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Volumn 2012, Issue , 2012, Pages

Membrane protein stability analyses by means of protein energy profiles in case of nephrogenic diabetes insipidus

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; DEFECTS; NONDESTRUCTIVE EXAMINATION;

EID: 84859736908     PISSN: 1748670X     EISSN: 17486718     Source Type: Journal    
DOI: 10.1155/2012/790281     Document Type: Article
Times cited : (7)

References (56)
  • 1
    • 13444280419 scopus 로고    scopus 로고
    • PDBTM: Selection and membrane localization of transmembrane proteins in the protein data bank
    • Tusndy G. E., Dosztnyi Z., Simon I., PDBTM: selection and membrane localization of transmembrane proteins in the protein data bank Nucleic Acids Research 2005 33 D275 D278
    • (2005) Nucleic Acids Research , vol.33
    • Tusndy, G.E.1    Dosztnyi, Z.2    Simon, I.3
  • 2
    • 10244252813 scopus 로고    scopus 로고
    • Transmembrane proteins in the Protein Data Bank: Identification and classification
    • DOI 10.1093/bioinformatics/bth340
    • Tusndy G. E., Dosztnyi Z., Simon I., Transmembrane proteins in the Protein Data Bank: identification and classification Bioinformatics 2004 20 17 2964 2972 (Pubitemid 39619188)
    • (2004) Bioinformatics , vol.20 , Issue.17 , pp. 2964-2972
    • Tusnady, G.E.1    Dosztanyi, Z.2    Simon, I.3
  • 4
    • 33846693208 scopus 로고    scopus 로고
    • A novel pattern recognition algorithm to classify membrane protein unfolding pathways with high-throughput single-molecule force spectroscopy
    • Marsico A., Labudde D., Sapra T., Muller D. J., Schroeder M., A novel pattern recognition algorithm to classify membrane protein unfolding pathways with high-throughput single-molecule force spectroscopy Bioinformatics 2007 23 2 e231 e236
    • (2007) Bioinformatics , vol.23 , Issue.2
    • Marsico, A.1    Labudde, D.2    Sapra, T.3    Muller, D.J.4    Schroeder, M.5
  • 9
    • 67649159317 scopus 로고    scopus 로고
    • Diabetes insipidus in pregnancy: Etiology, eva luation, and management
    • Ananthakrishnan S., Diabetes insipidus in pregnancy: etiology, eva luation, and management Endocrine Practice 2009 15 4 377 382
    • (2009) Endocrine Practice , vol.15 , Issue.4 , pp. 377-382
    • Ananthakrishnan, S.1
  • 10
    • 78650555603 scopus 로고    scopus 로고
    • Recurrent pregnancy-induced diabetes insipidus in a woman with hemochromatosis
    • Krysiak R., Kobielusz-Gembala I., Okopien B., Recurrent pregnancy-induced diabetes insipidus in a woman with hemochromatosis Endocrine Journal 2010 57 12 1023 1028
    • (2010) Endocrine Journal , vol.57 , Issue.12 , pp. 1023-1028
    • Krysiak, R.1    Kobielusz-Gembala, I.2    Okopien, B.3
  • 13
    • 0028326794 scopus 로고
    • Requirement of human renal water channel aquaporin-2 for vasopressin-dependent concentration of urine
    • Deen P. M. T., Verdijk M. A. J., Knoers N. V. A. M., Wieringa B., Monnens L. A. H., Van Os C. H., Van Oost B. A., Requirement of human renal water channel aquaporin-2 for vasopressin-dependent concentration of urine Science 1994 264 5155 92 95 (Pubitemid 24144492)
    • (1994) Science , vol.264 , Issue.5155 , pp. 92-95
    • Deen, P.M.T.1    Verdijk, M.A.J.2    Knoers, N.V.A.M.3    Wieringa, B.4    Monnens, L.A.H.5    Van Os, C.H.6    Van Oost, B.A.7
  • 15
    • 77956119735 scopus 로고    scopus 로고
    • Potential of nonpeptide (ant)agonists to rescue vasopressin V2 receptor mutants for the treatment of X-linked nephrogenic diabetes insipidus
    • Los E. L., Deen P. M., Robben J. H., Potential of nonpeptide (ant)agonists to rescue vasopressin V2 receptor mutants for the treatment of X-linked nephrogenic diabetes insipidus Journal of Neuroendocrinology 2010 22 5 393 399
    • (2010) Journal of Neuroendocrinology , vol.22 , Issue.5 , pp. 393-399
    • Los, E.L.1    Deen, P.M.2    Robben, J.H.3
  • 16
    • 33746586548 scopus 로고    scopus 로고
    • Cell biological aspects of the vasopressin type-2 receptor and aquaporin 2 water channel in nephrogenic diabetes insipidus
