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Volumn 43, Issue 2, 2011, Pages 110-117

Expression, purification, and functional characterization of recombinant PTD-SARA

Author keywords

Cloning; Protein expression and purification; PTD SARA fusion protein

Indexed keywords

CADHERIN; HYBRID PROTEIN; PTD SARA FUSION PROTEIN, HUMAN; PTD-SARA FUSION PROTEIN, HUMAN; RECOMBINANT PROTEIN; SERINE PROTEINASE; SIGNAL PEPTIDE; SMAD PROTEIN; TRANSFORMING GROWTH FACTOR BETA1; ZFYVE16 PROTEIN, HUMAN;

EID: 79551534534     PISSN: 16729145     EISSN: 17457270     Source Type: Journal    
DOI: 10.1093/abbs/gmq122     Document Type: Article
Times cited : (6)

References (24)
  • 2
    • 33644638349 scopus 로고    scopus 로고
    • Renal fibrosis: New insights into the pathogenesis and therapeutics
    • Liu Y. Renal fibrosis: new insights into the pathogenesis and therapeutics. Kidney Int 2006, 69: 213-217.
    • (2006) Kidney Int , vol.69 , pp. 213-217
    • Liu, Y.1
  • 3
    • 24644487312 scopus 로고    scopus 로고
    • TGF-beta and epithelial-to-mesenchymal transitions
    • Zavadil J and Böttinger EP. TGF-beta and epithelial-to-mesenchymal transitions. Oncogene 2005, 24: 5764-5774.
    • (2005) Oncogene , vol.24 , pp. 5764-5774
    • Zavadil, J.1    Böttinger, E.P.2
  • 4
    • 0032428684 scopus 로고    scopus 로고
    • SARA, a FYVE domain protein that recruits Smad2 to the TGFb receptor
    • Tsukazaki T, Chiang TA, Davison AF, Attisano L and Wrana JL. SARA, a FYVE domain protein that recruits Smad2 to the TGFb receptor. Cell 1998, 95: 779-791.
    • (1998) Cell , vol.95 , pp. 779-791
    • Tsukazaki, T.1    Chiang, T.A.2    Davison, A.F.3    Attisano, L.4    Wrana, J.L.5
  • 5
    • 0036682952 scopus 로고    scopus 로고
    • Smad3 allostery links TGF-beta receptor kinase activation to transcriptional control
    • Qin BY, Lam SS, Correia JJ and Lin K. Smad3 allostery links TGF-beta receptor kinase activation to transcriptional control. Genes Dev 2002, 16: 1950-1963.
    • (2002) Genes Dev , vol.16 , pp. 1950-1963
    • Qin, B.Y.1    Lam, S.S.2    Correia, J.J.3    Lin, K.4
  • 6
    • 14844307044 scopus 로고    scopus 로고
    • The role of internalization in transforming growth factor beta1-induced Smad2 association with Smad anchor for receptor activation (SARA) and Smad2-dependent signaling in human mesangial cells
    • Runyan CE, Schnaper HW and Poncelet AC. The role of internalization in transforming growth factor beta1-induced Smad2 association with Smad anchor for receptor activation (SARA) and Smad2-dependent signaling in human mesangial cells. J Biol Chem 2005, 280: 8300-8308.
    • (2005) J Biol Chem , vol.280 , pp. 8300-8308
    • Runyan, C.E.1    Schnaper, H.W.2    Poncelet, A.C.3
  • 8
    • 33748305561 scopus 로고    scopus 로고
    • Inhibition of transforming growth factor-beta1-induced signaling and epithelial-to-mesenchymal transition by the Smad-binding peptide aptamer Trx-SARA
    • Zhao BM and Hoffmann FM. Inhibition of transforming growth factor-beta1-induced signaling and epithelial-to-mesenchymal transition by the Smad-binding peptide aptamer Trx-SARA. Mol Biol Cell 2006, 17: 3819-3831.
    • (2006) Mol Biol Cell , vol.17 , pp. 3819-3831
    • Zhao, B.M.1    Hoffmann, F.M.2
  • 9
    • 5644276383 scopus 로고    scopus 로고
