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Volumn 49, Issue 7, 2009, Pages 1821-1830

On transversal hydrophobicity of some proteins and their modules

(1)  Galat, Andrzej a  

a DIF   (France)

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; ASCORBIC ACID; PROTEINS;

EID: 68149099512     PISSN: 15499596     EISSN: 1549960X     Source Type: Journal    
DOI: 10.1021/ci9001316     Document Type: Article
Times cited : (6)

References (82)
  • 2
    • 0037136435 scopus 로고    scopus 로고
    • Genomic analysis of membrane protein families: Abundance and conserved motifs
    • Liu, Y.; Engelman, D. M.; Gerstein, M. Genomic analysis of membrane protein families: abundance and conserved motifs. Genome Biol. 2002, 3, 1-12.
    • (2002) Genome Biol , vol.3 , pp. 1-12
    • Liu, Y.1    Engelman, D.M.2    Gerstein, M.3
  • 3
    • 0032987478 scopus 로고    scopus 로고
    • Membrane protein folding and stability: Physical principles
    • White, S. H.; Wimley, W. C. Membrane protein folding and stability: physical principles. Annu. Rev. Biophys. Biomol. Struct. 1999, 28, 319-365.
    • (1999) Annu. Rev. Biophys. Biomol. Struct , vol.28 , pp. 319-365
    • White, S.H.1    Wimley, W.C.2
  • 4
    • 34247595392 scopus 로고    scopus 로고
    • Experimental measures of amino acid hydrophobicity and the topology of transmembrane and globular proteins
    • Wolfenden, R. Experimental measures of amino acid hydrophobicity and the topology of transmembrane and globular proteins. J. Gen. Physiol. 2007, 129, 357-362.
    • (2007) J. Gen. Physiol , vol.129 , pp. 357-362
    • Wolfenden, R.1
  • 5
    • 41149127245 scopus 로고    scopus 로고
    • Vertebrate membrane proteins: Structure, function, and insights from biophysical approaches
    • Müller, D. J.; Wu, N.; Palczewski, K. Vertebrate membrane proteins: structure, function, and insights from biophysical approaches. Pharmacol. Rev. 2008, 60, 43-78.
    • (2008) Pharmacol. Rev , vol.60 , pp. 43-78
    • Müller, D.J.1    Wu, N.2    Palczewski, K.3
  • 6
    • 33644681545 scopus 로고    scopus 로고
    • Neurotransmission: The autonomic and somatic motor nervous systems
    • 11th ed, Brunton, L, Lazo, J, Parker, K, Eds, McGraw-Hill, Medical Publishing Division: New York
    • Westfall, T. C.; Westfall, D. P. Neurotransmission: the autonomic and somatic motor nervous systems. In Goodman & Gilman's: the Pharmacology Basis of Therapeutics, 11th ed.; Brunton, L., Lazo, J., Parker, K., Eds.; McGraw-Hill, Medical Publishing Division: New York, 2005; pp 137-181.
    • (2005) Goodman & Gilman's: The Pharmacology Basis of Therapeutics , pp. 137-181
    • Westfall, T.C.1    Westfall, D.P.2
  • 7
    • 0842324481 scopus 로고    scopus 로고
    • Hallucinogens
    • Nichols, D. E. Hallucinogens. Pharmacol. Ther. 2004, 101, 131-181.
    • (2004) Pharmacol. Ther , vol.101 , pp. 131-181
    • Nichols, D.E.1
  • 9
    • 68149102839 scopus 로고    scopus 로고
    • Charney, D. S.; Mihic, S. J.; Harris, R. A. Hypnotics and sedatives. In Goodman & Gilman's: the Pharmacology Basis of Therapeutics, 11th ed.; Brunton, L., Lazo, J., Parker, K., Eds.; McGraw-Hill Medical Publishing Division: New York, 2005; pp 401-427.
    • Charney, D. S.; Mihic, S. J.; Harris, R. A. Hypnotics and sedatives. In Goodman & Gilman's: the Pharmacology Basis of Therapeutics, 11th ed.; Brunton, L., Lazo, J., Parker, K., Eds.; McGraw-Hill Medical Publishing Division: New York, 2005; pp 401-427.
