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Volumn 80, Issue 3, 2001, Pages 1169-1173

Modeling Pseudomonas syringae ice-nucleation protein as a β-helical protein

Author keywords

[No Author keywords available]

Indexed keywords

ANTIFREEZE PROTEIN; MEMBRANE PROTEIN;

EID: 0035119209     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-3495(01)76093-6     Document Type: Article
Times cited : (77)

References (24)
  • 4
    • 0032872990 scopus 로고    scopus 로고
    • Ice-binding surface of fish type III antifreeze
    • Chen, G., and Z. Jia. 1999. Ice-binding surface of fish type III antifreeze. Biophys. J. 77:1602-1608.
    • (1999) Biophys. J. , vol.77 , pp. 1602-1608
    • Chen, G.1    Jia, Z.2
  • 6
    • 0000687463 scopus 로고
    • Size of bacterial ice nucleation sites measured in situ by radiation inactivation analysis
    • Govindarajan, A. G., and S. E. Lindow. 1988. Size of bacterial ice nucleation sites measured in situ by radiation inactivation analysis. Proc. Natl. Acad. Sci. U.S.A. 85:1334-1338.
    • (1988) Proc. Natl. Acad. Sci. U.S.A. , vol.85 , pp. 1334-1338
    • Govindarajan, A.G.1    Lindow, S.E.2
  • 7
    • 0033597140 scopus 로고    scopus 로고
    • Quantitative and qualitative analysis of type III antifreeze protein structure and function
    • Graether, S. P., C. I. DeLuca, J. Baardsnes, G. A. Hill, P. L. Davies, and Z. Jia. 1999. Quantitative and qualitative analysis of type III antifreeze protein structure and function. J. Biol. Chem. 274:11842-11847.
    • (1999) J. Biol. Chem. , vol.274 , pp. 11842-11847
    • Graether, S.P.1    Deluca, C.I.2    Baardsnes, J.3    Hill, G.A.4    Davies, P.L.5    Jia, Z.6
  • 8
    • 0034691594 scopus 로고    scopus 로고
    • β-Helix structure and ice-binding properties of a hyperactive antifreeze protein from an insect
    • Graether, S. P., M. J. Kuiper, S. M. Gagne, V. K. Walker, Z. Jia, B. D. Sykes, and P. L. Davies. 2000. β-Helix structure and ice-binding properties of a hyperactive antifreeze protein from an insect. Nature. 406: 325-327.
    • (2000) Nature , vol.406 , pp. 325-327
    • Graether, S.P.1    Kuiper, M.J.2    Gagne, S.M.3    Walker, V.K.4    Jia, Z.5    Sykes, B.D.6    Davies, P.L.7
  • 9
    • 0030760436 scopus 로고    scopus 로고
    • Hyperactive antifreeze protein from beetles
    • Graham, L. A., Y. C. Liou, V. K. Walker, and P. L. Davies. 1997. Hyperactive antifreeze protein from beetles. Nature. 388:727-728.
    • (1997) Nature , vol.388 , pp. 727-728
    • Graham, L.A.1    Liou, Y.C.2    Walker, V.K.3    Davies, P.L.4
  • 10
    • 0024227793 scopus 로고
    • Deletion mutagenesis of the ice nucleation gene from Pseudomonas syringae S203
    • Green, R. L., L. V. Corotto, and G. J. Warren. 1988. Deletion mutagenesis of the ice nucleation gene from Pseudomonas syringae S203. Mol. Gen. Genet. 215:165-172.
    • (1988) Mol. Gen. Genet. , vol.215 , pp. 165-172
    • Green, R.L.1    Corotto, L.V.2    Warren, G.J.3
  • 11
    • 0000243829 scopus 로고
    • PROCHECK: A program to check the stereochemical quality of protein structures
    • Laskowski, R. A., M. W. MacArthuer, D. Moss, and J. M. Thornton. 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    MacArthuer, M.W.2    Moss, D.3    Thornton, J.M.4
  • 12
    • 0034691568 scopus 로고    scopus 로고
    • Mimicry of ice structure by surface hydroxyls and water of a β-helix antifreeze protein
    • Liou, Y. C., A. Tocilj, P. L. Davies, and Z. Jia. 2000. Mimicry of ice structure by surface hydroxyls and water of a β-helix antifreeze protein. Nature. 406:322-324.
    • (2000) Nature , vol.406 , pp. 322-324
