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Volumn 3, Issue , 2002, Pages

Aggregation and retention of human urokinase type plasminogen activator in the yeast endoplasmic reticulum

Author keywords

[No Author keywords available]

Indexed keywords

RECOMBINANT PLASMINOGEN ACTIVATOR; UROKINASE;

EID: 0442310898     PISSN: 14712199     EISSN: None     Source Type: Journal    
DOI: 10.1186/1471-2199-3-15     Document Type: Article
Times cited : (27)

References (27)
  • 1
    • 0027137885 scopus 로고
    • Analysis of two mutated vacuolar proteins reveals a degradation pathway in the endoplasmic reticulum or a related compartment of yeast
    • Finger A, Knop M, Wolf DH: Analysis of two mutated vacuolar proteins reveals a degradation pathway in the endoplasmic reticulum or a related compartment of yeast. Eur J Biochem 1993, 218:565-574
    • (1993) Eur. J. Biochem. , vol.218 , pp. 565-574
    • Finger, A.1    Knop, M.2    Wolf, D.H.3
  • 2
    • 0003049256 scopus 로고    scopus 로고
    • Folding and stability of the Z and S(iiyama) genetic variants of human alpha1-antitrypsin
    • Kang HA, Lee KN, Yu MH: Folding and stability of the Z and S(iiyama) genetic variants of human alpha1-antitrypsin. J Biol Chem 1997, 272:510-516
    • (1997) J. Biol. Chem. , vol.272 , pp. 510-516
    • Kang, H.A.1    Lee, K.N.2    Yu, M.H.3
  • 3
    • 0029838640 scopus 로고    scopus 로고
    • ER degradation of a misfolded luminal protein by the cytosolic ubiquitin-proteasome pathway
    • Hiller MM, Finger A, Schweiger M, Wolf DH: ER degradation of a misfolded luminal protein by the cytosolic ubiquitin-proteasome pathway. Science 1996, 273:1725-1728
    • (1996) Science , vol.273 , pp. 1725-1728
    • Hiller, M.M.1    Finger, A.2    Schweiger, M.3    Wolf, D.H.4
  • 4
    • 0030447659 scopus 로고    scopus 로고
    • Proteasome-dependent endoplasmic reticulum-associated protein degradation: An unconventional route to a familiar fate
    • Werner ED, Brodsky JL, McCracken AA: Proteasome-dependent endoplasmic reticulum-associated protein degradation: an unconventional route to a familiar fate. Proc Natl Acad Sci U S A 1996, 93:13797-13801
    • (1996) Proc. Natl. Acad. Sci. U. S. A. , vol.93 , pp. 13797-13801
    • Werner, E.D.1    Brodsky, J.L.2    McCracken, A.A.3
  • 5
    • 0029829005 scopus 로고    scopus 로고
    • A pathway for targeting soluble misfolded proteins to the yeast vacuole
    • Hong E, Davidson AR, Kaiser CA: A pathway for targeting soluble misfolded proteins to the yeast vacuole. J Cell Biol 1996, 135:623-633
    • (1996) J. Cell Biol. , vol.135 , pp. 623-633
    • Hong, E.1    Davidson, A.R.2    Kaiser, C.A.3
  • 6
    • 0032511128 scopus 로고    scopus 로고
    • Different degradation pathways for heterologous glycoproteins in yeast
    • Holkeri H, Makarow M: Different degradation pathways for heterologous glycoproteins in yeast. FEBS Lett 1998, 429:162-166
    • (1998) FEBS Lett. , vol.429 , pp. 162-166
    • Holkeri, H.1    Makarow, M.2
  • 7
    • 0032945481 scopus 로고    scopus 로고
    • Reglucosylation of glycoproteins and quality control of glycoprotein folding in the endoplasmic reticulum of yeast cells
    • Parodi AJ: Reglucosylation of glycoproteins and quality control of glycoprotein folding in the endoplasmic reticulum of yeast cells. Biochim Biophys Acta 1999, 1426:287-295
    • (1999) Biochim. Biophys. Acta , vol.1426 , pp. 287-295
    • Parodi, A.J.1
  • 10
    • 0035970569 scopus 로고    scopus 로고
    • Mutation of the homologue of GDP-mannose pyrophosphorylase alters cell wall structure, protein glycosylation and secretion in Hansenula polymorpha
    • Agaphonov MO, Packeiser AN, Chechenova MB, Choi ES, Ter-Avanesyan MD: Mutation of the homologue of GDP-mannose pyrophosphorylase alters cell wall structure, protein glycosylation and secretion in Hansenula polymorpha. Yeast 2001, 18:391-402
    • (2001) Yeast , vol.18 , pp. 391-402
    • Agaphonov, M.O.1    Packeiser, A.N.2    Chechenova, M.B.3    Choi, E.S.4    Ter-Avanesyan, M.D.5
  • 12
    • 0025772644 scopus 로고
    • Strategies for the improvement of thrombolytic agents
    • Lijnen HR, Collen D: Strategies for the improvement of thrombolytic agents. Thromb Haemost 1991, 66:88-110
    • (1991) Thromb. Haemost. , vol.66 , pp. 88-110
    • Lijnen, H.R.1    Collen, D.2
  • 14
    • 0034527340 scopus 로고    scopus 로고
    • Catalytic and fibrinolytic properties of recombinant urokinase plasminogen activator from E. coli, mammalian, and yeast cell