    • Robben J. H., Knoers N. V. A. M., Deen P. M. T., Cell biological aspects of the vasopressin type-2 receptor and aquaporin 2 water channel in nephrogenic diabetes insipidus American Journal of Physiology 2006 291 2 F257 F270
    • (2006) American Journal of Physiology , vol.291 , Issue.2
    • Robben, J.H.1    Knoers, N.V.A.M.2    Deen, P.M.T.3
  • 17
    • 0031951116 scopus 로고    scopus 로고
    • Structural bases of vasopressin/oxytocin receptor function
    • DOI 10.1677/joe.0.1560223
    • Barberis C., Mouillac B., Durroux T., Structural bases of vasopressin/oxytocin receptor function Journal of Endocrinology 1998 156 2 223 229 (Pubitemid 28105809)
    • (1998) Journal of Endocrinology , vol.156 , Issue.2 , pp. 223-229
    • Barberis, C.1    Mouillac, B.2    Durroux, T.3
  • 18
    • 33644790823 scopus 로고    scopus 로고
    • α systems
    • DOI 10.1002/psc.714
    • lusarz M. J., Giedo A., lusarz R., Ciarkowski J., Analysis of interactions responsible for vasopressin binding to human neurohypophyseal hormone receptorsmolecular dynamics study of the activated receptor-vasopressin- G systems Journal of Peptide Science 2006 12 3 180 189 (Pubitemid 43349358)
    • (2006) Journal of Peptide Science , vol.12 , Issue.3 , pp. 180-189
    • Slusarz, M.J.1    Gieldon, A.2    Slusarz, R.3    Ciarkowski, J.4
  • 19
    • 33646111925 scopus 로고    scopus 로고
    • Molecular docking-based study of vasopressin analogues modified at positions 2 and 3 with N-methylphenylalanine: Influence on receptor-bound conformations and interactions with vasopressin and oxytocin receptors
    • lusarz M. J., Sikorska E., lusarz R., Ciarkowski J., Molecular docking-based study of vasopressin analogues modified at positions 2 and 3 with N-methylphenylalanine: influence on receptor-bound conformations and interactions with vasopressin and oxytocin receptors Journal of Medicinal Chemistry 2006 49 8 2463 2469
    • (2006) Journal of Medicinal Chemistry , vol.49 , Issue.8 , pp. 2463-2469
    • Lusarz, M.J.1    Sikorska, E.2    Lusarz, R.3    Ciarkowski, J.4
  • 20
    • 77954065271 scopus 로고    scopus 로고
    • I-TASSER: A unified platform for automated protein structure and function prediction
    • Roy A., Kucukural A., Zhang Y., I-TASSER: a unified platform for automated protein structure and function prediction Nature Protocols 2010 5 4 725 738
    • (2010) Nature Protocols , vol.5 , Issue.4 , pp. 725-738
    • Roy, A.1    Kucukural, A.2    Zhang, Y.3
  • 22
    • 0000224283 scopus 로고    scopus 로고
    • CHARMM: The energy function and its parameterization with an overview of the program
    • Schleyer P. V. R. Chichester, UK John Wiley Sons
    • MacKerell A. D., Brooks B., Brooks C. L., Schleyer P. V. R., CHARMM: the energy function and its parameterization with an overview of the program The Encyclopedia of Computational Chemistry. 1 1998 Chichester, UK John Wiley Sons 271 277
    • (1998) The Encyclopedia of Computational Chemistry. 1 , pp. 271-277
    • MacKerell, A.D.1    Brooks, B.2    Brooks, C.L.3
  • 23
    • 4444221676 scopus 로고    scopus 로고
    • From structure to disease: The evolving tale of aquaporin biology
    • DOI 10.1038/nrm1469
    • King L. S., Kozono D., Agre P., From structure to disease: the evolving tale of aquaporin biology Nature Reviews Molecular Cell Biology 2004 5 9 687 698 (Pubitemid 39208179)
    • (2004) Nature Reviews Molecular Cell Biology , vol.5 , Issue.9 , pp. 687-698
    • King, L.S.1    Kozono, D.2    Agre, P.3
  • 25
    • 0141534474 scopus 로고    scopus 로고
    • The mechanism of proton exclusion in the aquaporin-1 water channel
    • DOI 10.1016/j.jmb.2003.08.003
    • de Groot B. L., Frigato T., Helms V., Grubmller H., The mechanism of proton exclusion in the aquaporin-1 water channel Journal of Molecular Biology 2003 333 2 279 293 (Pubitemid 37188572)
    • (2003) Journal of Molecular Biology , vol.333 , Issue.2 , pp. 279-293
    • De Groot, B.L.1    Frigato, T.2    Helms, V.3    Grubmuller, H.4
  • 26
    • 1642493669 scopus 로고    scopus 로고
    • Molecular basis of proton blockage in aquaporins