    • Liou, Y.C.1    Tocilj, A.2    Davies, P.L.3    Jia, Z.4
  • 13
    • 0026610767 scopus 로고
    • Assessment of protein models with three-dimensional profiles
    • Luthy, R., J. U. Bowie, and D. Eisenberg. 1992. Assessment of protein models with three-dimensional profiles. Nature. 356:83-85.
    • (1992) Nature , vol.356 , pp. 83-85
    • Luthy, R.1    Bowie, J.U.2    Eisenberg, D.3
  • 14
    • 0026293775 scopus 로고
    • Principles and biotechnological applications of bacterial ice nucleation
    • Margaritis, A., and A. S. Bassi. 1991. Principles and biotechnological applications of bacterial ice nucleation. Crit. Rev. Biotechnol. 11: 277-295.
    • (1991) Crit. Rev. Biotechnol. , vol.11 , pp. 277-295
    • Margaritis, A.1    Bassi, A.S.2
  • 15
    • 0032973262 scopus 로고    scopus 로고
    • A leucine-rich repeat protein of carrot that exhibits antifreeze activity
    • Meyer, K., M. Keil, and M. J. Naldrett. 1999. A leucine-rich repeat protein of carrot that exhibits antifreeze activity. FEES Lett. 447:171-178.
    • (1999) FEES Lett. , vol.447 , pp. 171-178
    • Meyer, K.1    Keil, M.2    Naldrett, M.J.3
  • 16
    • 0024603266 scopus 로고
    • Prediction of the conformation of ice-nucleation protein by conformational energy calculation
    • Mizuno, H. 1989. Prediction of the conformation of ice-nucleation protein by conformational energy calculation. Proteins. 5:47-65.
    • (1989) Proteins , vol.5 , pp. 47-65
    • Mizuno, H.1
  • 17
    • 0028844306 scopus 로고
    • A left-handed parallel beta helix in the structure of UDP-N-acetylglucosamine acyltransferase
    • Raetz, C. R., and S. L. Roderick. 1995. A left-handed parallel beta helix in the structure of UDP-N-acetylglucosamine acyltransferase. Science. 270: 997-1000.
    • (1995) Science , vol.270 , pp. 997-1000
    • Raetz, C.R.1    Roderick, S.L.2
  • 18
    • 0030766938 scopus 로고    scopus 로고
    • Molecular organisation of the ice nucleation protein InaV from Pseudomonas syringae
    • Schmid, D., D. Pridmore, G. Capitani, R. Battistutta, J. R. Neeser, and A. Jann. 1997. Molecular organisation of the ice nucleation protein InaV from Pseudomonas syringae. FEES Lett. 414:590-594.
    • (1997) FEES Lett. , vol.414 , pp. 590-594
    • Schmid, D.1    Pridmore, D.2    Capitani, G.3    Battistutta, R.4    Neeser, J.R.5    Jann, A.6
  • 20
    • 0029081224 scopus 로고
    • Circular dichroism of the parallel β-helical proteins pectate lyase C and E
    • Sieber, V., F. Jurnak, and R. M. Gregory. 1995. Circular dichroism of the parallel β-helical proteins pectate lyase C and E. Proteins. 23:32-37.
    • (1995) Proteins , vol.23 , pp. 32-37
    • Sieber, V.1    Jurnak, F.2    Gregory, R.M.3
  • 22
    • 0023696514 scopus 로고
    • Nonlinear relationship between concentration and activity of a bacterial ice nucleation protein
    • Southworth, M. W., P. K. Wolber, and G. J. Warren. 1988. Nonlinear relationship between concentration and activity of a bacterial ice nucleation protein. J. Biol. Chem. 263:15211-15216.
    • (1988) J. Biol. Chem. , vol.263 , pp. 15211-15216
    • Southworth, M.W.1    Wolber, P.K.2    Warren, G.J.3
  • 24
    • 0031008303 scopus 로고    scopus 로고
    • A hairpin-loop conformation in tandem repeat sequence of the ice nucleation protein revealed by NMR spectroscopy
    • Tsuda, S., A. Ito, and N. Matsushima. 1997. A hairpin-loop conformation in tandem repeat sequence of the ice nucleation protein revealed by NMR spectroscopy. FEBS Lett. 409:227-231.
    • (1997) FEBS Lett. , vol.409 , pp. 227-231
    • Tsuda, S.1    Ito, A.2    Matsushima, N.3


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