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Volumn 7, Issue 5, 2002, Pages 433-440

Phage display of functional human TNF-α converting enzyme catalytic domain: A rapid method for the production of stabilized proteolytic proteins for assay development and high-throughput screening

Author keywords

[No Author keywords available]

Indexed keywords

ADAM PROTEIN; ENZYME INHIBITOR; GLUTATHIONE TRANSFERASE; METALLOPROTEINASE; PEPTIDE LIBRARY; PROTEIN; RECOMBINANT PROTEIN; TUMOR NECROSIS FACTOR ALPHA CONVERTING ENZYME; TUMOR NECROSIS FACTOR-ALPHA CONVERTASE;

EID: 0642370953     PISSN: 10870571     EISSN: None     Source Type: Journal    
DOI: 10.1177/108705702237675     Document Type: Article
Times cited : (4)

References (25)
  • 2
    • 8044250278 scopus 로고    scopus 로고
    • Cloning of a disintegrin metalloproteinase that processes precursor tumor-necrosis factor-a
    • Moss ML, Jin SL, Milla ME, Burkhart W, Carter HL, Chen WJ, et al: Cloning of a disintegrin metalloproteinase that processes precursor tumor-necrosis factor-a. Nature I997;385:733-736.
    • Nature I997 , vol.385 , pp. 733-736
    • Moss, M.L.1    Jin, S.L.2    Milla, M.E.3    Burkhart, W.4    Carter, H.L.5    Chen, W.J.6
  • 3
    • 0030834283 scopus 로고    scopus 로고
    • Metalloprotease-disintegrins: Links to cell adhesion and cleavage of TNFα and notch
    • Blobel CP: Metalloprotease-disintegrins: links to cell adhesion and cleavage of TNFα and notch. Cell 1997;90:589-592.
    • (1997) Cell , vol.90 , pp. 589-592
    • Blobel, C.P.1
  • 4
    • 0029045064 scopus 로고
    • ADAM, a widely distributed and developmentally regulated gene family encoding membrane proteins with a disintegrin and metalloprotease domain
    • Wolfsberg TG, Straight PD, Gerena R, Huovila AP, Primakoff P, Myles DG, et al: ADAM, a widely distributed and developmentally regulated gene family encoding membrane proteins with a disintegrin and metalloprotease domain. Dev Biol 1995;169:378-383.
    • (1995) Dev Biol , vol.169 , pp. 378-383
    • Wolfsberg, T.G.1    Straight, P.D.2    Gerena, R.3    Huovila, A.P.4    Primakoff, P.5    Myles, D.G.6
  • 5
    • 14444272986 scopus 로고    scopus 로고
    • Evidence that tumor necrosis factor α converting enzyme is involved in regulated a-secretase cleavage of the Alzheimer amyloid protein precursor
    • Buxbaum JD, Liu KN, Luo Y, Slack JL, Stocking KL, Peschon JJ, et al: Evidence that tumor necrosis factor α converting enzyme is involved in regulated a-secretase cleavage of the Alzheimer amyloid protein precursor. J Biol Chem 1998;273:27765-27767.
    • (1998) J Biol Chem , vol.273 , pp. 27765-27767
    • Buxbaum, J.D.1    Liu, K.N.2    Luo, Y.3    Slack, J.L.4    Stocking, K.L.5    Peschon, J.J.6
  • 7
    • 0032080801 scopus 로고    scopus 로고
    • TNF-α convertase enzyme from human arthritis-affected cartilage: Isolation of cDNA differential display, expression of the active enzyme, and regulation of TNF-α
    • Patel IR, Attur MG, Patel RN, Stuchin SA, Abagyan RA, Abramson SB, et al: TNF-α convertase enzyme from human arthritis-affected cartilage: isolation of cDNA differential display, expression of the active enzyme, and regulation of TNF-α. J Immunol 1998;160:4570-4579.
    • (1998) J Immunol , vol.160 , pp. 4570-4579
    • Patel, I.R.1    Attur, M.G.2    Patel, R.N.3    Stuchin, S.A.4    Abagyan, R.A.5    Abramson, S.B.6
  • 8
    • 0021818675 scopus 로고
    • Filamentous fusion phage: Novel expression vectors that display cloned antigen on the viron surface
    • Smith GP: Filamentous fusion phage: novel expression vectors that display cloned antigen on the viron surface. Science 1985;228:1315-1317.
    • (1985) Science , vol.228 , pp. 1315-1317
    • Smith, G.P.1
  • 9
    • 0026345777 scopus 로고
    • Phage-enzymes: Expression and affinity chromatography of functional alkaline phosphatase on the surface of bacteriophage
    • McCafferty J, Jackson RH, Chiswell DJ: Phage-enzymes: expression and affinity chromatography of functional alkaline phosphatase on the surface of bacteriophage. Protein Eng 1991 ;4:955-961.
    • (1991) Protein Eng , vol.4 , pp. 955-961
    • McCafferty, J.1    Jackson, R.H.2    Chiswell, D.J.3
  • 13
    • 0029148963 scopus 로고
    • Functional display and expression of chicken cyctatin using a phagemid system
