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Volumn 16, Issue 2, 1999, Pages 347-354

Production of chemokines CTAPIII and NAP/2 by digestion of recombinant ubiquitin-CTAPIII with yeast ubiquitin C-terminal hydrolase and human immunodeficiency virus protease

Author keywords

[No Author keywords available]

Indexed keywords

AFFINITY CHROMATOGRAPHY; CARBOXY TERMINAL HYDROLASE; CONNECTIVE TISSUE ACTIVATING PEPTIDE; ENZYME ACTIVITY; HYDROLYSIS; NEUTROPHIL ACTIVATING PEPTIDE 2; PROTEIN DIGESTION; PROTEINASE;

EID: 0033166214     PISSN: 10465928     EISSN: None     Source Type: Journal    
DOI: 10.1006/prep.1999.1081     Document Type: Article
Times cited : (6)

References (29)
  • 1
    • 0031259833 scopus 로고    scopus 로고
    • Affinity fusion strategies for detection, purification, and immobilization of recombinant proteins
    • Nilsson J., Stahl S., Lundeberg J., Uhlen, Nygren P-A. Affinity fusion strategies for detection, purification, and immobilization of recombinant proteins. Protein Express. Purif. 11:1997;1-16.
    • (1997) Protein Express. Purif. , vol.11 , pp. 1-16
    • Nilsson, J.1    Stahl, S.2    Lundeberg, J.3    Uhlen4    Nygren, P.-A.5
  • 2
    • 0030272645 scopus 로고    scopus 로고
    • Protein expression using ubiquitin fusion and cleavage
    • Baker R. T. Protein expression using ubiquitin fusion and cleavage. Curr. Opin. Biotechnol. 7:1996;541-546.
    • (1996) Curr. Opin. Biotechnol. , vol.7 , pp. 541-546
    • Baker, R.T.1
  • 3
    • 0026457302 scopus 로고
    • Ubiquitin-specific proteases of Saccharomyces cereviseae
    • Baker R. T., Tobias J. W., Varshavsky A. Ubiquitin-specific proteases of Saccharomyces cereviseae. J. Biol. Chem. 267:1992;23364-23375.
    • (1992) J. Biol. Chem. , vol.267 , pp. 23364-23375
    • Baker, R.T.1    Tobias, J.W.2    Varshavsky, A.3
  • 4
    • 0028859849 scopus 로고
    • A human de-ubiquitinating enzyme with both isopeptidase and peptidase activities in vitro
    • Falquet L., Paquet N., Fruitger S., Hughes G. J., Hoang-Van K., Jaton J.-C. A human de-ubiquitinating enzyme with both isopeptidase and peptidase activities in vitro. FEBS Lett. 359:1995;73-77.
    • (1995) FEBS Lett. , vol.359 , pp. 73-77
    • Falquet, L.1    Paquet, N.2    Fruitger, S.3    Hughes, G.J.4    Hoang-Van, K.5    Jaton, J.-C.6
  • 6
    • 0009851133 scopus 로고    scopus 로고
    • Molecular cloning of a novel ubiquitin-specific protease, UBP41, with isopeptidase activity in chick skeletal muscle
    • Baek S. H., Choi K. S., Yoo Y. J., Cho J. M., Baker R. T., Tanaka K., Chung C. H. Molecular cloning of a novel ubiquitin-specific protease, UBP41, with isopeptidase activity in chick skeletal muscle. J. Biol. Chem. 272:1997;25560-25565.
    • (1997) J. Biol. Chem. , vol.272 , pp. 25560-25565
    • Baek, S.H.1    Choi, K.S.2    Yoo, Y.J.3    Cho, J.M.4    Baker, R.T.5    Tanaka, K.6    Chung, C.H.7
  • 7
    • 0031463942 scopus 로고    scopus 로고
    • A ubiquitin specific protease that efficiently cleaves the ubiquitin-proline bond
    • Gilchrist C. A., Gray D. A., Baker R. T. A ubiquitin specific protease that efficiently cleaves the ubiquitin-proline bond. J. Biol. Chem. 272:1997;32280-32285.
    • (1997) J. Biol. Chem. , vol.272 , pp. 32280-32285
    • Gilchrist, C.A.1    Gray, D.A.2    Baker, R.T.3
  • 8
    • 0028018268 scopus 로고
    • The ubiquitin-proteasome proteolytic pathway
    • Ciechanover A. The ubiquitin-proteasome proteolytic pathway. Cell. 79:1994;13-21.
    • (1994) Cell , vol.79 , pp. 13-21
    • Ciechanover, A.1
  • 9
    • 0028935165 scopus 로고
    • Ubiquitin, proteasomes, and the regulation of intracellular protein degradation
    • Hochstrasser M. Ubiquitin, proteasomes, and the regulation of intracellular protein degradation. Curr. Opin. Cell Biol. 7:1995;215-223.
    • (1995) Curr. Opin. Cell Biol. , vol.7 , pp. 215-223
    • Hochstrasser, M.1
  • 10
    • 0023336183 scopus 로고
    • The yeast ubiquitin genes: A family of natural gene fusions
    • Ozkaynak E., Finley D., Solomon M. J., Varshavsky A. The yeast ubiquitin genes: a family of natural gene fusions. EMBO J. 6:1987;1429-1439.
    • (1987) EMBO J. , vol.6 , pp. 1429-1439
    • Ozkaynak, E.1    Finley, D.2    Solomon, M.J.3    Varshavsky, A.4
  • 11
    • 0344347445 scopus 로고
    • The tails of ubiquitin precursors are ribosomal proteins whose fusion to ubiquitin facilitates ribosome biogenesis
