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Volumn 11, Issue , 2011, Pages

Computational analysis of a novel mutation in ETFDH gene highlights its long-range effects on the FAD-binding motif

Author keywords

[No Author keywords available]

Indexed keywords

ELECTRON TRANSFER FLAVOPROTEIN DEHYDROGENASE; FLAVINE ADENINE NUCLEOTIDE; OXIDOREDUCTASE; UBIQUINONE DERIVATIVE; UBIQUINONE OXIDOREDUCTASE; UNCLASSIFIED DRUG; ELECTRON TRANSFERRING FLAVOPROTEIN; ELECTRON TRANSFERRING FLAVOPROTEIN DEHYDROGENASE; ELECTRON-TRANSFERRING-FLAVOPROTEIN DEHYDROGENASE; IRON SULFUR PROTEIN;

EID: 80054735129     PISSN: None     EISSN: 14726807     Source Type: Journal    
DOI: 10.1186/1472-6807-11-43     Document Type: Article
Times cited : (30)

References (51)
  • 1
    • 0003013226 scopus 로고    scopus 로고
    • Defects of electron transfer flavoprotein and electron transfer flavoprotein-ubiquinone oxidoreductase: Glutaric aciduria type II
    • New York: McGraw-Hill Scriver CR, Beaudet AL, Sly WS, Valle D, Childs B, Kinzler KW, Vogelstein B 8
    • Defects of electron transfer flavoprotein and electron transfer flavoprotein-ubiquinone oxidoreductase: glutaric aciduria type II. Frerman FE, Goodman SI, The metabolic and molecular bases of inherited disease New York: McGraw-Hill, Scriver CR, Beaudet AL, Sly WS, Valle D, Childs B, Kinzler KW, Vogelstein B, 8 2001 2357 2365
    • (2001) The Metabolic and Molecular Bases of Inherited Disease , pp. 2357-2365
    • Frerman, F.E.1    Goodman, S.I.2
  • 3
    • 0027400923 scopus 로고
    • Multiple acyl-coenzyme A dehydrogenation disorder responsive to riboflavin - Substrate oxidation, flavin metabolism, and flavoenzyme activities in fibroblasts
    • 10.1203/00006450-199302000-00008 8433888
    • Multiple acyl-coenzyme A dehydrogenation disorder responsive to riboflavin-substrate oxidation, flavin metabolism, and flavoenzyme activities in fibroblasts. Rhead W, Roettger V, Marshall T, Amendt B, Pediatric Research 1993 33 2 129 135 10.1203/00006450-199302000-00008 8433888
    • (1993) Pediatric Research , vol.33 , Issue.2 , pp. 129-135
    • Rhead, W.1    Roettger, V.2    Marshall, T.3    Amendt, B.4
  • 6
    • 77950458698 scopus 로고    scopus 로고
    • High resolution melting analysis facilitates mutation screening of ETFDH gene: Applications in riboflavin-responsive multiple acyl-CoA dehydrogenase deficiency
    • 10.1016/j.cca.2010.01.033
    • High resolution melting analysis facilitates mutation screening of ETFDH gene: Applications in riboflavin-responsive multiple acyl-CoA dehydrogenase deficiency. Er TK, Liang WC, Chang JG, Jong YJ, Clinica Chimica Acta 2010 411 9-10 690 699 10.1016/j.cca.2010.01.033
    • (2010) Clinica Chimica Acta , vol.411 , Issue.9-10 , pp. 690-699
    • Er, T.K.1    Liang, W.C.2    Chang, J.G.3    Jong, Y.J.4
  • 7
    • 79959965427 scopus 로고    scopus 로고
    • Molecular analysis of 51 unrelated pedigrees with late-onset multiple acyl-CoA dehydrogenation deficiency (MADD) in southern China confirmed the most common ETFDH mutation and high carrier frequency of c.250G > A
    • 10.1007/s00109-011-0725-7 21347544
