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Volumn 15, Issue 11, 2006, Pages 2612-2618

Stabilization of a binary protein complex by intein-mediated cyclization

Author keywords

Circular protein; Fusion protein; Intein; LIM domain; LMO4; Protein cyclization; Protein stability

Indexed keywords

BACTERIAL PROTEIN; BINDING PROTEIN; FLICE INHIBITORY PROTEIN; INTEIN; LIM PROTEIN; PROTEIN CZ FLINCA4; UNCLASSIFIED DRUG;

EID: 33751073463     PISSN: 09618368     EISSN: 1469896X     Source Type: Journal    
DOI: 10.1110/ps.062377006     Document Type: Article
Times cited : (30)

References (37)
  • 1
    • 0034004352 scopus 로고    scopus 로고
    • The LIM domain: Regulation by association
    • Bach, I. 2000. The LIM domain: Regulation by association. Mech. Dev. 91: 5-17.
    • (2000) Mech. Dev. , vol.91 , pp. 5-17
    • Bach, I.1
  • 2
    • 0033575092 scopus 로고    scopus 로고
    • Biosynthesis of a head-to-tail cyclized protein with improved biological activity
    • Camarero, J.A. and Muir, T.W. 1999. Biosynthesis of a head-to-tail cyclized protein with improved biological activity. J. Am. Chem. Soc. 121: 5597-5598.
    • (1999) J. Am. Chem. Soc. , vol.121 , pp. 5597-5598
    • Camarero, J.A.1    Muir, T.W.2
  • 3
    • 0034828385 scopus 로고    scopus 로고
    • Peptide chemical ligation inside living cells: In vivo generation of a circular protein domain
    • Camarero, J.A., Fushman, D., Cowburn, D., and Muir, T.W. 2001a. Peptide chemical ligation inside living cells: in vivo generation of a circular protein domain. Bioorg. Med. Chem. 9: 2479-2484.
    • (2001) Bioorg. Med. Chem. , vol.9 , pp. 2479-2484
    • Camarero, J.A.1    Fushman, D.2    Cowburn, D.3    Muir, T.W.4
  • 5
    • 0034797685 scopus 로고    scopus 로고
    • A hybrid plasmid for expression of toxic malarial proteins in Escherichia coli
    • Cinquin, O., Christopherson, R.I., and Menz, R.I. 2001. A hybrid plasmid for expression of toxic malarial proteins in Escherichia coli. Mol. Biochem. Parasitol. 117: 245-247.
    • (2001) Mol. Biochem. Parasitol. , vol.117 , pp. 245-247
    • Cinquin, O.1    Christopherson, R.I.2    Menz, R.I.3
  • 6
    • 0034855611 scopus 로고    scopus 로고
    • Design, production and characterization of FLIN2 and FLIN4: The engineering of intramolecular ldb1:LMO complexes
    • Deane, J.E., Sum, E., Mackay, J.P., Lindeman, G.J., Visvader, J.E., and Matthews, J.M. 2001. Design, production and characterization of FLIN2 and FLIN4: The engineering of intramolecular ldb1:LMO complexes. Protein Eng. 14: 493-499.
    • (2001) Protein Eng. , vol.14 , pp. 493-499
    • Deane, J.E.1    Sum, E.2    Mackay, J.P.3    Lindeman, G.J.4    Visvader, J.E.5    Matthews, J.M.6
  • 8
    • 0037543995 scopus 로고    scopus 로고
    • Structural basis for the recognition of ldb1 by the N-terminal LIM domains of LMO2 and LMO4
    • Deane, J.E., Mackay, J.P., Kwan, A.H., Sum, E.Y., Visvader, J.E., and Matthews, J.M. 2003a. Structural basis for the recognition of ldb1 by the N-terminal LIM domains of LMO2 and LMO4. EMBO J. 22: 2224-2233.
    • (2003) EMBO J. , vol.22 , pp. 2224-2233
    • Deane, J.E.1    Mackay, J.P.2    Kwan, A.H.3    Sum, E.Y.4    Visvader, J.E.5    Matthews, J.M.6
  • 12
    • 0344199948 scopus 로고    scopus 로고
    • Circular β-lactamase: Stability enhancement by cyclizing the backbone
    • Iwai, H. and Pluckthun, A. 1999. Circular β-lactamase: Stability enhancement by cyclizing the backbone. FEBS Lett. 459: 166-172.
    • (1999) FEBS Lett. , vol.459 , pp. 166-172
    • Iwai, H.1    Pluckthun, A.2
  • 13
    • 0035844128 scopus 로고    scopus 로고
    • Cyclic green fluorescent protein produced in vivo using an artificially split PI-PfuI intein from Pyrococcus furiosus
    • Iwai, H., Lingel, A., and Pluckthun, A. 2001. Cyclic green fluorescent protein produced in vivo using an artificially split PI-PfuI intein from Pyrococcus furiosus. J. Biol. Chem. 276: 16548-16554.
    • (2001) J. Biol. Chem. , vol.276 , pp. 16548-16554
    • Iwai, H.1    Lingel, A.2    Pluckthun, A.3
  • 14
    • 8444240109 scopus 로고    scopus 로고
    • The LIM domain: From the cytoskeleton to the nucleus
    • Kadrmas, J.L. and Beckerle, M.C. 2004. The LIM domain: From the cytoskeleton to the nucleus. Nat. Rev. Mol. Cell Biol. 5: 920-931.
    • (2004) Nat. Rev. Mol. Cell Biol. , vol.5 , pp. 920-931
    • Kadrmas, J.L.1    Beckerle, M.C.2
  • 15