    • Wang P, Zhang J, Sun Z, Chen Y, Gurewich V, Liu JN: Catalytic and fibrinolytic properties of recombinant urokinase plasminogen activator from E. coli, mammalian, and yeast cell. Thromb Res 2000, 100:461-467
    • (2000) Thromb. Res. , vol.100 , pp. 461-467
    • Wang, P.1    Zhang, J.2    Sun, Z.3    Chen, Y.4    Gurewich, V.5    Liu, J.N.6
  • 15
    • 0029817714 scopus 로고    scopus 로고
    • N-Glycosylation affects endoplasmic reticulum degradation of a mutated derivative of carboxypeptidase yscY in yeast
    • Knop M, Hauser N, Wolf DH: N-Glycosylation affects endoplasmic reticulum degradation of a mutated derivative of carboxypeptidase yscY in yeast. Yeast 1996, 12:1229-1238
    • (1996) Yeast , vol.12 , pp. 1229-1238
    • Knop, M.1    Hauser, N.2    Wolf, D.H.3
  • 17
    • 0029743974 scopus 로고    scopus 로고
    • A novel autonomously replicating sequence (ARS) for multiple integration in the yeast Hansenula polymorpha DL-1
    • Sohn JS, Choi ES, Kim CH, Agaphonov MO, Ter-Avanesyan MD, Rhee JS, Rhee SK: A novel autonomously replicating sequence (ARS) for multiple integration in the yeast Hansenula polymorpha DL-1. J Bacteriol 1996, 178:4420-4428
    • (1996) J. Bacteriol. , vol.178 , pp. 4420-4428
    • Sohn, J.S.1    Choi, E.S.2    Kim, C.H.3    Agaphonov, M.O.4    Ter-Avanesyan, M.D.5    Rhee, J.S.6    Rhee, S.K.7
  • 18
    • 0028785213 scopus 로고
    • A disruption-replacement approach for the targeted integration of foreign genes in Hansenula polymorpha
    • Agaphonov MO, Beburov MY, Ter-Avanesyan MD, Smirnov VN: A disruption-replacement approach for the targeted integration of foreign genes in Hansenula polymorpha. Yeast 1995, 11:1241-1247
    • (1995) Yeast , vol.11 , pp. 1241-1247
    • Agaphonov, M.O.1    Beburov, M.Y.2    Ter-Avanesyan, M.D.3    Smirnov, V.N.4
  • 19
    • 0032952119 scopus 로고    scopus 로고
    • Vectors for rapid selection of integrants with different plasmid copy numbers in the yeast Hansenula polymorpha DL1
    • Agaphonov MO, Trushkina PM, Sohn J-H, Choi E-S, Rhee S-K, Ter-Avanesyan MD: Vectors for rapid selection of integrants with different plasmid copy numbers in the yeast Hansenula polymorpha DL1. Yeast 1999, 15:541-551
    • (1999) Yeast , vol.15 , pp. 541-551
    • Agaphonov, M.O.1    Trushkina, P.M.2    Sohn, J.-H.3    Choi, E.-S.4    Rhee, S.-K.5    Ter-Avanesyan, M.D.6
  • 20
    • 0029061879 scopus 로고
    • STT10, a novel class-D VPS yeast gene required for osmotic integrity related to the PKC1/STT1 protein kinase pathway
    • Yoshida S, Ohya Y, Hirose R, Nakano A, Anraku Y: STT10, a novel class-D VPS yeast gene required for osmotic integrity related to the PKC1/STT1 protein kinase pathway. Gene 1995, 160:117-122
    • (1995) Gene , vol.160 , pp. 117-122
    • Yoshida, S.1    Ohya, Y.2    Hirose, R.3    Nakano, A.4    Anraku, Y.5
  • 21
    • 0000615498 scopus 로고
    • Plasmid vectors carrying the replication origin of filamentous single-stranded phages
    • (Edited by: Setlow JK) New York, Plenum Press
    • Cesareni G, Murray AH: Plasmid vectors carrying the replication origin of filamentous single-stranded phages. In: Genetic Engineering: Principles and Methods (Edited by: Setlow JK) New York, Plenum Press 1987, 135-154
    • (1987) Genetic Engineering: Principles and Methods , pp. 135-154
    • Cesareni, G.1    Murray, A.H.2
  • 22
    • 50449151040 scopus 로고
    • Fibrin plate method for estimating fibrinolytic activity
    • Astrup T, Muellerts S: Fibrin plate method for estimating fibrinolytic activity. Arch Biochem Biophys 1952, 40:346-351
    • (1952) Arch. Biochem. Biophys. , vol.40 , pp. 346-351
    • Astrup, T.1    Muellerts, S.2
  • 25
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford MM: A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 1976, 72:248-254
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 26
    • 0028940737 scopus 로고
    • Plasmid reorganization during integrative transformation in Hansenula polymorpha
    • Bogdanova AI, Agaphonov MO, Ter-Avanesyan MD: Plasmid reorganization during integrative transformation in Hansenula polymorpha. Yeast 1995, 11:343-353
    • (1995) Yeast , vol.11 , pp. 343-353
    • Bogdanova, A.I.1    Agaphonov, M.O.2    Ter-Avanesyan, M.D.3
  • 27
    • 0025675856 scopus 로고
    • High efficiency transformation of Escherichia coli with plasmids
    • Inoue H, Nojima H, Okayama H: High efficiency transformation of Escherichia coli with plasmids. Gene 1990, 96:23-28
    • (1990) Gene , vol.96 , pp. 23-28
    • Inoue, H.1    Nojima, H.2    Okayama, H.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.