메뉴 건너뛰기




Volumn 2013, Issue , 2013, Pages

Thermal and chemical stability of two homologous poz/btb domains of kctd proteins characterized by a different oligomeric Organization

Author keywords

[No Author keywords available]

Indexed keywords

BTB PROTEIN; HISTONE DEACETYLASE 1; KCTD PROTEIN; POZ PROTEIN; PROTEIN; TETRAMER; UNCLASSIFIED DRUG; KCASH3 PROTEIN, HUMAN; KCTD5 PROTEIN, HUMAN; POTASSIUM CHANNEL; SIGNAL TRANSDUCING ADAPTOR PROTEIN; UREA;

EID: 84888635955     PISSN: 23146133     EISSN: 23146141     Source Type: Journal    
DOI: 10.1155/2013/162674     Document Type: Article
Times cited : (13)

References (26)
  • 1
    • 46249083761 scopus 로고    scopus 로고
    • Assembly reflects evolution of protein complexes
    • DOI 10.1038/nature06942, PII NATURE06942
    • Levy E. D., Erba E. B., Robinson C. V., Teichmann S. A., Assembly reflects evolution of protein complexes. Nature 2008 453 7199 1262 1265 2-s2.0-46249083761 10.1038/nature06942 (Pubitemid 351913589)
    • (2008) Nature , vol.453 , Issue.7199 , pp. 1262-1265
    • Levy, E.D.1    Erba, E.B.2    Robinson, C.V.3    Teichmann, S.A.4
  • 3
    • 34548105127 scopus 로고    scopus 로고
    • Sequence and structural analysis of BTB domain proteins
    • 2-s2.0-34548105127 ARTICLE R82
    • Stogios P. J., Downs G. S., Jauhal J. J. S., Nandra S. K., Privé G. G., Sequence and structural analysis of BTB domain proteins. Genome Biology 2005 6 10, article R82 2-s2.0-34548105127
    • (2005) Genome Biology , vol.6 , Issue.10
    • Stogios, P.J.1    Downs, G.S.2    Jauhal, J.J.S.3    Nandra, S.K.4    Privé, G.G.5
  • 7
    • 70349168448 scopus 로고    scopus 로고
    • Cullin mediates degradation of RhoA through evolutionarily conserved BTB adaptors to control actin cytoskeleton structure and cell movement
    • 2-s2.0-70349168448 10.1016/j.molcel.2009.09.004
    • Chen Y., Yang Z., Meng M., Zhao Y., Dong N., Yan H., Liu L., Ding M., Peng H. B., Shao F., Cullin mediates degradation of RhoA through evolutionarily conserved BTB adaptors to control actin cytoskeleton structure and cell movement. Molecular Cell 2009 35 6 841 855 2-s2.0-70349168448 10.1016/j.molcel.2009.09.004
    • (2009) Molecular Cell , vol.35 , Issue.6 , pp. 841-855
    • Chen, Y.1    Yang, Z.2    Meng, M.3    Zhao, Y.4    Dong, N.5    Yan, H.6    Liu, L.7    Ding, M.8    Peng, H.B.9    Shao, F.10
  • 9
    • 84866600354 scopus 로고    scopus 로고
    • Expression, purification, and secondary structure characterization of recombinant KCTD1
    • 10.1134/S0006297912080160
    • Mei F., Xiang J., Han S., He Y., Lu Y., Xu J., Guo D., Xiao G., Tien P., Sun G., Expression, purification, and secondary structure characterization of recombinant KCTD1. Biochemistry 2012 77 8 941 945 10.1134/S0006297912080160
    • (2012) Biochemistry , vol.77 , Issue.8 , pp. 941-945
    • Mei, F.1    Xiang, J.2    Han, S.3    He, Y.4    Lu, Y.5    Xu, J.6    Guo, D.7    Xiao, G.8    Tien, P.9    Sun, G.10
  • 10
    • 79960239873 scopus 로고    scopus 로고
    • Progressive myoclonic epilepsy-associated gene KCTD7 is a regulator of potassium conductance in neurons
