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Volumn 1784, Issue 11, 2008, Pages 1720-1727

The stability and aggregation properties of the GTPase domain from human SEPT4

Author keywords

Alzheimer's and Parkinson's diseases; Amyloid like; Chemical denaturation; Circular dichroism; Metal ion; Septin; Unfolding intermediate

Indexed keywords

DIMER; GUANINE NUCLEOTIDE BINDING PROTEIN; GUANOSINE TRIPHOSPHATASE; GUANOSINE TRIPHOSPHATE; METAL ION; SEPT4 PROTEIN; UNCLASSIFIED DRUG; UREA;

EID: 54049115857     PISSN: 15709639     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbapap.2008.06.005     Document Type: Article
Times cited : (8)

References (46)
  • 1
    • 14444286600 scopus 로고    scopus 로고
    • Polymerization of purified yeast septins: evidence that organized filament arrays may not be required for septin function
    • Frazier J.A., Wong M.L., Longtine M.S., Pringle J.R., Mann M., Mitchison T.J., and Field C. Polymerization of purified yeast septins: evidence that organized filament arrays may not be required for septin function. J. Cell. Biol. 143 (1998) 737-749
    • (1998) J. Cell. Biol. , vol.143 , pp. 737-749
    • Frazier, J.A.1    Wong, M.L.2    Longtine, M.S.3    Pringle, J.R.4    Mann, M.5    Mitchison, T.J.6    Field, C.7
  • 3
    • 0032103420 scopus 로고    scopus 로고
    • Subunit composition, protein interactions, and structures of the mammalian brain sec6/8 complex and septin filaments
    • Hsu S.C., Hazuka C.D., Roth R., Foletti D.L., Heuser J., and Scheller R.H. Subunit composition, protein interactions, and structures of the mammalian brain sec6/8 complex and septin filaments. Neuron, 20 (1998) 1111-1122
    • (1998) Neuron , vol.20 , pp. 1111-1122
    • Hsu, S.C.1    Hazuka, C.D.2    Roth, R.3    Foletti, D.L.4    Heuser, J.5    Scheller, R.H.6
  • 4
    • 0028175009 scopus 로고
    • The Drosophila peanut gene is required for cytokinesis and encodes a protein similar to yeast putative bud neck filament proteins
    • Neufeld T.P., and Rubin G.M. The Drosophila peanut gene is required for cytokinesis and encodes a protein similar to yeast putative bud neck filament proteins. Cell, 77 (1994) 371-379
    • (1994) Cell , vol.77 , pp. 371-379
    • Neufeld, T.P.1    Rubin, G.M.2
  • 7
    • 0035063573 scopus 로고    scopus 로고
    • Novel roles for mammalian septins: from vesicle trafficking to oncogenesis
    • Kartmann B., and Roth D. Novel roles for mammalian septins: from vesicle trafficking to oncogenesis. J. Cell Sci. 114 (2001) 839-844
    • (2001) J. Cell Sci. , vol.114 , pp. 839-844
    • Kartmann, B.1    Roth, D.2
  • 8
    • 0033576647 scopus 로고    scopus 로고
    • Phosphatidylinositol polyphosphate binding to the mammalian septin H5 is modulated by GTP
    • Zhang J., Kong C., Xie H., McPherson P.S., Grinstein S., and Trimble W.S. Phosphatidylinositol polyphosphate binding to the mammalian septin H5 is modulated by GTP. Curr. Biol. 9 (1999) 1458-1467
    • (1999) Curr. Biol. , vol.9 , pp. 1458-1467
    • Zhang, J.1    Kong, C.2    Xie, H.3    McPherson, P.S.4    Grinstein, S.5    Trimble, W.S.6
  • 9
    • 0033214990 scopus 로고    scopus 로고
    • Septins: structural polymers or signaling GTPases?
    • Field C., and Kellogg D. Septins: structural polymers or signaling GTPases?. Trends Cell Biol. 9 (1999) 387-394
    • (1999) Trends Cell Biol. , vol.9 , pp. 387-394
    • Field, C.1    Kellogg, D.2
  • 10
    • 0037474299 scopus 로고    scopus 로고
    • Borg/septin interactions and the assembly of mammalian septin heterodimers, trimers, and filaments
