메뉴 건너뛰기




Volumn 22, Issue 6, 2013, Pages 840-850

A multipurpose fusion tag derived from an unstructured and hyperacidic region of the amyloid precursor protein

Author keywords

Amyloid precursor protein; Fusion tag; Inclusion body; Protein expression; Refolding

Indexed keywords

AMYLOID PRECURSOR PROTEIN; BACTERIUM LYSATE; FATT PROTEIN; HYBRID PROTEIN; POLYPEPTIDE; PROTEIN; UNCLASSIFIED DRUG;

EID: 84881275573     PISSN: 09618368     EISSN: 1469896X     Source Type: Journal    
DOI: 10.1002/pro.2254     Document Type: Article
Times cited : (24)

References (22)
  • 2
    • 0037255597 scopus 로고    scopus 로고
    • Overview of tag protein fusions: From molecular and biochemical fundamentals to commercial systems
    • Terpe K (2003) Overview of tag protein fusions: from molecular and biochemical fundamentals to commercial systems. Appl Microbiol Biotechnol 60:523-533.
    • (2003) Appl Microbiol Biotechnol , vol.60 , pp. 523-533
    • Terpe, K.1
  • 5
    • 28644437291 scopus 로고    scopus 로고
    • The amyloid- beta precursor protein: Integrating structure with biological function
    • Reinhard C, Hebert SS, De Strooper B (2005) The amyloid- beta precursor protein: integrating structure with biological function. EMBO J 24:3996-4006.
    • (2005) EMBO J , vol.24 , pp. 3996-4006
    • Reinhard, C.1    Hebert, S.S.2    De Strooper, B.3
  • 6
    • 34248172449 scopus 로고    scopus 로고
    • Structure and functions of the human amyloid precursor protein: The whole is more than the sum of its parts
    • Gralle M, Ferreira ST (2007) Structure and functions of the human amyloid precursor protein: the whole is more than the sum of its parts. Prog Neurobiol 82:11-32.
    • (2007) Prog Neurobiol , vol.82 , pp. 11-32
    • Gralle, M.1    Ferreira, S.T.2
  • 7
    • 77954657682 scopus 로고    scopus 로고
    • A rapid screening method for cell lines producing singly-tagged recombinant proteins using the "tARGET tag" system
    • Tabata S, Nampo M, Mihara E, Tamura-Kawakami K, Fujii I, Takagi J (2010) A rapid screening method for cell lines producing singly-tagged recombinant proteins using the "TARGET tag" system. J Proteomics 73:1777-1785.
    • (2010) J Proteomics , vol.73 , pp. 1777-1785
    • Tabata, S.1    Nampo, M.2    Mihara, E.3    Tamura-Kawakami, K.4    Fujii, I.5    Takagi, J.6
  • 8
    • 2342602909 scopus 로고    scopus 로고
    • Recombinant ATPases of the yeast 26S proteasome activate protein degradation by the 20S proteasome
    • Takeuchi J, Tamura T (2004) Recombinant ATPases of the yeast 26S proteasome activate protein degradation by the 20S proteasome. FEBS Lett 565:39-42.
    • (2004) FEBS Lett , vol.565 , pp. 39-42
    • Takeuchi, J.1    Tamura, T.2
  • 10
    • 79951959644 scopus 로고    scopus 로고
    • The substrate specificity of Metarhizium anisopliae and Bos taurus carboxypeptidases A: Insights into their use as tools for the removal of affinity tags
    • Austin BP, Tozser J, Bagossi P, Tropea JE, Waugh DS (2011) The substrate specificity of Metarhizium anisopliae and Bos taurus carboxypeptidases A: insights into their use as tools for the removal of affinity tags. Protein Expr Purif 77:53-61.
    • (2011) Protein Expr Purif , vol.77 , pp. 53-61
    • Austin, B.P.1    Tozser, J.2    Bagossi, P.3    Tropea, J.E.4    Waugh, D.S.5
  • 11
    • 84855487625 scopus 로고    scopus 로고
    • Isolation of Metarhizium anisopliae carboxypeptidase A with native disulfide bonds from the cytosol of Escherichia coli BL21(DE3)
    • Austin BP, Waugh DS (2012) Isolation of Metarhizium anisopliae carboxypeptidase A with native disulfide bonds from the cytosol of Escherichia coli BL21(DE3). Protein Expr Purif 82:116-124.
    • (2012) Protein Expr Purif , vol.82 , pp. 116-124