    • DOI 10.1016/j.str.2003.11.017
    • Chakrabarti N., Tajkhorshid E., Roux B., Poms R., Molecular basis of proton blockage in aquaporins Structure 2004 12 1 65 74 (Pubitemid 38114807)
    • (2004) Structure , vol.12 , Issue.1 , pp. 65-74
    • Chakrabarti, N.1    Tajkhorshid, E.2    Roux, B.3    Pomes, R.4
  • 27
    • 4644308725 scopus 로고    scopus 로고
    • Structural determinants of proton blockage in aquaporins
    • DOI 10.1016/j.jmb.2004.08.036, PII S0022283604010162
    • Chakrabarti N., Roux B., Poms R., Structural determinants of proton blockage in aquaporins Journal of Molecular Biology 2004 343 2 493 510 (Pubitemid 39296881)
    • (2004) Journal of Molecular Biology , vol.343 , Issue.2 , pp. 493-510
    • Chakrabarti, N.1    Roux, B.2    Pomes, R.3
  • 29
  • 30
    • 0015859467 scopus 로고
    • Principles that govern the folding of protein chains
    • Anfinsen C. B., Principles that govern the folding of protein chains Science 1973 181 4096 223 230
    • (1973) Science , vol.181 , Issue.4096 , pp. 223-230
    • Anfinsen, C.B.1
  • 32
    • 11144347566 scopus 로고    scopus 로고
    • Erratum: Development and testing of a general amber force field (Journal of Computational Chemistry (2004) 25 (1157))
    • ARTICLE 114
    • Wang J., Wolf R. M., Caldwell J. W., Kollman P. A., Case D. A., Erratum: Development and testing of a general amber force field (Journal of Computational Chemistry (2004) 25 (1157)) Journal of Computational Chemistry 2005 26 1, article 114
    • (2005) Journal of Computational Chemistry , vol.26 , Issue.1
    • Wang, J.1    Wolf, R.M.2    Caldwell, J.W.3    Kollman, P.A.4    Case, D.A.5
  • 34
    • 0017021957 scopus 로고
    • Medium- and long-range interaction parameters between amino acids for predicting three-dimensional structures of proteins
    • Tanaka S., Scheraga H. A., Medium- and long-range interaction parameters between amino acids for predicting three-dimensional structures of proteins Macromolecules 1976 9 6 945 950
    • (1976) Macromolecules , vol.9 , Issue.6 , pp. 945-950
    • Tanaka, S.1    Scheraga, H.A.2
  • 35
    • 0017926896 scopus 로고
    • Influence of water on protein structure. An analysis of the preferences of amino acid residues for the inside or outside and for specific conformations in a protein molecule
    • Wertz D. H., Scheraga H. A., Influence of water on protein structure. An analysis of the preferences of amino acid residues for the inside or outside and for specific conformations in a protein molecule Macromolecules 1978 11 1 9 15
    • (1978) Macromolecules , vol.11 , Issue.1 , pp. 9-15
    • Wertz, D.H.1    Scheraga, H.A.2
  • 37
    • 0025830469 scopus 로고
    • A method to identify protein sequences that fold into a known three-dimensional structure
    • Bowie J. U., Luthy R., Eisenberg D., A method to identify protein sequences that fold into a known three-dimensional structure Science 1991 253 5016 164 170 (Pubitemid 21917131)
    • (1991) Science , vol.253 , Issue.5016 , pp. 164-170
    • Bowie, J.U.1    Luthy, R.2    Eisenberg, D.3
  • 38
    • 66149176906 scopus 로고    scopus 로고
    • Context dependent reference states of solvent accessibility derived from native protein structures and assessed by predictability analysis
    • Singh H., Ahmad S., Context dependent reference states of solvent accessibility derived from native protein structures and assessed by predictability analysis BMC Structural Biology 2009 9, article 25
    • (2009) BMC Structural Biology , vol.925
    • Singh, H.1    Ahmad, S.2
  • 39
    • 0027650879 scopus 로고
    • Boltzmann's principle, knowledge-based mean fields and protein folding. An approach to the computational determination of protein structures
    • Sippl M. J., Boltzmann's principle, knowledge-based mean fields and protein folding. An approach to the computational determination of protein structures Journal of Computer-Aided Molecular Design 1993 7 4 473 501
    • (1993) Journal of Computer-Aided Molecular Design , vol.7 , Issue.4 , pp. 473-501
    • Sippl, M.J.1