    • Delivery of bioactive molecules into the cell: The Trojan horse approach
    • Dietz GP and Bähr M. Delivery of bioactive molecules into the cell: the Trojan horse approach. Mol Cell Neurosci 2004, 27: 85-131.
    • (2004) Mol Cell Neurosci , vol.27 , pp. 85-131
    • Dietz, G.P.1    Bähr, M.2
  • 10
    • 79551574468 scopus 로고    scopus 로고
    • Cloning, expression and purification of Microcystis viridis lectin in Escherichia coli
    • Epub ahead of print
    • Li Y, Liao X, Chen G, Yap Y and Zhang X. Cloning, expression and purification of Microcystis viridis lectin in Escherichia coli. Mol Biotechnol, 2010 [Epub ahead of print].
    • (2010) Mol Biotechnol
    • Li, Y.1    Liao, X.2    Chen, G.3    Yap, Y.4    Zhang, X.5
  • 11
    • 4143057927 scopus 로고    scopus 로고
    • Transforming growth factor-b1 stimulates collagen matrix remodeling through increased adhesive and contractive potential by human renal fibroblasts
    • Kondo S, Kagami S, Urushihara M, Kitamura A, Shimizu M, Strutz F and Müller GA, et al. Transforming growth factor-b1 stimulates collagen matrix remodeling through increased adhesive and contractive potential by human renal fibroblasts. Biochim Biophys Acta 2004, 1693: 91-100.
    • (2004) Biochim Biophys Acta , vol.1693 , pp. 91-100
    • Kondo, S.1    Kagami, S.2    Urushihara, M.3    Kitamura, A.4    Shimizu, M.5    Strutz, F.6    Müller, G.A.7
  • 12
    • 72949102843 scopus 로고    scopus 로고
    • URG11 mediates hypoxia-induced epithelial-to-mesenchymal transition by modulation of E-cadherin and beta-catenin
    • Du R, Huang C, Bi Q, Zhai Y, Xia L, Liu J and Sun S, et al. URG11 mediates hypoxia-induced epithelial-to-mesenchymal transition by modulation of E-cadherin and beta-catenin. Biochem Biophys Res Commun 2010, 391: 135-141.
    • (2010) Biochem Biophys Res Commun , vol.391 , pp. 135-141
    • Du, R.1    Huang, C.2    Bi, Q.3    Zhai, Y.4    Xia, L.5    Liu, J.6    Sun, S.7
  • 13
    • 0030904245 scopus 로고    scopus 로고
    • A truncated HIV-1 Tat protein basic domain rapidly translocates through the plasma membrane and accumulates in the cell nucleus
    • Vivès E, Brodin P and Lebleu B. A truncated HIV-1 Tat protein basic domain rapidly translocates through the plasma membrane and accumulates in the cell nucleus. J Biol Chem 1997, 272: 16010-16017.
    • (1997) J Biol Chem , vol.272 , pp. 16010-16017
    • Vivès, E.1    Brodin, P.2    Lebleu, B.3
  • 14
    • 33748433244 scopus 로고    scopus 로고
    • Cell-penetrating peptides as vectors for peptide, protein and oligonucleotide delivery
    • Mäe M and Langel U. Cell-penetrating peptides as vectors for peptide, protein and oligonucleotide delivery. Curr Opin Pharmacol 2006, 6: 509-514.
    • (2006) Curr Opin Pharmacol , vol.6 , pp. 509-514
    • Mäe, M.1    Langel, U.2
  • 15
    • 0031471203 scopus 로고    scopus 로고
    • Intercellular trafficking and protein delivery by a herpesvirus structural protein
    • Elliott G and O'Hare P. Intercellular trafficking and protein delivery by a herpesvirus structural protein. Cell 1997, 88: 223-233.
    • (1997) Cell , vol.88 , pp. 223-233
    • Elliott, G.1    O'Hare, P.2
  • 16
    • 0034910022 scopus 로고    scopus 로고
    • Is VP22 nuclear homing an artifact?
