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Volumn 22, Issue 3, 2015, Pages 387-397

Structural and functional consequences of succinate dehydrogenase subunit B mutations

Author keywords

Functional consequences; Paraganglioma; Phaeochromocytoma; SDHB; Succinate dehydrogenase

Indexed keywords

MITOCHONDRIAL PROTEIN; REACTIVE OXYGEN METABOLITE; SUCCINATE DEHYDROGENASE; SUCCINATE DEHYDROGENASE SUBUNIT B; UNCLASSIFIED DRUG; SDHB PROTEIN, HUMAN;

EID: 84937038780     PISSN: 13510088     EISSN: 14796821     Source Type: Journal    
DOI: 10.1530/ERC-15-0099     Document Type: Article
Times cited : (22)

References (48)
  • 3
    • 84862814774 scopus 로고    scopus 로고
    • Exploring biological electron transfer pathway dynamics with the Pathways plugin for VMD
    • Balabin IA, Hu X & Beratan DN 2012 Exploring biological electron transfer pathway dynamics with the Pathways plugin for VMD. Journal of Computational Chemistry 33 906-910. (doi:10.1002/jcc.22927)
    • (2012) Journal of Computational Chemistry , vol.33 , pp. 906-910
    • Balabin, I.A.1    Hu, X.2    Beratan, D.N.3
  • 5
    • 29144484161 scopus 로고    scopus 로고
    • The SDH mutation database: An online resource for succinate dehydrogenase sequence variants involved in pheochromocytoma, paraganglioma and mitochondrial complex II deficiency
    • Bayley J, Devilee P & Taschner PE 2005 The SDH mutation database: an online resource for succinate dehydrogenase sequence variants involved in pheochromocytoma, paraganglioma and mitochondrial complex II deficiency.BMCMedicalGenetics 639-45. (doi:10.1186/1471-2350-6-39)
    • (2005) BMCMedicalGenetics , pp. 639-645
    • Bayley, J.1    Devilee, P.2    Taschner, P.E.3
  • 7
    • 0026434593 scopus 로고
    • Protein electron transfer rates set by the bridging secondary and tertiary structure
    • Beratan DN, Betts JN & Onuchic JN 1991 Protein electron transfer rates set by the bridging secondary and tertiary structure. Science 252 1285-1288. (doi:10.1126/science.1656523)
    • (1991) Science , vol.252 , pp. 1285-1288
    • Beratan, D.N.1    Betts, J.N.2    Onuchic, J.N.3
  • 10
    • 84894556457 scopus 로고    scopus 로고
    • Pheochromocytoma and paraganglioma pathogenesis: Learning from genetic heterogeneity
    • Dahia PL 2014 Pheochromocytoma and paraganglioma pathogenesis: learning from genetic heterogeneity. Nature Reviews. Cancer 14 108-119. (doi:10.1038/nrc3648)
    • (2014) Nature Reviews. Cancer , vol.14 , pp. 108-119
    • Dahia, P.L.1
  • 13
    • 50149097983 scopus 로고    scopus 로고
    • Hypoxia, HIF1 and glucose metabolism in the solid tumour
    • Denko NC 2008 Hypoxia, HIF1 and glucose metabolism in the solid tumour. Nature Reviews. Cancer 8 705-713. (doi:10.1038/nrc2468)
    • (2008) Nature Reviews. Cancer , vol.8 , pp. 705-713
    • Denko, N.C.1
  • 19
    • 0035213138 scopus 로고    scopus 로고
    • The R22X mutation of the SDHD gene in hereditary paraganglioma abolishes the enzymatic activity of complex II in the mitochondrial respiratory chain and activates the hypoxia pathway