    • Sheffield P.J., Oliver C.J., Kremer B.E., Sheng S., Shao Z., and Macara I.G. Borg/septin interactions and the assembly of mammalian septin heterodimers, trimers, and filaments. J. Biol. Chem. 278 (2003) 3483-3488
    • (2003) J. Biol. Chem. , vol.278 , pp. 3483-3488
    • Sheffield, P.J.1    Oliver, C.J.2    Kremer, B.E.3    Sheng, S.4    Shao, Z.5    Macara, I.G.6
  • 13
    • 0032911523 scopus 로고    scopus 로고
    • Characterization of the mammalian septin H5: distinct patterns of cytoskeletal and membrane association from other septin proteins
    • Xie H., Surka M., Howard J., and Trimble W.S. Characterization of the mammalian septin H5: distinct patterns of cytoskeletal and membrane association from other septin proteins. Cell Motil. Cytoskeleton. 43 (1999) 52-62
    • (1999) Cell Motil. Cytoskeleton. , vol.43 , pp. 52-62
    • Xie, H.1    Surka, M.2    Howard, J.3    Trimble, W.S.4
  • 14
  • 15
    • 0036267419 scopus 로고    scopus 로고
    • Impaired expression of a human septin family gene Bradeion inhibits the growth and tumorigenesis of colorectal cancer in vitro and in vivo
    • Tanaka T., Kijima H., Itoh J., Matsuda T., and Tanaka T. Impaired expression of a human septin family gene Bradeion inhibits the growth and tumorigenesis of colorectal cancer in vitro and in vivo. Cancer Gene Therapy. 9 (2002) 483-488
    • (2002) Cancer Gene Therapy. , vol.9 , pp. 483-488
    • Tanaka, T.1    Kijima, H.2    Itoh, J.3    Matsuda, T.4    Tanaka, T.5
  • 17
    • 0038342507 scopus 로고    scopus 로고
    • Association of the cytoskeletal GTP-binding protein Sept4/H5 with cytoplasmatic inclusions found in Parkinson's disease and others synucleinopathies
    • Ihara M., Tomimoto H., Kitayama H., Morioka Y., Akigunchi I., Shibasaki H., Noda M., and Kinoshita M. Association of the cytoskeletal GTP-binding protein Sept4/H5 with cytoplasmatic inclusions found in Parkinson's disease and others synucleinopathies. J. Biol. Chem. 278 (2003) 24012-24095
    • (2003) J. Biol. Chem. , vol.278 , pp. 24012-24095
    • Ihara, M.1    Tomimoto, H.2    Kitayama, H.3    Morioka, Y.4    Akigunchi, I.5    Shibasaki, H.6    Noda, M.7    Kinoshita, M.8
  • 18
    • 7944228563 scopus 로고    scopus 로고
    • The pathobiology of the septin gene family
    • Hall P., and Russell S. The pathobiology of the septin gene family. J. Pathol. 204 (2004) 489-505
    • (2004) J. Pathol. , vol.204 , pp. 489-505
    • Hall, P.1    Russell, S.2
  • 19
    • 0032961592 scopus 로고    scopus 로고
    • Characterization of a novel gene, PNULT2, on human chromosome 17q22-23 and its exclusion as the Meckel syndrome gene
    • Paavola P., Horelli-Kuitunen N., Palotie A., and Peltonen L. Characterization of a novel gene, PNULT2, on human chromosome 17q22-23 and its exclusion as the Meckel syndrome gene. Genomics 55 (1999) 122-125
    • (1999) Genomics , vol.55 , pp. 122-125
    • Paavola, P.1    Horelli-Kuitunen, N.2    Palotie, A.3    Peltonen, L.4
  • 20
    • 0034739803 scopus 로고    scopus 로고
    • Characterization and expression analysis of two human septin genes, PNUTL1 and PNUTL2
    • Zieger B., Tran H., Hainmanna I., Wunderle D., Zgaga-Griesz A., Blaser S., and Ware J. Characterization and expression analysis of two human septin genes, PNUTL1 and PNUTL2. Gene 261 (2000) 197-203
    • (2000) Gene , vol.261 , pp. 197-203
    • Zieger, B.1    Tran, H.2    Hainmanna, I.3    Wunderle, D.4    Zgaga-Griesz, A.5    Blaser, S.6    Ware, J.7
  • 24
    • 0035941201 scopus 로고    scopus 로고
    • Metal-triggered structural transformations, aggregation and fibrillation of human a-synunclein