  • 10
    • 41149176081 scopus 로고    scopus 로고
    • Mammalian bombesin receptors: Nomenclature, distribution, pharmacology, signaling, and functions in normal and disease states
    • Rev
    • Jensen, R. T.; Battey, J. F.; Spindel, E. R.; Benya, R. V. Mammalian bombesin receptors: nomenclature, distribution, pharmacology, signaling, and functions in normal and disease states. Pharmacol. Rev. 2008, 60, 1-42.
    • (2008) Pharmacol , vol.60 , pp. 1-42
    • Jensen, R.T.1    Battey, J.F.2    Spindel, E.R.3    Benya, R.V.4
  • 12
    • 58849094130 scopus 로고    scopus 로고
    • Topology of class A G protein-coupled receptors: Insights gained from crystal structures of rhodopsins, adrenergic and adenosine receptors
    • Mustafi, D.; Palczewski, K. Topology of class A G protein-coupled receptors: insights gained from crystal structures of rhodopsins, adrenergic and adenosine receptors. Mol. Pharmacol. 2009, 75, 1-12.
    • (2009) Mol. Pharmacol , vol.75 , pp. 1-12
    • Mustafi, D.1    Palczewski, K.2
  • 14
    • 33748796612 scopus 로고    scopus 로고
    • Involvment of some large immunophilins and their ligands in the protection and regeneration of neurons: A hypothetical mode of action
    • Galat, A. Involvment of some large immunophilins and their ligands in the protection and regeneration of neurons: a hypothetical mode of action. Comp. Biol. Chem. 2006, 30, 348-359.
    • (2006) Comp. Biol. Chem , vol.30 , pp. 348-359
    • Galat, A.1
  • 15
    • 37249067732 scopus 로고    scopus 로고
    • The origin of protein interactions and allostery in colocalization
    • Kuriyan, J.; Eisenberg, D. The origin of protein interactions and allostery in colocalization. Nature 2007, 450, 983-990.
    • (2007) Nature , vol.450 , pp. 983-990
    • Kuriyan, J.1    Eisenberg, D.2
  • 16
    • 47649125643 scopus 로고    scopus 로고
    • Allosteric regulation and catalysis emerge via a common route
    • Goodey, N. M.; Benkovic, S. J. Allosteric regulation and catalysis emerge via a common route. Nat. Chem. Biol. 2008, 4, 474-482.
    • (2008) Nat. Chem. Biol , vol.4 , pp. 474-482
    • Goodey, N.M.1    Benkovic, S.J.2
  • 19
    • 36049033946 scopus 로고    scopus 로고
    • Hedgehog regulates smoothened activity by inducing a conformational switch
    • Zhao, Y.; Tong, C.; Jiang, J. Hedgehog regulates smoothened activity by inducing a conformational switch. Nature 2007, 450, 252-258.
    • (2007) Nature , vol.450 , pp. 252-258
    • Zhao, Y.1    Tong, C.2    Jiang, J.3
  • 22
    • 47049130668 scopus 로고    scopus 로고
    • Crystal structure of the ligand-free G-protein-coupled receptor opsin
    • Park, J. H.; Scheerer, P.; Hofmann, K. P.; Choe, H. W.; Ernst, O. P. Crystal structure of the ligand-free G-protein-coupled receptor opsin. Nature 2008, 454, 183-187.
    • (2008) Nature , vol.454 , pp. 183-187
    • Park, J.H.1    Scheerer, P.2    Hofmann, K.P.3    Choe, H.W.4    Ernst, O.P.5
  • 23
    • 43749109187 scopus 로고    scopus 로고
    • Crystal structure of squid rhodopsin
    • Murakami, M.; Kouyama, T. Crystal structure of squid rhodopsin. Nature 2008, 453, 363-368.
