool for direct peptide profiling
    • Li L., Garden R. W. and Sweedler J. V. (2000) Single-cell MALDI: a new tool for direct peptide profiling. Trends Biotechnol. 18, 151-160.
    • (2000) Trends Biotechnol. , vol.18 , pp. 151-160
    • Li, L.1    Garden, R.W.2    Sweedler, J.V.3
  • 11
    • 0031758717 scopus 로고    scopus 로고
    • Mass spectrometric survey of interganglionically transported peptides in Aplysia
    • Li L., Moroz T. P., Garden R. W., Floyd P. D., Weiss K. R. and Sweedler J. V. (1998) Mass spectrometric survey of interganglionically transported peptides in Aplysia. Peptides 19, 1425-1433.
    • (1998) Peptides , vol.19 , pp. 1425-1433
    • Li, L.1    Moroz, T.P.2    Garden, R.W.3    Floyd, P.D.4    Weiss, K.R.5    Sweedler, J.V.6
  • 12
    • 0024278787 scopus 로고
    • Proteolytic processing of egg-laying hormone-related precursors in Aplysia
    • Nagle G. T., Painter S. D., Blankenship J. E. and Kurosky A. (1988) Proteolytic processing of egg-laying hormone-related precursors in Aplysia. J. Biol. Chem. 263, 9223-9237.
    • (1988) J. Biol. Chem. , vol.263 , pp. 9223-9237
    • Nagle, G.T.1    Painter, S.D.2    Blankenship, J.E.3    Kurosky, A.4
  • 13
    • 0030345078 scopus 로고    scopus 로고
    • Serine proteinase inhibitors from insect hemolymph
    • Polanowski A. and Wilusz T. (1996) Serine proteinase inhibitors from insect hemolymph. Acta Biochim. Pol. 43, 445-453.
    • (1996) Acta Biochim. Pol. , vol.43 , pp. 445-453
    • Polanowski, A.1    Wilusz, T.2
  • 14
    • 0030748779 scopus 로고    scopus 로고
    • A renin-like enzyme in the leech Theromyzon tessulatum
    • Salzet M. and Stefano G. (1997) A renin-like enzyme in the leech Theromyzon tessulatum. Mol. Cell Biol. 131, 1-8.
    • (1997) Mol. Cell Biol. , vol.131 , pp. 1-8
    • Salzet, M.1    Stefano, G.2
  • 17
    • 0021272399 scopus 로고
    • Golgi/granule processing of peptide hormone and neuropeptide precursors: A minireview
    • Steiner D. F., Docherty K. and Carroll R. (1984) Golgi/granule processing of peptide hormone and neuropeptide precursors: a minireview. J. Cell Biochem. 24, 121-130.
    • (1984) J. Cell Biochem. , vol.24 , pp. 121-130
    • Steiner, D.F.1    Docherty, K.2    Carroll, R.3
  • 18
    • 0017812750 scopus 로고
    • Amino acid sequence of honeybee prepromelittin synthesized in vitro
    • Suchanek G., Kreil G. and Hermodson M. A. (1978) Amino acid sequence of honeybee prepromelittin synthesized in vitro. Proc. Natl Acad. Sci. USA 75, 701-704.
    • (1978) Proc. Natl. Acad. Sci. USA , vol.75 , pp. 701-704
    • Suchanek, G.1    Kreil, G.2    Hermodson, M.A.3
  • 20
    • 0034132245 scopus 로고    scopus 로고
    • Mono- and dibasic proteolytic cleavage sites in insect neuroendocrine peptide precursors
    • Veenstra J. A. (2000) Mono- and dibasic proteolytic cleavage sites in insect neuroendocrine peptide precursors. Arch. Insect Biochem. Physiol. 43, 49-63.
    • (2000) Arch. Insect Biochem. Physiol. , vol.43 , pp. 49-63
    • Veenstra, J.A.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.