    • Uversky V.N., Li J., and Fink A.L. Metal-triggered structural transformations, aggregation and fibrillation of human a-synunclein. J. Biol. Chem. 276 (2001) 44284-44296
    • (2001) J. Biol. Chem. , vol.276 , pp. 44284-44296
    • Uversky, V.N.1    Li, J.2    Fink, A.L.3
  • 25
    • 34848893368 scopus 로고    scopus 로고
    • An intermediate structure in the thermal unfolding of the GTPase domain of human septin 4 (SEPT4/Bradeion-b) forms amyloid-like filaments in vitro
    • Garcia W., Araújo A.P.U., Lara F., Foguel D., Tanaka M., Tanaka T., and Garratt R.C. An intermediate structure in the thermal unfolding of the GTPase domain of human septin 4 (SEPT4/Bradeion-b) forms amyloid-like filaments in vitro. Biochemistry 46 (2007) 11101-11109
    • (2007) Biochemistry , vol.46 , pp. 11101-11109
    • Garcia, W.1    Araújo, A.P.U.2    Lara, F.3    Foguel, D.4    Tanaka, M.5    Tanaka, T.6    Garratt, R.C.7
  • 26
    • 0023950869 scopus 로고
    • Solubility of different folding conformers of bovine growth hormone
    • Brems D.N. Solubility of different folding conformers of bovine growth hormone. Biochemistry 27 (1988) 4541-4546
    • (1988) Biochemistry , vol.27 , pp. 4541-4546
    • Brems, D.N.1
  • 27
    • 0037154980 scopus 로고    scopus 로고
    • Protein folding and unfolding at atomic resolution
    • Fersht A.R., and Daggett V. Protein folding and unfolding at atomic resolution. Cell, 108 (1999) 573-582
    • (1999) Cell , vol.108 , pp. 573-582
    • Fersht, A.R.1    Daggett, V.2
  • 28
    • 0027730097 scopus 로고
    • Rationally designing the accumulation of a folding intermediate of barnase by protein engineering
    • Sanz J.M., and Fersht A.R. Rationally designing the accumulation of a folding intermediate of barnase by protein engineering. Biochemistry 32 (1993) 13584-13592
    • (1993) Biochemistry , vol.32 , pp. 13584-13592
    • Sanz, J.M.1    Fersht, A.R.2
  • 29
    • 54049106663 scopus 로고    scopus 로고
    • C.M. Dobson, Oxford University press, New York. (2000) 1-33.
    • C.M. Dobson, Oxford University press, New York. (2000) 1-33.
  • 31
    • 0024448151 scopus 로고
    • Calculation of proteins extinction coefficients from amino acid sequence data
    • Gill S.C., and von Hippel P.H. Calculation of proteins extinction coefficients from amino acid sequence data. Anal. Biochem. 182 (1989) 319-326
    • (1989) Anal. Biochem. , vol.182 , pp. 319-326
    • Gill, S.C.1    von Hippel, P.H.2
  • 32
    • 0025308218 scopus 로고
    • Interactions of tubulin with guanylyl-(beta-gamma-methylene)diphosphonate-formation and assembly of a stoichiometric complex
    • Seckler R., Wu G.M., and Timasheff S.N. Interactions of tubulin with guanylyl-(beta-gamma-methylene)diphosphonate-formation and assembly of a stoichiometric complex. J. Biol. Chem. 265 (1990) 7655-7661
    • (1990) J. Biol. Chem. , vol.265 , pp. 7655-7661
    • Seckler, R.1    Wu, G.M.2    Timasheff, S.N.3
  • 34
    • 84944815124 scopus 로고
    • Small-angle-scattering-data treatment by the regularization method
    • Svergun D.I., Semenyuk A.V., and Feigin L.A. Small-angle-scattering-data treatment by the regularization method. Acta crystallogr. 44 (1988) 244-250
    • (1988) Acta crystallogr. , vol.44 , pp. 244-250
    • Svergun, D.I.1    Semenyuk, A.V.2    Feigin, L.A.3
  • 35
    • 0026910457 scopus 로고
    • Determination of the regularization parameter in indirect-transform methods using perceptual criteria
    • Svergun D.I. Determination of the regularization parameter in indirect-transform methods using perceptual criteria. J. Appl. Crystallogr. 25 (1992) 495-503
    • (1992) J. Appl. Crystallogr. , vol.25 , pp. 495-503