    • (2008) Nature , vol.453 , pp. 363-368
    • Murakami, M.1    Kouyama, T.2
  • 30
    • 33751035450 scopus 로고    scopus 로고
    • Crystal structure of a multidomain immunophilin from Arabidopsis thaliana: A paradigm for regulation of plant ABC transporters
    • Granzin, J.; Eckhoff, A.; Weiergraber, O. H. Crystal structure of a multidomain immunophilin from Arabidopsis thaliana: a paradigm for regulation of plant ABC transporters. J. Mol. Biol. 2006, 364, 799-809.
    • (2006) J. Mol. Biol , vol.364 , pp. 799-809
    • Granzin, J.1    Eckhoff, A.2    Weiergraber, O.H.3
  • 32
    • 2942593899 scopus 로고    scopus 로고
    • 3D structure of human FK506-binding protein 52: Implications for the assembly of the glucocorticoid receptor/Hsp90/immunophilin heterocomplex
    • Wu, B.; Li, R.; Liu, Y.; Lou, Z.; Ding, Y.; Shu, C.; Ye, S.; Bartlam, M.; Shen, B.; Rao, Z. 3D structure of human FK506-binding protein 52: implications for the assembly of the glucocorticoid receptor/Hsp90/immunophilin heterocomplex. Proc. Natl. Acad. Sci. U.S.A. 2004, 101, 8348-8353.
    • (2004) Proc. Natl. Acad. Sci. U.S.A , vol.101 , pp. 8348-8353
    • Wu, B.1    Li, R.2    Liu, Y.3    Lou, Z.4    Ding, Y.5    Shu, C.6    Ye, S.7    Bartlam, M.8    Shen, B.9    Rao, Z.10
  • 33
    • 0345144024 scopus 로고    scopus 로고
    • Structure of the large FK506-binding protein FKBP51, an Hsp90-binding protein and a component of steroid receptor complex
    • Sinars, C.; Cheung-Flynn, J.; Rimerman, R. A.; Scammell, J. G.; Smith, D. F.; Clardy, J. Structure of the large FK506-binding protein FKBP51, an Hsp90-binding protein and a component of steroid receptor complex. Proc. Natl. Acad. Sci. U.S.A. 2003, 100, 868-873.
    • (2003) Proc. Natl. Acad. Sci. U.S.A , vol.100 , pp. 868-873
    • Sinars, C.1    Cheung-Flynn, J.2    Rimerman, R.A.3    Scammell, J.G.4    Smith, D.F.5    Clardy, J.6
  • 34
    • 0036405903 scopus 로고    scopus 로고
    • Redesign of a four-helix bundle protein by phage display coupled with proteolysis and structural characterization by NMR and X-ray crystallography
    • Chu, R.; Takei, J.; Knowlton, J. R.; Andrykovitch, M.; Pei, W.; Kajava, A. V.; Steinbach, P. J.; Ji, X.; Bai, Y. Redesign of a four-helix bundle protein by phage display coupled with proteolysis and structural characterization by NMR and X-ray crystallography. J. Mol. Biol. 2002, 323, 253-262.
    • (2002) J. Mol. Biol , vol.323 , pp. 253-262
    • Chu, R.1    Takei, J.2    Knowlton, J.R.3    Andrykovitch, M.4    Pei, W.5    Kajava, A.V.6    Steinbach, P.J.7    Ji, X.8    Bai, Y.9
  • 35
    • 53849148622 scopus 로고    scopus 로고
    • Covalent and noncovalent intermediates of an NAD utilizing enzyme, human CD38
    • Liu, Q.; Kriksunov, I. A.; Jiang, H.; Graeff, R.; Lin, H.; Lee, H. C.; Hao, Q. Covalent and noncovalent intermediates of an NAD utilizing enzyme, human CD38. Chem. Biol. 2008, 15, 1068-1078.
    • (2008) Chem. Biol , vol.15 , pp. 1068-1078
    • Liu, Q.1    Kriksunov, I.A.2    Jiang, H.3    Graeff, R.4    Lin, H.5    Lee, H.C.6    Hao, Q.7
  • 36
    • 0034124850 scopus 로고    scopus 로고
    • Flt3 ligand structure and unexpected commonalities of helical bundles and cystine knots
    • Savvides, S. N.; Boone, T.; Karplus, P. A. Flt3 ligand structure and unexpected commonalities of helical bundles and cystine knots. Nat. Struct. Biol. 2000, 7, 486-491.