    • 0031576337 scopus 로고    scopus 로고
    • Glutamine, alanine or glycine repeats inserted into the loop of a protein have minimal effects on stability and folding rates
    • Ladurner, A.G. and Fersht, A.R. 1997. Glutamine, alanine or glycine repeats inserted into the loop of a protein have minimal effects on stability and folding rates. J. Mol. Biol. 273: 330-337.
    • (1997) J. Mol. Biol. , vol.273 , pp. 330-337
    • Ladurner, A.G.1    Fersht, A.R.2
  • 16
    • 0000243829 scopus 로고
    • PROCHECK: A program to check the stereochemical quality of protein structures
    • Laskowski, R.A., MacArthur, M.W., Moss, D.S., and Thornton, J.M. 1993. PROCHECK: A program to check the stereochemical quality of protein structures. J. Appl. Cryst. 26: 283-291.
    • (1993) J. Appl. Cryst. , vol.26 , pp. 283-291
    • Laskowski, R.A.1    MacArthur, M.W.2    Moss, D.S.3    Thornton, J.M.4
  • 20
    • 0032584098 scopus 로고    scopus 로고
    • Protein splicing in trans by purified N- and C-terminal fragments of the Mycobacterium tuberculosis RecA intein
    • Mills, K.V., Lew, B.M., Jiang, S.-q., and Paulus, H. 1998. Protein splicing in trans by purified N- and C-terminal fragments of the Mycobacterium tuberculosis RecA intein. Proc. Natl. Acad. Sci. 95: 3543-3548.
    • (1998) Proc. Natl. Acad. Sci. , vol.95 , pp. 3543-3548
    • Mills, K.V.1    Lew, B.M.2    Jiang, S.-Q.3    Paulus, H.4
  • 21
    • 33644873716 scopus 로고    scopus 로고
    • CyBase: A database of cyclic protein sequence and structure
    • Mulvenna, J.P., Wang, C., and Craik, D.J. 2006. CyBase: A database of cyclic protein sequence and structure. Nucleic Acids Res. 34: D192-D194.
    • (2006) Nucleic Acids Res. , vol.34
    • Mulvenna, J.P.1    Wang, C.2    Craik, D.J.3
  • 23
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski, Z. and Minor, W. 1997. Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol. 276: 307-326.
    • (1997) Methods Enzymol. , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 25
    • 0033782899 scopus 로고    scopus 로고
    • Protein splicing and related forms of protein autoprocessing
    • Paulus, H. 2000. Protein splicing and related forms of protein autoprocessing. Annu. Rev. Biochem. 69: 447-496.
    • (2000) Annu. Rev. Biochem. , vol.69 , pp. 447-496
    • Paulus, H.1
  • 26
    • 0036084146 scopus 로고    scopus 로고
    • InBase: The intein database
    • Perler, F.B. 2002. InBase: The intein database. Nucleic Acids Res. 30: 383-384.
    • (2002) Nucleic Acids Res. , vol.30 , pp. 383-384
    • Perler, F.B.1
  • 27
    • 23444433268 scopus 로고    scopus 로고
    • Protein splicing mechanisms and applications
    • Perler, F.B. 2005. Protein splicing mechanisms and applications. IUBMB Life 57: 469-476.
    • (2005) IUBMB Life , vol.57 , pp. 469-476
    • Perler, F.B.1
  • 28
    • 0032964481 scopus 로고    scopus 로고
    • Automated protein model building combined with iterative structure refinement
    • Perrakis, A., Morris, R., and Lamzin, V.S. 1999. Automated protein model building combined with iterative structure refinement. Nat. Struct. Biol. 6: 458-463.
    • (1999) Nat. Struct. Biol. , vol.6 , pp. 458-463
    • Perrakis, A.1    Morris, R.2    Lamzin, V.S.3
  • 29
    • 0032502839 scopus 로고    scopus 로고
    • Contact order, transition state placement and the refolding rates of single domain proteins
    • Plaxco, K.W., Simons, K.T., and Baker, D. 1998. Contact order, transition state placement and the refolding rates of single domain proteins. J. Mol. Biol. 277: 985-994.
    • (1998) J. Mol. Biol. , vol.277 , pp. 985-994
    • Plaxco, K.W.1    Simons, K.T.2    Baker, D.3
  • 31
    • 0031715982 scopus 로고    scopus 로고
    • Protein structure alignment by incremental combinatorial extension (CE) of the optimal path
    • Shindyalov, I.N. and Bourne, P.E. 1998. Protein structure alignment by incremental combinatorial extension (CE) of the optimal path. Protein Eng. 11: 739-747.
    • (1998) Protein Eng. , vol.11 , pp. 739-747
    • Shindyalov, I.N.1    Bourne, P.E.2
  • 36
    • 0034854231 scopus 로고    scopus 로고
    • Intein-mediated ligation and cyclization of expressed proteins
    • Xu, M.Q. and Evans Jr., T.C. 2001. Intein-mediated ligation and cyclization of expressed proteins. Methods 24: 257-277.
    • (2001) Methods , vol.24 , pp. 257-277
    • Xu, M.Q.1    Evans Jr., T.C.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.