    • Finley D., Bartel B., Varshavsky A. The tails of ubiquitin precursors are ribosomal proteins whose fusion to ubiquitin facilitates ribosome biogenesis. Science. 234:1986;179-186.
    • (1986) Science , vol.234 , pp. 179-186
    • Finley, D.1    Bartel, B.2    Varshavsky, A.3
  • 12
    • 0024560651 scopus 로고
    • Identification of the long ubiquitin extension as ribosomal protein S27a
    • Redman K. L., Rechsteiner M. Identification of the long ubiquitin extension as ribosomal protein S27a. Nature. 338:1989;438-440.
    • (1989) Nature , vol.338 , pp. 438-440
    • Redman, K.L.1    Rechsteiner, M.2
  • 13
    • 0344415987 scopus 로고
    • In vivo half-life of a protein is a function of its amino-terminal residue
    • Bachmair A., Finley D., Varshavsky A. In vivo half-life of a protein is a function of its amino-terminal residue. Nature. 338:1986;394-401.
    • (1986) Nature , vol.338 , pp. 394-401
    • Bachmair, A.1    Finley, D.2    Varshavsky, A.3
  • 14
    • 0024308204 scopus 로고
    • Cloning and expression of a yeast ubiquitin-protein cleaving activity in Escherichia coli
    • Miller H. I., Henzel W. J., Ridgway J. B., Kuang W. J., Chisholm V., Liu C-C. Cloning and expression of a yeast ubiquitin-protein cleaving activity in Escherichia coli. Biotechnology. 7:1989;698-704.
    • (1989) Biotechnology , vol.7 , pp. 698-704
    • Miller, H.I.1    Henzel, W.J.2    Ridgway, J.B.3    Kuang, W.J.4    Chisholm, V.5    Liu, C.-C.6
  • 16
    • 0029052114 scopus 로고
    • Specificity of HIV-1 proteases: An analysis of non-viral protein substrates
    • Tomasselli A. G., Heinrikson R. L. Specificity of HIV-1 proteases: An analysis of non-viral protein substrates. Methods Enzymol. Retroviral Proteases. 241:1994;279-301.
    • (1994) Methods Enzymol. Retroviral Proteases , vol.241 , pp. 279-301
    • Tomasselli, A.G.1    Heinrikson, R.L.2
  • 19
    • 0029071643 scopus 로고
    • Chemokines and tissue injury
    • Furie M. B., Randolph G. J. Chemokines and tissue injury. Am. J. Pathol. 146:1995;1287-1301.
    • (1995) Am. J. Pathol. , vol.146 , pp. 1287-1301
    • Furie, M.B.1    Randolph, G.J.2
  • 21
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli U. K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 227:1970;680-684.
    • (1970) Nature , vol.227 , pp. 680-684
    • Laemmli, U.K.1
  • 22
    • 0018409403 scopus 로고
    • Motility and adhesiveness in human neutrophils: Effects of chemotatic factors
    • Smith C. W., Hollars J. C., Patrick R. A., Hassett C. Motility and adhesiveness in human neutrophils: Effects of chemotatic factors. J. Clin. Invest. 63:1979;221-229.
    • (1979) J. Clin. Invest. , vol.63 , pp. 221-229
    • Smith, C.W.1    Hollars, J.C.2    Patrick, R.A.3    Hassett, C.4
  • 26
    • 0025991456 scopus 로고
    • Cloning and functional analysis of a ubiquitin-specific protease gene UBP1 of Saccharomyces cerevisiae
    • Tobias J. W., Varshavsky A. Cloning and functional analysis of a ubiquitin-specific protease gene UBP1 of Saccharomyces cerevisiae. J. Biol. Chem. 266:1991;12021-12028.
    • (1991) J. Biol. Chem. , vol.266 , pp. 12021-12028
    • Tobias, J.W.1    Varshavsky, A.2
  • 28
    • 0028965079 scopus 로고
    • The crystal structure of recombinant human neutrophil-activating peptide-2 (M6L) at 1.9-A resolution
    • Malkowski M. G., Wu J. Y., Lazar J. B., Johnson P. H., Edwards B. F. P. The crystal structure of recombinant human neutrophil-activating peptide-2 (M6L) at 1.9-A resolution. J. Biol. Chem. 270:1995;7077-7087.
    • (1995) J. Biol. Chem. , vol.270 , pp. 7077-7087
    • Malkowski, M.G.1    Wu, J.Y.2    Lazar, J.B.3    Johnson, P.H.4    Edwards, B.F.P.5
  • 29
    • 0028952217 scopus 로고
    • Limited and defined truncation at the C terminus enhances receptor binding and degranulation activity of the neutrophil-activating peptide 2 (NAP-2)
    • Ehlert J. E., Petersen F., Kubbutat M. H. G., Gerdes J., Flad H-D., Brandt E. Limited and defined truncation at the C terminus enhances receptor binding and degranulation activity of the neutrophil-activating peptide 2 (NAP-2). J. Biol. Chem. 270:1995;6338-6344.
    • (1995) J. Biol. Chem. , vol.270 , pp. 6338-6344
    • Ehlert, J.E.1    Petersen, F.2    Kubbutat, M.H.G.3    Gerdes, J.4    Flad, H.-D.5    Brandt, E.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.