    • Gimenez-Roqueplo AP, Favier J, Rustin P, Mourad J, Plouin P, Corvol P, Rotig A & Jeunemaitre X 2001 The R22X mutation of the SDHD gene in hereditary paraganglioma abolishes the enzymatic activity of complex II in the mitochondrial respiratory chain and activates the hypoxia pathway. American Journal of Human Genetics 69 1186-1197. (doi:10.1086/324413)
    • (2001) American Journal of Human Genetics , vol.69 , pp. 1186-1197
    • Gimenez-Roqueplo, A.P.1    Favier, J.2    Rustin, P.3    Mourad, J.4    Plouin, P.5    Corvol, P.6    Rotig, A.7    Jeunemaitre, X.8
  • 21
    • 84860834761 scopus 로고    scopus 로고
    • An update on the genetics of paraganglioma, pheochromocytoma, and associated hereditary syndromes
    • Gimenez-Roqueplo AP, Dahia PL & Robledo M 2012 An update on the genetics of paraganglioma, pheochromocytoma, and associated hereditary syndromes. Hormone and Metabolic Research 44 328-333. (doi:10.1055/s-0031-1301302)
    • (2012) Hormone and Metabolic Research , vol.44 , pp. 328-333
    • Gimenez-Roqueplo, A.P.1    Dahia, P.L.2    Robledo, M.3
  • 22
    • 65449185779 scopus 로고    scopus 로고
    • Functional study in a yeast model of a novel succinate dehydrogenase subunit B gene germline missense mutation (C191Y) diagnosed in a patient affected by a glomus tumor
    • Goffrini P, Ercolino T, Panizza E, GiachèV, Cavone L, Chiarugi A, Dima V, Ferror I & MannelliM2009 Functional study in a yeast model of a novel succinate dehydrogenase subunit B gene germline missense mutation (C191Y) diagnosed in a patient affected by a glomus tumor. Human Molecular Genetics 18 1860-1868. (doi:10.1093/hmg/ddp102)
    • (2009) Human Molecular Genetics , vol.18 , pp. 1860-1868
    • Goffrini, P.1    Ercolino, T.2    Panizza, E.3    Giachè, V.4    Cavone, L.5    Chiarugi, A.6    Dima, V.7    Ferror, I.8    Mannelli, M.9
  • 27
    • 84903774921 scopus 로고    scopus 로고
    • HIF signaling pathway in pheochromocytoma and other neuroendocrine tumors
    • Jochmanová I, Zelinka T, Widimský J & Pacak K 2014 HIF signaling pathway in pheochromocytoma and other neuroendocrine tumors. Physiological Research 63 S251-S262.
    • (2014) Physiological Research , vol.63 , pp. S251-S262
    • Jochmanová, I.1    Zelinka, T.2    Widimský, J.3    Pacak, K.4
  • 29
    • 84895748764 scopus 로고    scopus 로고
    • The lure of a LYR: The logistics of iron sulfur cluster delivery
    • Lane DJ, Merlot AM & Richardson DR 2014 The lure of a LYR: the logistics of iron sulfur cluster delivery. Cell Metabolism 19 348-350. (doi:10.1016/j.cmet.2014.02.011)
    • (2014) Cell Metabolism , vol.19 , pp. 348-350
    • Lane, D.J.1    Merlot, A.M.2    Richardson, D.R.3
  • 31
    • 36849056626 scopus 로고    scopus 로고
    • High frequency of germline succinate dehydrogenase mutations in sporadic cervical paragangliomas in northern Spain: Mitochondrial succinate dehydrogenase structure-function relationships and clinical-pathological correlations
    • Lima J, Feijao T, Ferreira da Silva A, Pereira-Castro I, Fernandez-Ballester G, Máximo V & Garcia-Rostan G 2007 High frequency of germline succinate dehydrogenase mutations in sporadic cervical paragangliomas in northern Spain: mitochondrial succinate dehydrogenase structure-function relationships and clinical-pathological correlations. Journal of Clinical Endocrinology and Metabolism 92 4853-4864. (doi:10.1210/jc.2007-0640)