    • Molecular analysis of 51 unrelated pedigrees with late-onset multiple acyl-CoA dehydrogenation deficiency (MADD) in southern China confirmed the most common ETFDH mutation and high carrier frequency of c.250G > A. Wang ZQ, Chen XJ, Murong SX, Wang N, Wu ZY, Journal of Molecular Medicine 2011 89 569 576 10.1007/s00109-011-0725-7 21347544
    • (2011) Journal of Molecular Medicine , vol.89 , pp. 569-576
    • Wang, Z.Q.1    Chen, X.J.2    Murong, S.X.3    Wang, N.4    Wu, Z.Y.5
  • 8
    • 61849090857 scopus 로고    scopus 로고
    • ETFDH mutations, CoQ(10) levels, and respiratory chain activities in patients with riboflavin-responsive multiple acyl-CoA dehydrogenase deficiency
    • 10.1016/j.nmd.2009.01.008 19249206
    • ETFDH mutations, CoQ(10) levels, and respiratory chain activities in patients with riboflavin-responsive multiple acyl-CoA dehydrogenase deficiency. Liang WC, Ohkuma A, Hayashi YK, Lopez LC, Hirano M, Nonaka I, Noguchi S, Chen LH, Jong YJ, Nishino I, Neuromuscular Disorders 2009 19 3 212 216 10.1016/j.nmd.2009.01.008 19249206
    • (2009) Neuromuscular Disorders , vol.19 , Issue.3 , pp. 212-216
    • Liang, W.C.1    Ohkuma, A.2    Hayashi, Y.K.3    Lopez, L.C.4    Hirano, M.5    Nonaka, I.6    Noguchi, S.7    Chen, L.H.8    Jong, Y.J.9    Nishino, I.10
  • 10
    • 78149263592 scopus 로고    scopus 로고
    • High frequency of ETFDH c.250G > A mutation in Taiwanese patients with late-onset lipid storage myopathy
    • 10.1111/j.1399-0004.2010.01421.x 20370797
    • High frequency of ETFDH c.250G > A mutation in Taiwanese patients with late-onset lipid storage myopathy. Lan MY, Fu MH, Liu YF, Huang CC, Chang YY, Liu JS, Peng CH, Chen SS, Clinical Genetics 2010 78 6 565 569 10.1111/j.1399-0004.2010.01421.x 20370797
    • (2010) Clinical Genetics , vol.78 , Issue.6 , pp. 565-569
    • Lan, M.Y.1    Fu, M.H.2    Liu, Y.F.3    Huang, C.C.4    Chang, Y.Y.5    Liu, J.S.6    Peng, C.H.7    Chen, S.S.8
  • 11
    • 67349122702 scopus 로고    scopus 로고
    • Novel mutations in ETFDH gene in Chinese patients with riboflavin-responsive multiple acyl-CoA dehydrogenase deficiency
    • 10.1016/j.cca.2009.02.015
    • Novel mutations in ETFDH gene in Chinese patients with riboflavin-responsive multiple acyl-CoA dehydrogenase deficiency. Law LK, Tang NLS, Hui J, Fung SLM, Ruiter J, Wanders RJA, Fok TF, Lam CWK, Clinica Chimica Acta 2009 404 2 95 99 10.1016/j.cca.2009.02.015
    • (2009) Clinica Chimica Acta , vol.404 , Issue.2 , pp. 95-99
    • Law, L.K.1    Tang, N.L.S.2    Hui, J.3    Fung, S.L.M.4    Ruiter, J.5    Wanders, R.J.A.6    Fok, T.F.7    Lam, C.W.K.8
  • 13
    • 63249105550 scopus 로고    scopus 로고
    • Role of Flavinylation in a Mild Variant of Multiple Acyl-CoA Dehydrogenation Deficiency A molecular rationale for the effects of riboflavin supplementation
    • 19088074
    • Role of Flavinylation in a Mild Variant of Multiple Acyl-CoA Dehydrogenation Deficiency A molecular rationale for the effects of riboflavin supplementation. Henriques BJ, Rodrigues JV, Olsen RK, Bross P, Gomes CM, Journal of Biological Chemistry 2009 284 7 4222 4229 19088074