    • 2-s2.0-79960239873 10.1007/s12035-011-8194-0
    • Azizieh R., Orduz D., van Bogaert P., Bouschet T., Rodriguez W., Schiffmann S. N., Pirson I., Abramowicz M. J., Progressive myoclonic epilepsy-associated gene KCTD7 is a regulator of potassium conductance in neurons. Molecular Neurobiology 2011 44 1 111 121 2-s2.0-79960239873 10.1007/s12035-011-8194-0
    • (2011) Molecular Neurobiology , vol.44 , Issue.1 , pp. 111-121
    • Azizieh, R.1    Orduz, D.2    Van Bogaert, P.3    Bouschet, T.4    Rodriguez, W.5    Schiffmann, S.N.6    Pirson, I.7    Abramowicz, M.J.8
  • 13
    • 79951713773 scopus 로고    scopus 로고
    • Protected from the inside: Endogenous histone deacetylase inhibitors and the road to cancer
    • 2-s2.0-79951713773 10.1016/j.bbcan.2011.01.002
    • Di Marcotullio L., Canettieri G., Infante P., Greco A., Gulino A., Protected from the inside: endogenous histone deacetylase inhibitors and the road to cancer. Biochimica et Biophysica Acta 2011 1815 2 241 252 2-s2.0-79951713773 10.1016/j.bbcan.2011.01.002
    • (2011) Biochimica et Biophysica Acta , vol.1815 , Issue.2 , pp. 241-252
    • Di Marcotullio, L.1    Canettieri, G.2    Infante, P.3    Greco, A.4    Gulino, A.5
  • 15
    • 79953802203 scopus 로고    scopus 로고
    • Design, synthesis and characterization of a peptide able to bind proteins of the KCTD family: Implications for KCTD-cullin 3 recognition
    • 2-s2.0-79953802203 10.1002/psc.1366
    • Pirone L., Correale S., de Paola I., Zaccaro L., Simone G. D., Vitagliano L., Pedone E., Gaetano S. D., Design, synthesis and characterization of a peptide able to bind proteins of the KCTD family: implications for KCTD-cullin 3 recognition. Journal of Peptide Science 2011 17 5 373 376 2-s2.0-79953802203 10.1002/psc.1366
    • (2011) Journal of Peptide Science , vol.17 , Issue.5 , pp. 373-376
    • Pirone, L.1    Correale, S.2    De Paola, I.3    Zaccaro, L.4    Simone, G.D.5    Vitagliano, L.6    Pedone, E.7    Gaetano, S.D.8
  • 18
    • 84863509384 scopus 로고    scopus 로고
    • Obscurin and KCTD6 regulate cullin-dependent small ankyrin-1 (sAnk1. 5) protein turnover
    • Lange S., Perera S., Teh P., Chen J., Obscurin and KCTD6 regulate cullin-dependent small ankyrin-1 (sAnk1. 5) protein turnover. Molecular Biology of the Cell 2012 23 2490 2504
    • (2012) Molecular Biology of the Cell , vol.23 , pp. 2490-2504
    • Lange, S.1    Perera, S.2    Teh, P.3    Chen, J.4
  • 20
    • 0029000171 scopus 로고
    • Thermodynamic analysis of the structural stability of the tetrameric oligomerization domain of p53 tumor suppressor
    • 2-s2.0-0029000171
    • Johnson C. R., Morin P. E., Arrowsmith C. H., Freire E., Thermodynamic analysis of the structural stability of the tetrameric oligomerization domain of p53 tumor suppressor. Biochemistry 1995 34 16 5309 5316 2-s2.0-0029000171
    • (1995) Biochemistry , vol.34 , Issue.16 , pp. 5309-5316
    • Johnson, C.R.1    Morin, P.E.2    Arrowsmith, C.H.3    Freire, E.4
  • 21
    • 0029797086 scopus 로고    scopus 로고