    • Lundberg M and Johansson M. Is VP22 nuclear homing an artifact? Nat Biotechnol 2001, 19: 713-714.
    • (2001) Nat Biotechnol , vol.19 , pp. 713-714
    • Lundberg, M.1    Johansson, M.2
  • 17
    • 0028239908 scopus 로고
    • The third helix of the Antennapedia homeodomain translocates through biological membranes
    • Derossi D, Joliot AH, Chassaing G and Prochiantz A. The third helix of the Antennapedia homeodomain translocates through biological membranes. J Biol Chem 1994, 269: 10444-10450.
    • (1994) J Biol Chem , vol.269 , pp. 10444-10450
    • Derossi, D.1    Joliot, A.H.2    Chassaing, G.3    Prochiantz, A.4
  • 18
    • 0041816277 scopus 로고    scopus 로고
    • Antennapedia and HIV transactivator of transcription (TAT) 'protein transduction domains' promote endocytosis of high molecular weight cargo upon binding to cell surface glycosaminoglycans
    • Console S, Marty C, García-Echeverría C, Schwendener R and Ballmer-Hofer K. Antennapedia and HIV transactivator of transcription (TAT) 'protein transduction domains' promote endocytosis of high molecular weight cargo upon binding to cell surface glycosaminoglycans. J Biol Chem 2003, 278: 35109-35114.
    • (2003) J Biol Chem , vol.278 , pp. 35109-35114
    • Console, S.1    Marty, C.2    García-Echeverría, C.3    Schwendener, R.4    Ballmer-Hofer, K.5
  • 19
    • 0029982569 scopus 로고    scopus 로고
    • Cell internalization of the third helix of the Antennapedia homeodomain is receptor-independent
    • Derossi D, Calvet S, Trembleau A, Brunissen A, Chassaing G and Prochiantz A. Cell internalization of the third helix of the Antennapedia homeodomain is receptor-independent. J Biol Chem 1996, 271: 18188-18193.
    • (1996) J Biol Chem , vol.271 , pp. 18188-18193
    • Derossi, D.1    Calvet, S.2    Trembleau, A.3    Brunissen, A.4    Chassaing, G.5    Prochiantz, A.6
  • 21
    • 0031950560 scopus 로고    scopus 로고
    • Refolding of recombinant proteins
    • Clark EDB. Refolding of recombinant proteins. Curr Opin Biotechnol 1998, 9: 157-163.
    • (1998) Curr Opin Biotechnol , vol.9 , pp. 157-163
    • Clark, E.D.B.1
  • 22
    • 5044222901 scopus 로고    scopus 로고
    • Protein sequencing by mass analysis of polypeptide ladders after controlled protein hydrolysis
    • Zhong H, Zhang Y, Wen Z and Li L. Protein sequencing by mass analysis of polypeptide ladders after controlled protein hydrolysis. Nat Biotechnol 2004, 22: 1242-1243.
    • (2004) Nat Biotechnol , vol.22 , pp. 1242-1243
    • Zhong, H.1    Zhang, Y.2    Wen, Z.3    Li, L.4
  • 23
    • 0038333588 scopus 로고    scopus 로고
    • Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides
    • Gevaert K, Goethals M, Martens L, Van Damme J, Staes A and Thomas GR, et al. Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides. Nat Biotechnol 2003, 21: 566-569.
    • (2003) Nat Biotechnol , vol.21 , pp. 566-569
    • Gevaert, K.1    Goethals, M.2    Martens, L.3    Van Damme, J.4    Staes, A.5    Thomas, G.R.6
  • 24
    • 4444335470 scopus 로고    scopus 로고
    • The ABC's (and XYZ's) of peptide sequencing
    • Steen H and Mann M. The ABC's (and XYZ's) of peptide sequencing. Nat Rev Mol Cell Biol 2004, 5: 699-711.
    • (2004) Nat Rev Mol Cell Biol , vol.5 , pp. 699-711
    • Steen, H.1    Mann, M.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.