    • (2000) Nat. Struct. Biol , vol.7 , pp. 486-491
    • Savvides, S.N.1    Boone, T.2    Karplus, P.A.3
  • 37
    • 44349135549 scopus 로고    scopus 로고
    • Conserved structural determinants in three-fingered protein domains
    • Galat, A.; Gross, G.; Drevet, P.; Sato, A.; Ménez, A. Conserved structural determinants in three-fingered protein domains. FEBS J. 2008, 275, 3207-3225.
    • (2008) FEBS J , vol.275 , pp. 3207-3225
    • Galat, A.1    Gross, G.2    Drevet, P.3    Sato, A.4    Ménez, A.5
  • 38
    • 0029098342 scopus 로고
    • Isolation of a cDNA encoding a novel human FK506-binding protein homolog containing leucine zipper and tetratricopeptide repeat motifs
    • Lam, E.; Martin, M.; Wiederrecht, G. Isolation of a cDNA encoding a novel human FK506-binding protein homolog containing leucine zipper and tetratricopeptide repeat motifs. Gene 1995, 160, 297-302.
    • (1995) Gene , vol.160 , pp. 297-302
    • Lam, E.1    Martin, M.2    Wiederrecht, G.3
  • 39
    • 0031002895 scopus 로고    scopus 로고
    • Ma, Q.; Whitlock, J. P. A novel cytoplasmic protein that interacts with the Ah receptor contains tetratricopeptide repeat motifs, and augments the transcriptional response to 2,3,7,8-tetrachlorodibenzo-p-dioxin. J. Biol. Chem. 1997, 272, 8878-8884.
    • Ma, Q.; Whitlock, J. P. A novel cytoplasmic protein that interacts with the Ah receptor contains tetratricopeptide repeat motifs, and augments the transcriptional response to 2,3,7,8-tetrachlorodibenzo-p-dioxin. J. Biol. Chem. 1997, 272, 8878-8884.
  • 41
    • 0027968068 scopus 로고
    • CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting position-specific gap penalties and weight matrix choice
    • Thompson, J. D.; Higgins, D. G.; Gibson, T. J. CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting position-specific gap penalties and weight matrix choice. Nucleic Acids Res. 1994, 22, 4673-4680.
    • (1994) Nucleic Acids Res , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 42
    • 33846036096 scopus 로고    scopus 로고
    • The worldwide Protein Data Bank (wwPDB): Ensuring a single, uniform archive of PDB data
    • Berman, H. M.; Henrick, K.; Nakamura, H.; Markley, J. L. The worldwide Protein Data Bank (wwPDB): ensuring a single, uniform archive of PDB data. Nucleic Acids Res. 2007, 35, D301-D303.
    • (2007) Nucleic Acids Res , vol.35
    • Berman, H.M.1    Henrick, K.2    Nakamura, H.3    Markley, J.L.4
  • 43
    • 44349186241 scopus 로고    scopus 로고
    • Functional drift of sequence attributes in the FK506-binding proteins (FKBPs)
    • Galat, A. Functional drift of sequence attributes in the FK506-binding proteins (FKBPs). J. Chem. Inf. Model. 2008, 48, 1118-1130.
    • (2008) J. Chem. Inf. Model , vol.48 , pp. 1118-1130
    • Galat, A.1
  • 44
    • 68149143904 scopus 로고    scopus 로고
    • DeLano Scientific: San Carlos, CA, U.S.A, accessed Jan 12, 2009
    • DeLano, W. L. The PyMOL Molecular Graphics System; DeLano Scientific: San Carlos, CA, U.S.A., 2002. www://pymol.sourceforge.net/ (accessed Jan 12, 2009).
    • (2002)
    • DeLano, W.L.1
  • 45
    • 0029011701 scopus 로고    scopus 로고
    • Cornell, W. D.; Cieplak, P.; Bayly, C. I.; Gould, I. R.; Merz, K. M.; Ferguson, M.; Spellmeyer, D. C.; Fox, T.; Caldwell, J. W.; Kollman, P. A. A second generation force field for the simulation of proteins, nucleic acids, and organic molecules. J. Am. Chem. Soc. 1995, 117, 5179-5197.