    • Tanaka AS, Sampaio CAM, Fritz H, Auerswald EA: Functional display and expression of chicken cyctatin using a phagemid system. Biochem Biophys Res Commun 1995;214:389-395.
    • (1995) Biochem Biophys Res Commun , vol.214 , pp. 389-395
    • Tanaka, A.S.1    Cam, S.2    Fritz, H.3    Auerswald, E.A.4
  • 14
    • 0030071615 scopus 로고    scopus 로고
    • A stablephage-display system using a phagemid vector-phage display of hen egg-white lysozyme (HEL), Escherichia coli alkaline phosphatase, and anti-HEL monoclonal antibody, HYHEL 10
    • Maenaka K, Kuruta M, Tsumoto K, Watanabe K, Ueda Y, Kumagai I: A stablephage-display system using a phagemid vector-phage display of hen egg-white lysozyme (HEL), Escherichia coli alkaline phosphatase, and anti-HEL monoclonal antibody, HYHEL 10. Biochem Biophys Res Commun 1996;218:682-687.
    • (1996) Biochem Biophys Res Commun , vol.218 , pp. 682-687
    • Maenaka, K.1    Kuruta, M.2    Tsumoto, K.3    Watanabe, K.4    Ueda, Y.5    Kumagai, I.6
  • 15
    • 0030896039 scopus 로고    scopus 로고
    • Enzymatic properties of phage-displayed fragments of human plasminogen
    • Lasters I, Van HN, Lijnen HR, Collen D, Jespers L: Enzymatic properties of phage-displayed fragments of human plasminogen. Eur J Biochem 1997:244:946-952.
    • (1997) Eur J Biochem , vol.244 , pp. 946-952
    • Lasters, I.1    Van, H.N.2    Lijnen, H.R.3    Collen, D.4    Jespers, L.5
  • 16
    • 0031578799 scopus 로고    scopus 로고
    • Display of functional thrombin inhibitor hirudin on the surface of phage M13
    • Wirsching F, Opitz T, Dietrich R, Schwienhorst A: Display of functional thrombin inhibitor hirudin on the surface of phage M13. Gene 1997;204:177-84.
    • (1997) Gene , vol.204 , pp. 177-184
    • Wirsching, F.1    Opitz, T.2    Dietrich, R.3    Schwienhorst, A.4
  • 17
    • 0032522097 scopus 로고    scopus 로고
    • Serection in Escherichia coli und phage-display of recombinant insulinlike growth factor binding protein-2
    • Lucie MR, Forbes BE, Grosvenor SE, Carr JM, Wallace JC, Forsberg G: Serection in Escherichia coli und phage-display of recombinant insulinlike growth factor binding protein-2. J Biotechnol 1998;61:95-108.
    • (1998) J Biotechnol , vol.61 , pp. 95-108
    • Lucie, M.R.1    Forbes, B.E.2    Grosvenor, S.E.3    Carr, J.M.4    Wallace, J.C.5    Forsberg, G.6
  • 18
    • 0032929537 scopus 로고    scopus 로고
    • Selective enrichment and high-throughput screening of phage surface-displayed cDNA libraries from complex allergenic systems
    • Crameri R, Walter G: Selective enrichment and high-throughput screening of phage surface-displayed cDNA libraries from complex allergenic systems. Combinatorial Chemistry & High Throughput Screening 1999;2:63-72.
    • (1999) Combinatorial Chemistry & High Throughput Screening , vol.2 , pp. 63-72
    • Crameri, R.1    Walter, G.2
  • 19
    • 0031550263 scopus 로고    scopus 로고
    • The recombinant catalytic domain of mouse coIlagenase-3 depolymerizes type i collagen by cleaving its aminotelopeptides
    • Lemaitre V, Jungblutli A, Eeckhout Y: The recombinant catalytic domain of mouse coIlagenase-3 depolymerizes type I collagen by cleaving its aminotelopeptides. Biochem Biophys Res Commun 1997;230:202-205.
    • (1997) Biochem Biophys Res Commun , vol.230 , pp. 202-205
    • Lemaitre, V.1    Jungblutli, A.2    Eeckhout, Y.3
  • 20
    • 0030577022 scopus 로고    scopus 로고
    • Activation of a recombinant membrane type 1-matrix metalloproteinase (MT1-MMP) by furin and its interaction with tissue inhibitor of metalloproteinase (TIMP)-2
    • Sato H, Kinoshita T, Takino T, Nakayama K, Sciki M: Activation of a recombinant membrane type 1-matrix metalloproteinase (MT1-MMP) by furin and its interaction with tissue inhibitor of metalloproteinase (TIMP)-2. FEES Lett 1996;393:101-104.
    • (1996) FEES Lett , vol.393 , pp. 101-104
    • Sato, H.1    Kinoshita, T.2    Takino, T.3    Nakayama, K.4    Sciki, M.5
  • 21
    • 0000661488 scopus 로고    scopus 로고
    • Protein degradation and proteolytic modification
    • Neihardt FC (ed): Washington, DC: ASM Press
    • Miller CG: Protein degradation and proteolytic modification. In Neihardt FC (ed): Escherichia coli and Salmonella: Cellular and Molecular Biology. Washington, DC: ASM Press, 1996:938-954.
    • (1996) Escherichia Coli and Salmonella: Cellular and Molecular Biology , pp. 938-954
    • Miller, C.G.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.