    • Austin, B.P.1    Waugh, D.S.2
  • 12
    • 0033515653 scopus 로고    scopus 로고
    • Cloning, expression, and substrate specificity of MeCPA, a zinc carboxypeptidase that is secreted into infected tissues by the fungal entomopathogen Metarhizium anisopliae
    • Joshi L, St Leger RJ (1999) Cloning, expression, and substrate specificity of MeCPA, a zinc carboxypeptidase that is secreted into infected tissues by the fungal entomopathogen Metarhizium anisopliae. J Biol Chem 274:9803-9811.
    • (1999) J Biol Chem , vol.274 , pp. 9803-9811
    • Joshi, L.1    St Leger, R.J.2
  • 14
    • 0343953095 scopus 로고    scopus 로고
    • Effects of ionic surfactants used in reversed micelles on cutinase activity and stability
    • Goncalves AM, Serro AP, Aires-Barros MR, Cabral JM (2000) Effects of ionic surfactants used in reversed micelles on cutinase activity and stability. Biochim Biophys Acta 1480:92-106.
    • (2000) Biochim Biophys Acta , vol.1480 , pp. 92-106
    • Goncalves, A.M.1    Serro, A.P.2    Aires-Barros, M.R.3    Cabral, J.M.4
  • 16
    • 84860273145 scopus 로고    scopus 로고
    • Crystal structure of alpha5beta1 integrin ectodomain: Atomic details of the fibronectin receptor
    • Nagae M, Re S, Mihara E, Nogi T, Sugita Y, Takagi J (2012) Crystal structure of alpha5beta1 integrin ectodomain: atomic details of the fibronectin receptor. J Cell Biol 197:131-140.
    • (2012) J Cell Biol , vol.197 , pp. 131-140
    • Nagae, M.1    Re, S.2    Mihara, E.3    Nogi, T.4    Sugita, Y.5    Takagi, J.6
  • 17
    • 84862806935 scopus 로고    scopus 로고
    • A combined strategy improves the solubility of aggregation- prone single-chain variable fragment antibodies
    • Sun W, Xie J, Lin H, Mi S, Li Z, Hua F, Hu Z (2012) A combined strategy improves the solubility of aggregation- prone single-chain variable fragment antibodies. Protein Expr Purif 83:21-29.
    • (2012) Protein Expr Purif , vol.83 , pp. 21-29
    • Sun, W.1    Xie, J.2    Lin, H.3    Mi, S.4    Li, Z.5    Hua, F.6    Hu, Z.7
  • 18
    • 56749168901 scopus 로고    scopus 로고
    • Novel affinity tag system using structurally defined antibody-tag interaction: Application to singlestep protein purification
    • Nogi T, Sangawa T, Tabata S, Nagae M, Tamura- Kawakami K, Beppu A, Hattori M, Yasui N, Takagi J (2008) Novel affinity tag system using structurally defined antibody-tag interaction: application to singlestep protein purification. Protein Sci 17:2120-2126.
    • (2008) Protein Sci , vol.17 , pp. 2120-2126
    • Nogi, T.1    Sangawa, T.2    Tabata, S.3    Nagae, M.4    Tamura- Kawakami, K.5    Beppu, A.6    Hattori, M.7    Yasui, N.8    Takagi, J.9
  • 19
    • 14644444571 scopus 로고    scopus 로고
    • Negatively charged purification tags for selective anion-exchange recovery
    • Hedhammar M, Graslund T, Uhlen M, Hober S (2004) Negatively charged purification tags for selective anion-exchange recovery. Protein Eng Des Sel 17:779- 786.
    • (2004) Protein Eng des Sel , vol.17 , pp. 779-786
    • Hedhammar, M.1    Graslund, T.2    Uhlen, M.3    Hober, S.4
  • 20
    • 19444373996 scopus 로고    scopus 로고
    • Making the most of affinity tags
    • Waugh DS (2005) Making the most of affinity tags. Trends Biotechnol 23:316-320.
    • (2005) Trends Biotechnol , vol.23 , pp. 316-320
    • Waugh, D.S.1
  • 22
    • 0035041854 scopus 로고    scopus 로고
    • C-terminal opening mimics "inside-out" activation of integrin a5b1
    • Takagi J, Erickson HP, Springer TA (2001) C-terminal opening mimics "inside-out" activation of integrin a5b1. Nature Struct Biol 8:412-416.
    • (2001) Nature Struct Biol , vol.8 , pp. 412-416
    • Takagi, J.1    Erickson, H.P.2    Springer, T.A.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.