    • Cornell, W. D.; Cieplak, P.; Bayly, C. I.; Gould, I. R.; Merz, K. M.; Ferguson, M.; Spellmeyer, D. C.; Fox, T.; Caldwell, J. W.; Kollman, P. A. A second generation force field for the simulation of proteins, nucleic acids, and organic molecules. J. Am. Chem. Soc. 1995, 117, 5179-5197.
  • 46
    • 0020475449 scopus 로고
    • A simple method for displaying the hydropathic character of a protein
    • Kyte, J.; Doolittle, R. F. A simple method for displaying the hydropathic character of a protein. J. Mol. Biol. 1982, 157, 105-132.
    • (1982) J. Mol. Biol , vol.157 , pp. 105-132
    • Kyte, J.1    Doolittle, R.F.2
  • 47
    • 0000448982 scopus 로고
    • Prediction of protein antigenic determinants from amino acid sequences
    • Hopp, T. P.; Woods, K. R. Prediction of protein antigenic determinants from amino acid sequences. Proc. Natl. Acad. Sci. U.S.A. 1981, 78, 3824-3828.
    • (1981) Proc. Natl. Acad. Sci. U.S.A , vol.78 , pp. 3824-3828
    • Hopp, T.P.1    Woods, K.R.2
  • 48
    • 0023645034 scopus 로고
    • Hydrophobicity scales and computational techniques for detecting amphipathic structures in proteins
    • Cornette, J. L.; Cease, K. B.; Margalit, H.; Spouge, J. L.; Berzofsky, J. A.; DeLisi, C. Hydrophobicity scales and computational techniques for detecting amphipathic structures in proteins. J. Mol. Biol. 1987, 195, 659-685.
    • (1987) J. Mol. Biol , vol.195 , pp. 659-685
    • Cornette, J.L.1    Cease, K.B.2    Margalit, H.3    Spouge, J.L.4    Berzofsky, J.A.5    DeLisi, C.6
  • 49
    • 0029738872 scopus 로고    scopus 로고
    • Experimentally determined hydrophobicity scale for proteins at membrane interfaces
    • Wimley, W. C.; White, S. H. Experimentally determined hydrophobicity scale for proteins at membrane interfaces. Nat. Struct. Biol. 1996, 3, 842-848.
    • (1996) Nat. Struct. Biol , vol.3 , pp. 842-848
    • Wimley, W.C.1    White, S.H.2
  • 52
    • 0033516705 scopus 로고    scopus 로고
    • The packing density in proteins: Standard radii and volumes
    • Tsai, J.; Taylor, R.; Chothia, C.; Gerstein, M. The packing density in proteins: standard radii and volumes. J. Mol. Biol. 1999, 290, 253-266.
    • (1999) J. Mol. Biol , vol.290 , pp. 253-266
    • Tsai, J.1    Taylor, R.2    Chothia, C.3    Gerstein, M.4
  • 53
    • 2142763316 scopus 로고
    • Amino acid solubility and protein stability in aqueous maltitol solutions
    • Gekko, K.; Idota, Y. Amino acid solubility and protein stability in aqueous maltitol solutions. Aerig. Biol. Chem. 1989, 53, 89-95.
    • (1989) Aerig. Biol. Chem , vol.53 , pp. 89-95
    • Gekko, K.1    Idota, Y.2
  • 54
    • 0010232287 scopus 로고    scopus 로고
    • Solubilities of the common L-a-amino acids as a function of temperature and solution pH
    • Amend, J. P.; Helgeson, H. C. Solubilities of the common L-a-amino acids as a function of temperature and solution pH. Pure Appl. Chem. 1997, 69, 935-942.
    • (1997) Pure Appl. Chem , vol.69 , pp. 935-942
    • Amend, J.P.1    Helgeson, H.C.2
  • 55
    • 10244258777 scopus 로고
    • The anomalous hydrophilic character of proline
    • Gibbs, P. R.; Radzicka, A.; Wolfenden, R. The anomalous hydrophilic character of proline. J. Am. Chem. Soc. 1991, 113, 4714-4715.