    • (2007) Journal of Clinical Endocrinology and Metabolism , vol.92 , pp. 4853-4864
    • Lima, J.1    Feijao, T.2    Ferreira Da Silva, A.3    Pereira-Castro, I.4    Fernandez-Ballester, G.5    Máximo, V.6    Garcia-Rostan, G.7
  • 33
    • 84895735383 scopus 로고    scopus 로고
    • Cochaperone binding to LYR motifs confers specificity of iron sulfur cluster delivery
    • Maio N, Singh A, Uhrigshardt H, Saxena N, Tong WH & Rouault TA 2014 Cochaperone binding to LYR motifs confers specificity of iron sulfur cluster delivery. Cell Metabolism 19 445-457. (doi:10.1016/j.cmet.2014.01.015)
    • (2014) Cell Metabolism , vol.19 , pp. 445-457
    • Maio, N.1    Singh, A.2    Uhrigshardt, H.3    Saxena, N.4    Tong, W.H.5    Rouault, T.A.6
  • 34
    • 0028304962 scopus 로고
    • Satisfying hydrogen bonding potential in proteins
    • McDonald IK & Thornton JM 1994 Satisfying hydrogen bonding potential in proteins. Journal of Molecular Biology 238 777-793. (doi:10.1006/jmbi.1994.1334)
    • (1994) Journal of Molecular Biology , vol.238 , pp. 777-793
    • McDonald, I.K.1    Thornton, J.M.2
  • 35
    • 84905860097 scopus 로고    scopus 로고
    • The LYR factors SDHAF1 and SDHAF3 mediate maturation of the iron-sulfur subunit of succinate dehydrogenase
    • Na U, Yu W, Cox J, Bricker DK, Brockmann K, Rutter J, Thummel CS & Winge DR 2014 The LYR factors SDHAF1 and SDHAF3 mediate maturation of the iron-sulfur subunit of succinate dehydrogenase. Cell Metabolism 20 253-266. (doi:10.1016/j.cmet.2014.05.014)
    • (2014) Cell Metabolism , vol.20 , pp. 253-266
    • Na, U.1    Yu, W.2    Cox, J.3    Bricker, D.K.4    Brockmann, K.5    Rutter, J.6    Thummel, C.S.7    Winge, D.R.8
  • 36
    • 0035026704 scopus 로고    scopus 로고
    • Predicting deleterious amino acid substitutions
    • Ng PC & Henikoff S 2001 Predicting deleterious amino acid substitutions. Genome Research 11 863-874. (doi:10.1101/gr.176601)
    • (2001) Genome Research , vol.11 , pp. 863-874
    • Ng, P.C.1    Henikoff, S.2
  • 38
    • 84937029527 scopus 로고    scopus 로고
    • Generalized portrait of cancer metabolic pathways inferred froma list of genes overexpressed in cancer
    • 646193
    • Poliakov E, Managadze D & Rogozin I 2014 Generalized portrait of cancer metabolic pathways inferred froma list of genes overexpressed in cancer. Genetics Research International 646193 1-8. (doi:10.1155/2014/646193)
    • (2014) Genetics Research International , pp. 1-8
    • Poliakov, E.1    Managadze, D.2    Rogozin, I.3
  • 39
    • 84907646316 scopus 로고    scopus 로고
    • Krebs cycle metabolite profiling for identification and stratification of pheochromocytomas/paragangliomas due to succinate dehydrogenase deficiency
    • Richter S, PeitzschM, Rapizzi E, Lenders J, Qin N, de Cubas A & Eisenhofer G 2014 Krebs cycle metabolite profiling for identification and stratification of pheochromocytomas/paragangliomas due to succinate dehydrogenase deficiency. Journal of Clinical Endocrinology and Metabolism 99 3903-3911. (doi:10.1210/jc.2014-2151)
    • (2014) Journal of Clinical Endocrinology and Metabolism , vol.99 , pp. 3903-3911
    • Richter, S.1    Peitzsch, M.2    Rapizzi, E.3    Lenders, J.4    Qin, N.5    De Cubas, A.6    Eisenhofer, G.7