    • (2009) Journal of Biological Chemistry , vol.284 , Issue.7 , pp. 4222-4229
    • Henriques, B.J.1    Rodrigues, J.V.2    Olsen, R.K.3    Bross, P.4    Gomes, C.M.5
  • 14
    • 0043122919 scopus 로고    scopus 로고
    • SIFT: Predicting amino acid changes that affect protein function
    • 10.1093/nar/gkg509 12824425
    • SIFT: predicting amino acid changes that affect protein function. Ng PC, Henikoff S, Nucleic Acids Research 2003 31 13 3812 3814 10.1093/nar/gkg509 12824425
    • (2003) Nucleic Acids Research , vol.31 , Issue.13 , pp. 3812-3814
    • Ng, P.C.1    Henikoff, S.2
  • 15
    • 68149165614 scopus 로고    scopus 로고
    • Predicting the effects of coding non-synonymous variants on protein function using the SIFT algorithm
    • 19561590
    • Predicting the effects of coding non-synonymous variants on protein function using the SIFT algorithm. Kumar P, Henikoff S, Ng PC, Nature Protocols 2009 4 7 1073 1082 19561590
    • (2009) Nature Protocols , vol.4 , Issue.7 , pp. 1073-1082
    • Kumar, P.1    Henikoff, S.2    Ng, P.C.3
  • 16
    • 80655144006 scopus 로고    scopus 로고
    • SIFT. http://sift.bii.a-star.edu.sg/
    • SIFT
  • 17
    • 33747825121 scopus 로고    scopus 로고
    • 2: Protein structure prediction server
    • 10.1093/nar/gkl187 16844981
    • 2: protein structure prediction server. Chen CC, Hwang JK, Yang JM, Nucleic Acids Research 2006 34 152 W157 10.1093/nar/gkl187 16844981
    • (2006) Nucleic Acids Research , vol.34
    • Chen, C.C.1    Hwang, J.K.2    Yang, J.M.3
  • 18
    • 70749119427 scopus 로고    scopus 로고
    • 2-v2: Template-based protein structure prediction server
    • 10.1186/1471-2105-10-366 19878598
    • 2-v2: template-based protein structure prediction server. Chen CC, Hwang JK, Yang JM, BMC Bioinformatics 2009 10 366 10.1186/1471-2105-10- 366 19878598
    • (2009) BMC Bioinformatics , vol.10 , pp. 366
    • Chen, C.C.1    Hwang, J.K.2    Yang, J.M.3
  • 20
    • 0038438514 scopus 로고    scopus 로고
    • IMPALA: Matching a protein sequence against a collection of PSI-BLAST-constructed position-specific score matrices
    • 10.1093/bioinformatics/15.12.1000 10745990
    • IMPALA: matching a protein sequence against a collection of PSI-BLAST-constructed position-specific score matrices. Schaffer AA, Wolf YI, Ponting CP, Koonin EV, Aravind L, Altschul SF, Bioinformatics 1999 15 12 1000 1011 10.1093/bioinformatics/15.12.1000 10745990
    • (1999) Bioinformatics , vol.15 , Issue.12 , pp. 1000-1011
    • Schaffer, A.A.1    Wolf, Y.I.2    Ponting, C.P.3    Koonin, E.V.4    Aravind, L.5    Altschul, S.F.6
  • 21
    • 0034623005 scopus 로고    scopus 로고
    • T-Coffee: A novel method for fast and accurate multiple sequence alignment
    • 10.1006/jmbi.2000.4042 10964570
    • T-Coffee: A novel method for fast and accurate multiple sequence alignment. Notredame C, Higgins DG, Heringa J, J Mol Biol 2000 302 1 205 217 10.1006/jmbi.2000.4042 10964570
    • (2000) J Mol Biol , vol.302 , Issue.1 , pp. 205-217
    • Notredame, C.1    Higgins, D.G.2    Heringa, J.3
  • 22
    • 33750814320 scopus 로고    scopus 로고