    • (1991) J. Am. Chem. Soc , vol.113 , pp. 4714-4715
    • Gibbs, P.R.1    Radzicka, A.2    Wolfenden, R.3
  • 56
    • 0015217634 scopus 로고
    • The solubility of amino acids and two glycine peptides in aqueous ethanol and dioxane solutions. Establishment of a hydrophobicity scale
    • Nozaki, Y.; Tanford, C. The solubility of amino acids and two glycine peptides in aqueous ethanol and dioxane solutions. Establishment of a hydrophobicity scale. J. Biol. Chem. 1971, 246, 2211-2217.
    • (1971) J. Biol. Chem , vol.246 , pp. 2211-2217
    • Nozaki, Y.1    Tanford, C.2
  • 58
    • 0035812599 scopus 로고    scopus 로고
    • Energetics, stability, and prediction of transmembrane helices
    • Jayasinghe, S.; Hristova, K.; White, S. H. Energetics, stability, and prediction of transmembrane helices. J. Mol. Biol. 2001, 312, 927-934.
    • (2001) J. Mol. Biol , vol.312 , pp. 927-934
    • Jayasinghe, S.1    Hristova, K.2    White, S.H.3
  • 59
  • 60
    • 2342529037 scopus 로고    scopus 로고
    • A note on clustering the functionally-related paralogues and orthologues of proteins: A case of the FK506-binding proteins (FKBPs)
    • Galat, A. A note on clustering the functionally-related paralogues and orthologues of proteins: a case of the FK506-binding proteins (FKBPs). Comp. Biol. Chem. 2004, 28, 129-140.
    • (2004) Comp. Biol. Chem , vol.28 , pp. 129-140
    • Galat, A.1
  • 61
    • 4043129511 scopus 로고    scopus 로고
    • Function-dependent clustering of orthologues and paralogues of cyclophilins
    • Galat, A. Function-dependent clustering of orthologues and paralogues of cyclophilins. Proteins 2004, 56, 808-820.
    • (2004) Proteins , vol.56 , pp. 808-820
    • Galat, A.1
  • 62
    • 55549092037 scopus 로고    scopus 로고
    • The three-fingered protein domain of the human genome
    • Galat, A. The three-fingered protein domain of the human genome. Cell. Mol. Life Sci. 2008, 65, 3481-3493.
    • (2008) Cell. Mol. Life Sci , vol.65 , pp. 3481-3493
    • Galat, A.1
  • 63
    • 0031008576 scopus 로고    scopus 로고
    • Hydrophobicity regained
    • Karplus, P. A. Hydrophobicity regained. Protein Sci. 1997, 6, 1302-1307.
    • (1997) Protein Sci , vol.6 , pp. 1302-1307
    • Karplus, P.A.1
  • 64
    • 33745194016 scopus 로고    scopus 로고
    • Hydrophobic collapse in (in silico) protein folding
    • Brylinski, M.; Konieczny, L.; Roterman, I. Hydrophobic collapse in (in silico) protein folding. Comput. Biol. Chem. 2006, 30, 255-267.
    • (2006) Comput. Biol. Chem , vol.30 , pp. 255-267
    • Brylinski, M.1    Konieczny, L.2    Roterman, I.3
  • 65
    • 34250787537 scopus 로고    scopus 로고
    • Anchoring of the 26S proteasome to the organellar membrane by FKBP38
    • Nakagawa, T.; Shirane, M.; Iemura, S.; Natsume, T.; Nakayama, K. I. Anchoring of the 26S proteasome to the organellar membrane by FKBP38. Genes Cells 2007, 12, 709-719.