    • Svergun, D.I.1
  • 36
    • 0033001996 scopus 로고    scopus 로고
    • Restoring low resolution structure of biological macromolecules from solution scattering using simulated annealing
    • Svergun D.I. Restoring low resolution structure of biological macromolecules from solution scattering using simulated annealing. Biophys. J. 76 (1999) 2879-2886
    • (1999) Biophys. J. , vol.76 , pp. 2879-2886
    • Svergun, D.I.1
  • 37
    • 0037701771 scopus 로고    scopus 로고
    • New methods for domain structure determination of proteins from solution scattering data
    • Petoukhov M.V., and Svergun D.I. New methods for domain structure determination of proteins from solution scattering data. J. Appl. Crystallogr. 36 (2003) 540-544
    • (2003) J. Appl. Crystallogr. , vol.36 , pp. 540-544
    • Petoukhov, M.V.1    Svergun, D.I.2
  • 38
    • 0037166276 scopus 로고    scopus 로고
    • Amyloid-like fibril formation in an all beta-barrel protein involves the formation of partially structured intermediate(s)
    • Srisailam S., Wang H.M., Kumar T.K.S., Rajalingam D., Sivaraja V., Sheu H.S., Chang Y.C., and Yu C. Amyloid-like fibril formation in an all beta-barrel protein involves the formation of partially structured intermediate(s). J. Biol. Chem. 277 (2002) 19027-19036
    • (2002) J. Biol. Chem. , vol.277 , pp. 19027-19036
    • Srisailam, S.1    Wang, H.M.2    Kumar, T.K.S.3    Rajalingam, D.4    Sivaraja, V.5    Sheu, H.S.6    Chang, Y.C.7    Yu, C.8
  • 39
    • 33746377894 scopus 로고    scopus 로고
    • Protein misfolding, functional amyloid, and human disease
    • Chiti F., and Dobson C.M. Protein misfolding, functional amyloid, and human disease. Annu. Rev. Biochem. 75 (2006) 333-366
    • (2006) Annu. Rev. Biochem. , vol.75 , pp. 333-366
    • Chiti, F.1    Dobson, C.M.2
  • 40
    • 0035914136 scopus 로고    scopus 로고
    • p53 unfolding detected by CD but not by tryptophan fluorescence
    • Nichols N.M., and Matthews K.S. p53 unfolding detected by CD but not by tryptophan fluorescence. Biochem. Biophys. Res. Commun. 288 (2001) 111-115
    • (2001) Biochem. Biophys. Res. Commun. , vol.288 , pp. 111-115
    • Nichols, N.M.1    Matthews, K.S.2
  • 41
    • 1442337555 scopus 로고    scopus 로고
    • The majority of the Saccharomyces cerevisiae septin complexes do not exchange guanine nucleotides
    • Vrabioiu A.M., Gerber S.A., Gygi S.P., Field C.M., and Mitchison T.J. The majority of the Saccharomyces cerevisiae septin complexes do not exchange guanine nucleotides. J. Biol. Chem. 279 (2004) 3111-3118
    • (2004) J. Biol. Chem. , vol.279 , pp. 3111-3118
    • Vrabioiu, A.M.1    Gerber, S.A.2    Gygi, S.P.3    Field, C.M.4    Mitchison, T.J.5
  • 43
    • 0030871206 scopus 로고    scopus 로고
    • Refolding of urea-denatured tubulin: recovery of native-like structure and colchicine binding activity from partly unfolded states
    • Guha S., and Bhattacharyya B. Refolding of urea-denatured tubulin: recovery of native-like structure and colchicine binding activity from partly unfolded states. Biochemistry 36 (1997) 13208-13213
    • (1997) Biochemistry , vol.36 , pp. 13208-13213
    • Guha, S.1    Bhattacharyya, B.2
  • 44
    • 0029562577 scopus 로고
    • Partially folded states of proteins - characterization by X-ray-scattering
    • Doniach S., Bascle J., Garel T., and Orland H. Partially folded states of proteins - characterization by X-ray-scattering. J. Mol. Biol. 254 (1995) 960-967
    • (1995) J. Mol. Biol. , vol.254 , pp. 960-967
    • Doniach, S.1    Bascle, J.2    Garel, T.3    Orland, H.4


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