메뉴 건너뛰기




Volumn 107, Issue 7, 2010, Pages 2824-2829

Engineering an artificial zymogen by alternate frame protein folding

Author keywords

Design; HIV protease; Molecular switch; Mutually exclusive folding

Indexed keywords

ENZYME PRECURSOR; POLYPEPTIDE; PROTEINASE; RIBONUCLEASE; RIBONUCLEASE BARNASE; TRYPSIN; UNCLASSIFIED DRUG; UREA;

EID: 77649241924     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.0907668107     Document Type: Article
Times cited : (29)

References (22)
  • 2
    • 57049128294 scopus 로고    scopus 로고
    • Design and characterization of an HIV-specific ribonuclease zymogen
    • Turcotte RF, Raines RT (2008) Design and characterization of an HIV-specific ribonuclease zymogen. AIDS Res Hum Retro 24:1357-1363.
    • (2008) AIDS Res Hum Retro , vol.24 , pp. 1357-1363
    • Turcotte, R.F.1    Raines, R.T.2
  • 3
    • 33751112474 scopus 로고    scopus 로고
    • A ribonuclease zymogen activated by the NS3 protease of the hepatitis C virus
    • Johnson RJ, Lin SR, Raines RT (2006) A ribonuclease zymogen activated by the NS3 protease of the hepatitis C virus. FEBS J 273:5457-5465.
    • (2006) FEBS J , vol.273 , pp. 5457-5465
    • Johnson, R.J.1    Lin, S.R.2    Raines, R.T.3
  • 4
    • 65249094239 scopus 로고    scopus 로고
    • Structural and thermodynamic analysis of a conformationally-strained circular permutant of barnase
    • Butler JS, Mitrea DM, Mitrousis G, Cingolani G, Loh SN (2009) Structural and thermodynamic analysis of a conformationally-strained circular permutant of barnase. Biochemistry 48:3497-3507.
    • (2009) Biochemistry , vol.48 , pp. 3497-3507
    • Butler, J.S.1    Mitrea, D.M.2    Mitrousis, G.3    Cingolani, G.4    Loh, S.N.5
  • 5
    • 0024501923 scopus 로고
    • Kinetic characterization of the recombinant ribonuclease from Bacillus amyloliquifaciens (barnase) and investigation of key residues in catalysis by site-directed mutagenesis
    • Mossakowska DE, Nyberg K, Fersht AR (1989) Kinetic characterization of the recombinant ribonuclease from Bacillus amyloliquifaciens (barnase) and investigation of key residues in catalysis by site-directed mutagenesis. Biochemistry 28:3843-3850.
    • (1989) Biochemistry , vol.28 , pp. 3843-3850
    • Mossakowska, D.E.1    Nyberg, K.2    Fersht, A.R.3
  • 6
    • 58149164666 scopus 로고    scopus 로고
    • 2+-sensing molecular switch based on alternate frame protein folding
    • 2+-sensing molecular switch based on alternate frame protein folding. ACS Chem Biol 3:723-732.
    • (2008) ACS Chem Biol , vol.3 , pp. 723-732
    • Stratton, M.M.1    Mitrea, D.M.2    Loh, S.N.3
  • 7
    • 0034284978 scopus 로고    scopus 로고
    • Identification of efficiently cleaved substrates for HIV-1 protease using a phage display library and use in inhibitor development
    • Beck ZQ, Hervio L, Dawson PE, Elder JH, Madison EL (2000) Identification of efficiently cleaved substrates for HIV-1 protease using a phage display library and use in inhibitor development. Virology 274:391-401.
    • (2000) Virology , vol.274 , pp. 391-401
    • Beck, Z.Q.1    Hervio, L.2    Dawson, P.E.3    Elder, J.H.4    Madison, E.L.5
  • 8
    • 0034032433 scopus 로고    scopus 로고
    • Stability and folding of the protein complexes of barnase
    • Neira JL, Vázquez E, Fersht AR (2000) Stability and folding of the protein complexes of barnase. Eur J Biochem 267:2859-2870.
    • (2000) Eur J Biochem , vol.267 , pp. 2859-2870
    • Neira, J.L.1    Vázquez, E.2    Fersht, A.R.3
  • 9
    • 0027527209 scopus 로고
    • Circular dichroism studies of barnase and its mutants: Characterization of the contribution of aromatic side chains
    • Vuilleumier S, Sancho J, Loewenthal R, Fersht AR (1993) Circular dichroism studies of barnase and its mutants: Characterization of the contribution of aromatic side chains. Biochemistry 32:10303-10313.
    • (1993) Biochemistry , vol.32 , pp. 10303-10313
    • Vuilleumier, S.1    Sancho, J.2    Loewenthal, R.3    Fersht, A.R.4
  • 10
    • 33644831449 scopus 로고    scopus 로고
    • Modular enzyme design: Regulation by mutually exclusive protein folding
    • Ha J-H, Butler JS, Mitrea DM, Loh SN (2006) Modular enzyme design: Regulation by mutually exclusive protein folding. J Mol Biol 357:1058-1062.
    • (2006) J Mol Biol , vol.357 , pp. 1058-1062
    • Ha, J.-H.1    Butler, J.S.2    Mitrea, D.M.3    Loh, S.N.4
  • 11
