메뉴 건너뛰기




Volumn 32, Issue 5, 1999, Pages 645-649

Detection of the basement membrane-degrading proteolytic activity of Paracoccidioides brasiliensis after SDS-PAGE using agarose overlays containing Abz-MKALTLQ-EDDnp

Author keywords

Fluorescent quenched peptides; P. brasiliensis; SDS PAGE; Serine thiol proteinase

Indexed keywords

PARACOCCIDIOIDES BRASILIENSIS;

EID: 0033125570     PISSN: 0100879X     EISSN: 1414431X     Source Type: Journal    
DOI: 10.1590/S0100-879X1999000500019     Document Type: Article
Times cited : (16)

References (14)
  • 1
    • 84907130727 scopus 로고
    • Host-parasite relationships in paracoccidioidomycosis
    • Franco M (1987). Host-parasite relationships in paracoccidioidomycosis. Journal of Medical and Veterinary Mycology, 25: 5-18.
    • (1987) Journal of Medical and Veterinary Mycology , vol.25 , pp. 5-18
    • Franco, M.1
  • 2
    • 0003056291 scopus 로고
    • Biochemistry of Paracoccidioides brasiliensis dimorphism
    • Franco M, Lacaz CS, Restrepo-Moreno A & Del Negro C (Editors), CRC Press, Boca Raton
    • San-Blas G & San-Bias F (1994). Biochemistry of Paracoccidioides brasiliensis dimorphism. In: Franco M, Lacaz CS, Restrepo-Moreno A & Del Negro C (Editors), Paracoccidioidomycosis. CRC Press, Boca Raton.
    • (1994) Paracoccidioidomycosis
    • San-Blas, G.1    San-Bias, F.2
  • 3
  • 4
    • 0030458257 scopus 로고    scopus 로고
    • Monoclonal antibodies against the 43,000 Da glycoprotein from Paracoccidioides brasiliensis modulate laminin-mediated fungal adhesion to epithelial cells and pathogenesis
    • Gesztesi JL, Puccia R, Travassos LR, Vicentini AP, Franco MF & Lopes JD (1996). Monoclonal antibodies against the 43,000 Da glycoprotein from Paracoccidioides brasiliensis modulate laminin-mediated fungal adhesion to epithelial cells and pathogenesis. Hybridoma, 15: 415-422.
    • (1996) Hybridoma , vol.15 , pp. 415-422
    • Gesztesi, J.L.1    Puccia, R.2    Travassos, L.R.3    Vicentini, A.P.4    Franco, M.F.5    Lopes, J.D.6
  • 5
    • 0031950901 scopus 로고    scopus 로고
    • Mapping of the T-cell epitope in the major 43-kilodalton glycoprotein of Paracoccidioides brasiliensis which induces a Th-1 response protective against fungal infection in BALB/c mice
    • Taborda CP, Juliano MA, Puccia R, Franco M & Travassos LR (1998). Mapping of the T-cell epitope in the major 43-kilodalton glycoprotein of Paracoccidioides brasiliensis which induces a Th-1 response protective against fungal infection in BALB/c mice. Infection and Immunity, 66: 786-793.
    • (1998) Infection and Immunity , vol.66 , pp. 786-793
    • Taborda, C.P.1    Juliano, M.A.2    Puccia, R.3    Franco, M.4    Travassos, L.R.5
  • 7
    • 33746431354 scopus 로고    scopus 로고
    • Exocellular proteolytic activity of Paracoccidioides brasiliensis: Cleavage of components associated with the basement membrane
    • Puccia R, Carmona AK, Gesztesi JL, Juliano L & Travassos LR (1998). Exocellular proteolytic activity of Paracoccidioides brasiliensis: cleavage of components associated with the basement membrane. Medical Mycology, 36: 345-348.
    • (1998) Medical Mycology , vol.36 , pp. 345-348
    • Puccia, R.1    Carmona, A.K.2    Gesztesi, J.L.3    Juliano, L.4    Travassos, L.R.5
  • 8
    • 0025967144 scopus 로고
    • Intramolecularly quenched fluorogenic tetrapeptide substrates for tissue and plasma kallikreins
    • Chagas JR, Juliano L & Prado ES (1991). Intramolecularly quenched fluorogenic tetrapeptide substrates for tissue and plasma kallikreins. Analytical Biochemistry, 192: 419-425.
    • (1991) Analytical Biochemistry , vol.192 , pp. 419-425
    • Chagas, J.R.1    Juliano, L.2    Prado, E.S.3
  • 10
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli UK (1970). Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature, 227: 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 11
    • 0028857512 scopus 로고
    • A new method for detection of proteolytic activity in Pseudomonas lundensis after sodium dodecyl sulfate-polyacrylamide gel electrophoresis
    • Lundy FT, Magee AC, Blair IS & McDwell DA (1995). A new method for detection of proteolytic activity in Pseudomonas lundensis after sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Electrophoresis, 16: 43-45.
    • (1995) Electrophoresis , vol.16 , pp. 43-45
    • Lundy, F.T.1    Magee, A.C.2    Blair, I.S.3    McDwell, D.A.4
  • 13
    • 0030043105 scopus 로고    scopus 로고
    • Cloning and characterization of the gene encoding the major diagnostic antigen of Paracoccidioides brasiliensis: Expression of epitopes of the 43,000 da glycoprotein recognized by antibodies from human patients
    • Cisalpino PS, Puccia R, Yamauchi LM, Cano MIN, Silveira JF & Travassos LR (1996). Cloning and characterization of the gene encoding the major diagnostic antigen of Paracoccidioides brasiliensis: expression of epitopes of the 43,000 Da glycoprotein recognized by antibodies from human patients. Journal of Biological Chemistry, 271:4553-4560.
    • (1996) Journal of Biological Chemistry , vol.271 , pp. 4553-4560
    • Cisalpino, P.S.1    Puccia, R.2    Yamauchi, L.M.3    Cano, M.I.N.4    Silveira, J.F.5    Travassos, L.R.6
  • 14
    • 0025933474 scopus 로고
    • The 43-kda glycoprotein from Paracoccidioides brasiliensis and its deglycosylated form: Excretion and susceptibility to proteolysis
    • Puccia R & Travassos LR (1991). The 43-kDa glycoprotein from Paracoccidioides brasiliensis and its deglycosylated form: excretion and susceptibility to proteolysis. Archives of Biochemistry and Biophysics, 289: 298-302.
    • (1991) Archives of Biochemistry and Biophysics , vol.289 , pp. 298-302
    • Puccia, R.1    Travassos, L.R.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.