    • (2007) Genes Cells , vol.12 , pp. 709-719
    • Nakagawa, T.1    Shirane, M.2    Iemura, S.3    Natsume, T.4    Nakayama, K.I.5
  • 66
    • 49049103512 scopus 로고    scopus 로고
    • FKBP8 cell-autonomously controls neural tube patterning through a GU2- and Kif3a-dependent mechanism
    • Cho, A.; Ko, H. W.; Eggenschwiler, J. T. FKBP8 cell-autonomously controls neural tube patterning through a GU2- and Kif3a-dependent mechanism. Dev. Biol. 2008, 321, 27-39.
    • (2008) Dev. Biol , vol.321 , pp. 27-39
    • Cho, A.1    Ko, H.W.2    Eggenschwiler, J.T.3
  • 67
    • 0037227946 scopus 로고    scopus 로고
    • Inherent calcineurin inhibitor FKBP38 targets Bc1-2 to mitochondria and inhibits apoptosis
    • Shirane, M.; Nakayama, K. I. Inherent calcineurin inhibitor FKBP38 targets Bc1-2 to mitochondria and inhibits apoptosis. Nat. Cell Biol. 2003, 5, 28-37.
    • (2003) Nat. Cell Biol , vol.5 , pp. 28-37
    • Shirane, M.1    Nakayama, K.I.2
  • 68
    • 54449097914 scopus 로고    scopus 로고
    • The switch I region of Rheb is critical for its interaction with FKBP38
    • Ma, D.; Bai, X.; Guo, S.; Jiang, Y. The switch I region of Rheb is critical for its interaction with FKBP38. J. Biol. Chem. 2008, 283, 25963-25970.
    • (2008) J. Biol. Chem , vol.283 , pp. 25963-25970
    • Ma, D.1    Bai, X.2    Guo, S.3    Jiang, Y.4
  • 69
    • 57649165557 scopus 로고    scopus 로고
    • Re-evaluating the roles of proposed modulators of mammalian target of rapamycin complex 1 (mTORCl) signaling
    • Wang, X.; Fonseca, B. D.; Tang, H.; Liu, R.; Elia, A.; Clemens, M. J.; Bommer, U. A.; Proud, C. G. Re-evaluating the roles of proposed modulators of mammalian target of rapamycin complex 1 (mTORCl) signaling. J. Biol. Chem. 2008, 283, 30482-30492.
    • (2008) J. Biol. Chem , vol.283 , pp. 30482-30492
    • Wang, X.1    Fonseca, B.D.2    Tang, H.3    Liu, R.4    Elia, A.5    Clemens, M.J.6    Bommer, U.A.7    Proud, C.G.8
  • 70
    • 21244498243 scopus 로고    scopus 로고
    • G protein receptors 7 and 8 are expressed in human adrenocortical cells, and their endogenous ligands neuropeptides B and W enhance cortisol secretion by activating adenylate cyclase- and phospholipase C-dependent signaling cascades
    • Mazzocchi, G.; Rebuffat, P.; Ziolkowska, A.; Rossi, G. P.; Malendowicz, L. K.; Nussdorfer, G. G. G protein receptors 7 and 8 are expressed in human adrenocortical cells, and their endogenous ligands neuropeptides B and W enhance cortisol secretion by activating adenylate cyclase- and phospholipase C-dependent signaling cascades. J. Clin. Endocrinol. Metab. 2005, 90, 3466-3471.
    • (2005) J. Clin. Endocrinol. Metab , vol.90 , pp. 3466-3471
    • Mazzocchi, G.1    Rebuffat, P.2    Ziolkowska, A.3    Rossi, G.P.4    Malendowicz, L.K.5    Nussdorfer, G.G.6
  • 73
    • 11444265536 scopus 로고    scopus 로고
    • The crystal structure of NlpI. A prokaryotic tetratricopeptide repeat protein with a globular fold
    • Wilson, C. G.; Kajander, T.; Regan, L. The crystal structure of NlpI. A prokaryotic tetratricopeptide repeat protein with a globular fold. FEBS J. 2005, 272, 166-179.
    • (2005) FEBS J , vol.272 , pp. 166-179
    • Wilson, C.G.1    Kajander, T.2    Regan, L.3
  • 74
    • 34250796909 scopus 로고    scopus 로고
    • Kajander, T.; Cortajarena, A. L.; Mochrie, S.; Regan, L. Structure and stability of designed TPR protein superhelices: unusual crystal packing and implications for natural TPR proteins. Acta Crystalloer., Sect. D: Biol. Crystalloer. 2007, 63 (Pt 7), 800-811.