    • 0026553768 scopus 로고
    • The folding of an enzyme II. Substructure of barnase and the contribution of different interactions to protein stability
    • Serrano L, Kellis JTJ, Cann P, Matouschek A, Fersht AR (1992) The folding of an enzyme II. Substructure of barnase and the contribution of different interactions to protein stability. J Mol Biol 224:783-804.
    • (1992) J Mol Biol , vol.224 , pp. 783-804
    • Serrano, L.1    Kellis, J.T.J.2    Cann, P.3    Matouschek, A.4    Fersht, A.R.5
  • 12
    • 0034807947 scopus 로고    scopus 로고
    • Fast, facile, hypersensitive assays for ribonucleolytic activity
    • Park C, et al. (2001) Fast, facile, hypersensitive assays for ribonucleolytic activity. Methods Enzymol 341:81-94.
    • (2001) Methods Enzymol , vol.341 , pp. 81-94
    • Park, C.1
  • 13
    • 65249094873 scopus 로고    scopus 로고
    • Crystal structure of procaspase-1 zymogen domain reveals insight into inflammatory caspase autoactivation
    • Elliott JM, Rouge L, Wiesmann C, Scheer JM (2009) Crystal structure of procaspase-1 zymogen domain reveals insight into inflammatory caspase autoactivation. J Biol Chem 284(10):6546-6553.
    • (2009) J Biol Chem , vol.284 , Issue.10 , pp. 6546-6553
    • Elliott, J.M.1    Rouge, L.2    Wiesmann, C.3    Scheer, J.M.4
  • 15
    • 0033613235 scopus 로고    scopus 로고
    • Circular permutation and receptor insertion within green fluorescent protein
    • Baird GS, Zacharias DA, Tsien RY (1999) Circular permutation and receptor insertion within green fluorescent protein. Proc Natl Acad Sci USA 96:11241-11246.
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 11241-11246
    • Baird, G.S.1    Zacharias, D.A.2    Tsien, R.Y.3
  • 16
    • 34247593368 scopus 로고    scopus 로고
    • Exploring subdomain cooperativity in T4 lysozyme I: Structural and energetic studies of a circular permutant and protein fragment
    • Cellitti J, et al. (2007) Exploring subdomain cooperativity in T4 lysozyme I: Structural and energetic studies of a circular permutant and protein fragment. Protein Sci 16(5):842-851.
    • (2007) Protein Sci , vol.16 , Issue.5 , pp. 842-851
    • Cellitti, J.1
  • 17
    • 33845980623 scopus 로고    scopus 로고
    • Mechanical unfolding pathways of the enhanced yellow fluorescent protein revealed by single molecule force spectroscopy
    • Perez-Jiminez R, Garcia-Manyes S, Ainavarapu SRK, Fernandez JM (2006) Mechanical unfolding pathways of the enhanced yellow fluorescent protein revealed by single molecule force spectroscopy. J Biol Chem 281:40010-40014.
    • (2006) J Biol Chem , vol.281 , pp. 40010-40014
    • Perez-Jiminez, R.1    Garcia-Manyes, S.2    Ainavarapu, S.R.K.3    Fernandez, J.M.4
  • 18
    • 0029760326 scopus 로고    scopus 로고
    • Different folding transition states may result in the same native structure
    • Viguera AR, Serrano L, Wilmanns M (1996) Different folding transition states may result in the same native structure. Nat Struct Biol 3:874-880.
    • (1996) Nat Struct Biol , vol.3 , pp. 874-880
    • Viguera, A.R.1    Serrano, L.2    Wilmanns, M.3
  • 19
    • 0031586001 scopus 로고    scopus 로고
    • Stabilization of a recombinant Fv fragment by base-loop interconnection and VH-VL permutation
    • Brinkmann U, et al. (1997) Stabilization of a recombinant Fv fragment by base-loop interconnection and VH-VL permutation. J Mol Biol 268:107-117.
    • (1997) J Mol Biol , vol.268 , pp. 107-117
    • Brinkmann, U.1
  • 20
    • 55549098922 scopus 로고    scopus 로고
    • Changes of protein-folding pathways by circular permutation: Overlapping nuclei promote global cooperativity
    • OlivebergM
    • Haglund E, Lindberg MO, OlivebergM(2008) Changes of protein-folding pathways by circular permutation: Overlapping nuclei promote global cooperativity. J Biol Chem 283:27904-27915.
    • (2008) J Biol Chem , vol.283 , pp. 27904-27915
    • Haglund, E.1    Lindberg, M.O.2
  • 21
    • 0026516388 scopus 로고
    • A fully active variant of dihydrofolate reductase with a circularly permuted sequence
    • Buchwalder A, Szadkowski H, Kirschner K (1992) A fully active variant of dihydrofolate reductase with a circularly permuted sequence. Biochemistry 31:1621-1630.
    • (1992) Biochemistry , vol.31 , pp. 1621-1630
    • Buchwalder, A.1    Szadkowski, H.2    Kirschner, K.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.