    • Temperature-induced denaturation of ribonuclease S: A thermodynamic study
    • DOI 10.1021/bi960855h
    • Catanzano F., Giancola C., Graziano G., Barone G., Temperature-induced denaturation of ribonuclease S: a thermodynamic study. Biochemistry 1996 35 41 13378 13385 2-s2.0-0029797086 10.1021/bi960855h (Pubitemid 26349432)
    • (1996) Biochemistry , vol.35 , Issue.41 , pp. 13378-13385
    • Catanzano, F.1    Giancola, C.2    Graziano, G.3    Barone, G.4
  • 22
    • 8544277232 scopus 로고    scopus 로고
    • The BACK domain in BTB-kelch proteins
    • DOI 10.1016/j.tibs.2004.10.003, PII S0968000404002634
    • Stogios P. J., Privé G. G., The BACK domain in BTB-kelch proteins. Trends in Biochemical Sciences 2004 29 12 634 637 2-s2.0-8544277232 10.1016/j.tibs.2004.10.003 (Pubitemid 39491260)
    • (2004) Trends in Biochemical Sciences , vol.29 , Issue.12 , pp. 634-637
    • Stogios, P.J.1    Prive, G.G.2
  • 23
    • 0028820703 scopus 로고
    • Denaturant m values and heat capacity changes: Relation to changes in accessible surface areas of protein unfolding
    • 2-s2.0-0028820703
    • Myers J. K., Pace C. N., Scholtz J. M., Denaturant m values and heat capacity changes: relation to changes in accessible surface areas of protein unfolding. Protein Science 1995 4 10 2138 2148 2-s2.0-0028820703
    • (1995) Protein Science , vol.4 , Issue.10 , pp. 2138-2148
    • Myers, J.K.1    Pace, C.N.2    Scholtz, J.M.3
  • 24
    • 12144259012 scopus 로고    scopus 로고
    • Dissecting contributions to the denaturant sensitivities of proteins
    • DOI 10.1021/bi048389g
    • Dempsey C. E., Piggot T. J., Mason P. E., Dissecting contributions to the denaturant sensitivities of proteins. Biochemistry 2005 44 2 775 781 2-s2.0-12144259012 10.1021/bi048389g (Pubitemid 40105509)
    • (2005) Biochemistry , vol.44 , Issue.2 , pp. 775-781
    • Dempsey, C.E.1    Piggot, T.J.2    Mason, P.E.3
  • 25
    • 0032525133 scopus 로고    scopus 로고
    • Nine hydrophobic side chains are key determinants of the thermodynamic stability and oligomerization status of tumour suppressor p53 tetramerization domain
    • DOI 10.1093/emboj/17.10.2748
    • Mateu M. G., Fersht A. R., Nine hydrophobic side chains are key determinants of the thermodynamic stability and oligomerization status of tumour suppressor p53 tetramerization domain. The EMBO Journal 1998 17 10 2748 2758 2-s2.0-0032525133 10.1093/emboj/17.10.2748 (Pubitemid 28227121)
    • (1998) EMBO Journal , vol.17 , Issue.10 , pp. 2748-2758
    • Mateu, M.G.1    Fersht, A.R.2
  • 26
    • 67649634849 scopus 로고    scopus 로고
    • Defining the human deubiquitinating enzyme interaction landscape
    • 2-s2.0-67649634849 10.1016/j.cell.2009.04.042
    • Sowa M. E., Bennett E. J., Gygi S. P., Harper J. W., Defining the human deubiquitinating enzyme interaction landscape. Cell 2009 138 2 389 403 2-s2.0-67649634849 10.1016/j.cell.2009.04.042
    • (2009) Cell , vol.138 , Issue.2 , pp. 389-403
    • Sowa, M.E.1    Bennett, E.J.2    Gygi, S.P.3    Harper, J.W.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.