    • Kajander, T.; Cortajarena, A. L.; Mochrie, S.; Regan, L. Structure and stability of designed TPR protein superhelices: unusual crystal packing and implications for natural TPR proteins. Acta Crystalloer., Sect. D: Biol. Crystalloer. 2007, 63 (Pt 7), 800-811.
  • 75
    • 41149127699 scopus 로고    scopus 로고
    • Dimerization and oligomerization of G-protein-coupled receptors: Debated structures with established and emerging functions
    • Szidonya, L.; Cserzo, M.; Hunyady, L. Dimerization and oligomerization of G-protein-coupled receptors: debated structures with established and emerging functions. J. Endocrinol. 2008, 196, 435-453.
    • (2008) J. Endocrinol , vol.196 , pp. 435-453
    • Szidonya, L.1    Cserzo, M.2    Hunyady, L.3
  • 77
    • 46449109015 scopus 로고    scopus 로고
    • Structure and energetics of the hydrogenbonded backbone in protein folding
    • Bolen, D. W.; Rose, G. D. Structure and energetics of the hydrogenbonded backbone in protein folding. Annu. Rev. Biochem. 2008, 77, 339-362.
    • (2008) Annu. Rev. Biochem , vol.77 , pp. 339-362
    • Bolen, D.W.1    Rose, G.D.2
  • 78
    • 0004053611 scopus 로고
    • 2nd edition; John Wiley & Sons: New York
    • Voet, D.; Voet, J. G. Biochemistry, 2nd edition; John Wiley & Sons: New York, 1995; pp 141-214.
    • (1995) Biochemistry , pp. 141-214
    • Voet, D.1    Voet, J.G.2
  • 79
    • 66149109184 scopus 로고    scopus 로고
    • Solvent accessible surface area of amino acid residues in globular proteins: Correlation of apparebt transfer free energies with the experimental hydrophobicity scales
    • Shaytan, A. K.; Shaitan, K. V.; Khokhlov, A. R. Solvent accessible surface area of amino acid residues in globular proteins: correlation of apparebt transfer free energies with the experimental hydrophobicity scales. Biomacromolecules 2009, 10, 1224-1237.
    • (2009) Biomacromolecules , vol.10 , pp. 1224-1237
    • Shaytan, A.K.1    Shaitan, K.V.2    Khokhlov, A.R.3
  • 80
    • 49149124400 scopus 로고    scopus 로고
    • Characterization of the tetratricopeptide-containing domain of BUB1, BUBR1, and PP5 proves that domain amphiphilicity over amino acid sequence specificity governs protein adsorption and interfacial activity
    • Beaufils, S.; Grossmann, J. G.; Renault, A.; Bolanos-Garcia, V. M. Characterization of the tetratricopeptide-containing domain of BUB1, BUBR1, and PP5 proves that domain amphiphilicity over amino acid sequence specificity governs protein adsorption and interfacial activity. J. Phys. Chem. B 2008, 112, 7984-7991.
    • (2008) J. Phys. Chem. B , vol.112 , pp. 7984-7991
    • Beaufils, S.1    Grossmann, J.G.2    Renault, A.3    Bolanos-Garcia, V.M.4
  • 82
    • 0033551778 scopus 로고    scopus 로고
    • The tetratricopeptide repeat domain and a C-terminal region control the activity of Ser/Thr protein phosphatase 5
    • Sinclair, C.; Borchers, C.; Parker, C.; Tomer, K.; Charbonneau, H.; Rossie, S. The tetratricopeptide repeat domain and a C-terminal region control the activity of Ser/Thr protein phosphatase 5. J. Biol. Chem. 1999, 274, 23666-23672.
    • (1999) J. Biol. Chem , vol.274 , pp. 23666-23672
    • Sinclair, C.1    Borchers, C.2    Parker, C.3    Tomer, K.4    Charbonneau, H.5    Rossie, S.6


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