  • 40
    • 0014757386 scopus 로고
    • A general method applicable to the search for similarities in the amino acid sequence of two proteins
    • Needleman S. B., Wunsch C. D., A general method applicable to the search for similarities in the amino acid sequence of two proteins Journal of Molecular Biology 1970 48 3 443 453
    • (1970) Journal of Molecular Biology , vol.48 , Issue.3 , pp. 443-453
    • Needleman, S.B.1    Wunsch, C.D.2
  • 41
    • 0019887799 scopus 로고
    • Identification of common molecular subsequences
    • Smith T. F., Waterman M. S., Identification of common molecular subsequences Journal of Molecular Biology 1981 147 1 195 197
    • (1981) Journal of Molecular Biology , vol.147 , Issue.1 , pp. 195-197
    • Smith, T.F.1    Waterman, M.S.2
  • 42
    • 0029976603 scopus 로고    scopus 로고
    • [22] using CLUSTAL for multiple sequence alignments
    • Higgins D. G., Thompson J. D., Gibson T. J., [22] Using CLUSTAL for multiple sequence alignments Methods in Enzymology 1996 266 383 400 (Pubitemid 126509340)
    • (1996) Methods in Enzymology , vol.266 , pp. 383-400
    • Higgins, D.G.1    Thompson, J.D.2    Gibson, T.J.3
  • 43
    • 1842298212 scopus 로고    scopus 로고
    • From levinthal to pathways to funnels
    • DOI 10.1038/nsb0197-10
    • Dill K. A., Chan H. S., From levinthal to pathways to funnels Nature Structural Biology 1997 4 1 10 19 (Pubitemid 27020916)
    • (1997) Nature Structural Biology , vol.4 , Issue.1 , pp. 10-19
    • Dill, K.A.1    Chan, H.S.2
  • 44
    • 13444307044 scopus 로고    scopus 로고
    • Secondary-structure matching (SSM), a new tool for fast protein structure alignment in three dimensions
    • DOI 10.1107/S0907444904026460
    • Krissinel E., Henrick K., Secondary-structure matching (SSM), a new tool for fast protein structure alignment in three dimensions Acta Crystallographica Section D 2004 60 12, part 1 2256 2268 (Pubitemid 41742778)
    • (2004) Acta Crystallographica Section D: Biological Crystallography , vol.60 , Issue.12 , pp. 2256-2268
    • Krissinel, E.1    Henrick, K.2
  • 46
    • 0000742931 scopus 로고
    • A neural-gas network learns topologies
    • Kohonen T. Mkisara K. Simula O. Kangas J. Amsterdam, The Netherlands North-Holland
    • Martinetz T. M., Schulten K. J., Kohonen T., Mkisara K., Simula O., Kangas J., A neural-gas network learns topologies Artificial Neural Networks 1991 Amsterdam, The Netherlands North-Holland 397 402
    • (1991) Artificial Neural Networks , pp. 397-402
    • Martinetz, T.M.1    Schulten, K.J.2
  • 48
    • 74049093947 scopus 로고    scopus 로고
    • Application of the PM6 semi-empirical method to modeling proteins enhances docking accuracy of AutoDock
    • ARTICLE 15
    • Bikadi Z., Hazai E., Application of the PM6 semi-empirical method to modeling proteins enhances docking accuracy of AutoDock Journal of Cheminformatics 2009 1 1, article 15
    • (2009) Journal of Cheminformatics , vol.1 , Issue.1
    • Bikadi, Z.1    Hazai, E.2
  • 50
    • 32144432437 scopus 로고    scopus 로고
    • The SWISS-MODEL workspace: A web-based environment for protein structure homology modelling
    • DOI 10.1093/bioinformatics/bti770
    • Arnold K., Bordoli L., Kopp J., Schwede T., The SWISS-MODEL workspace: a web-based environment for protein structure homology modelling Bioinformatics 2006 22 2 195 201 (Pubitemid 43205406)
    • (2006) Bioinformatics , vol.22 , Issue.2 , pp. 195-201
    • Arnold, K.1    Bordoli, L.2    Kopp, J.3    Schwede, T.4
  • 54
    • 22344454347 scopus 로고    scopus 로고
    • Characterization of vasopressin V2 receptor mutants in nephrogenic diabetes insipidus in a polarized cell model
    • Robben J. H., Knoers N. V. A. M., Deen P. M. T., Characterization of vasopressin V2 receptor mutants in nephrogenic diabetes insipidus in a polarized cell model American Journal of Physiology 2005 289 2 F265 F272
    • (2005) American Journal of Physiology , vol.289 , Issue.2
    • Robben, J.H.1    Knoers, N.V.A.M.2    Deen, P.M.T.3


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