  • 40
    • 0027136282 scopus 로고
    • Comparative protein modelling by satisfaction of spatial restraints
    • Šali A & Blundell TL 1993 Comparative protein modelling by satisfaction of spatial restraints. Journal of Molecular Biology 234 779-815. (doi:10.1006/jmbi.1993.1626)
    • (1993) Journal of Molecular Biology , vol.234 , pp. 779-815
    • Šali, A.1    Blundell, T.L.2
  • 43
    • 21244503033 scopus 로고    scopus 로고
    • Crystal structure of mitochondrial respiratory membrane protein complex II
    • Sun F, Huo X, Zhai Y, Wang A, Xu J, Su D, Bartlam M & Rao Z 2005 Crystal structure of mitochondrial respiratory membrane protein complex II. Cell 121 1043-1057. (doi:10.1016/j.cell.2005.05.025)
    • (2005) Cell , vol.121 , pp. 1043-1057
    • Sun, F.1    Huo, X.2    Zhai, Y.3    Wang, A.4    Xu, J.5    Su, D.6    Bartlam, M.7    Rao, Z.8
  • 45
    • 84903610916 scopus 로고    scopus 로고
    • Current views on cell metabolism in SDHx-related pheochromocytoma and paraganglioma
    • Vicha A, Taieb D & Pacak K 2014 Current views on cell metabolism in SDHx-related pheochromocytoma and paraganglioma. Endocrine-Related Cancer 21 261-277. (doi:10.1530/ERC-13-0398)
    • (2014) Endocrine-Related Cancer , vol.21 , pp. 261-277
    • Vicha, A.1    Taieb, D.2    Pacak, K.3
  • 46
    • 0028922586 scopus 로고
    • LIGPLOT: A program to generate schematic diagrams of protein-ligand interactions
    • Wallace AC, Laskowski RA & Thornton JM 1995 LIGPLOT: a program to generate schematic diagrams of protein-ligand interactions. Protein Engineering, Design & Selection 8 127-134. (doi:10.1093/protein/8.2.127)
    • (1995) Protein Engineering, Design & Selection , vol.8 , pp. 127-134
    • Wallace, A.C.1    Laskowski, R.A.2    Thornton, J.M.3
  • 47
    • 0025225686 scopus 로고
    • Site-directed mutagenesis of conserved cysteine residues in Escherichia coli fumarate reductase: Modification of the spectroscopic and electrochemical properties of the [2Fe-2S] cluster
    • Werth MT, Cecchini G, Manodori A, Ackrell BA, Schröder I, Gunsalus RP & Johnson MK 1990 Site-directed mutagenesis of conserved cysteine residues in Escherichia coli fumarate reductase: modification of the spectroscopic and electrochemical properties of the [2Fe-2S] cluster. PNAS 87 8965-8969. (doi:10.1073/pnas.87.22.8965)
    • (1990) PNAS , vol.87 , pp. 8965-8969
    • Werth, M.T.1    Cecchini, G.2    Manodori, A.3    Ackrell, B.A.4    Schröder, I.5    Gunsalus, R.P.6    Johnson, M.K.7
  • 48
    • 84868298330 scopus 로고    scopus 로고
    • Missense mutations in the human SDHB gene increase protein degradation without altering intrinsic enzymatic function
    • YangC, Matro JC, HuntoonKM, Donald YY, Huynh YT, Fliedner SM, Breza J, Zhuang Z & Pacak K 2012 Missense mutations in the human SDHB gene increase protein degradation without altering intrinsic enzymatic function. FASEB Journal 26 4506-4516. (doi:10.1096/fj.12-210146)
    • (2012) FASEB Journal , vol.26 , pp. 4506-4516
    • Yang, C.1    Matro, J.C.2    Huntoon, K.M.3    Donald, Y.Y.4    Huynh, Y.T.5    Fliedner, S.M.6    Breza, J.7    Zhuang, Z.8    Pacak, K.9


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