    • Structure of electron transfer flavoprotein-ubiquinone oxidoreductase and electron transfer to the mitochondrial ubiquinone pool
    • 10.1073/pnas.0604567103 17050691
    • Structure of electron transfer flavoprotein-ubiquinone oxidoreductase and electron transfer to the mitochondrial ubiquinone pool. Zhang J, Frerman FE, Kim JJP, Proceedings of the National Academy of Sciences of the United States of America 2006 103 44 16212 16217 10.1073/pnas.0604567103 17050691
    • (2006) Proceedings of the National Academy of Sciences of the United States of America , vol.103 , Issue.44 , pp. 16212-16217
    • Zhang, J.1    Frerman, F.E.2    Kim, J.J.P.3
  • 23
  • 25
    • 0037131229 scopus 로고    scopus 로고
    • FAD is a preferred substrate and an inhibitor of Escherichia coli general NAD(P)H: Flavin oxidoreductase
    • 10.1074/jbc.M206339200 12177066
    • FAD is a preferred substrate and an inhibitor of Escherichia coli general NAD(P)H: flavin oxidoreductase. Louie TM, Yang H, Karnchanaphanurach P, Xie XS, Xun LY, Journal of Biological Chemistry 2002 277 42 39450 39455 10.1074/jbc.M206339200 12177066
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.42 , pp. 39450-39455
    • Louie, T.M.1    Yang, H.2    Karnchanaphanurach, P.3    Xie, X.S.4    Xun, L.Y.5
  • 26
    • 0000388705 scopus 로고    scopus 로고
    • LINCS: A linear constraint solver for molecular simulations
    • 10.1002/(SICI)1096-987X(199709)18:12<1463: AID-JCC4>3.0.CO;2-H
    • LINCS: A linear constraint solver for molecular simulations. Hess B, Bekker H, Berendsen HJC, Fraaije J, Journal of Computational Chemistry 1997 18 12 1463 1472 10.1002/(SICI)1096-987X(199709)18:12<1463::AID-JCC4>3.0.CO;2- H
    • (1997) Journal of Computational Chemistry , vol.18 , Issue.12 , pp. 1463-1472
    • Hess, B.1    Bekker, H.2    Berendsen, H.J.C.3    Fraaije, J.4
  • 27
    • 0033955909 scopus 로고    scopus 로고
    • Protein thermal stability: Insights from atomic displacement parameters (B values)
    • 10.1093/protein/13.1.9 10679524
    • Protein thermal stability: insights from atomic displacement parameters (B values). Parthasarathy S, Murthy MRN, Protein Engineering 2000 13 1 9 13 10.1093/protein/13.1.9 10679524
    • (2000) Protein Engineering , vol.13 , Issue.1 , pp. 9-13
    • Parthasarathy, S.1    Murthy, M.R.N.2
  • 29
    • 0022419152 scopus 로고
    • Protein normal-mode dynamics - Trypsin-inhibitor, crambin, ribonuclease and lysozyme
    • 10.1016/0022-2836(85)90230-X 2580101
    • Protein normal-mode dynamics-trypsin-inhibitor, crambin, ribonuclease and lysozyme. Levitt M, Sander C, Stern PS, J Mol Biol 1985 181 3 423 447 10.1016/0022-2836(85)90230-X 2580101
    • (1985) J Mol Biol , vol.181 , Issue.3 , pp. 423-447
    • Levitt, M.1    Sander, C.2    Stern, P.S.3
  • 30
    • 0026663419 scopus 로고
    • Normal mode refinement - Crystallographic refinement of protein dynamic structure. I. Theory and test by simulated diffraction data
    • 10.1016/0022-2836(92)90932-A 1593630
    • Normal mode refinement-crystallographic refinement of protein dynamic structure. I. Theory and test by simulated diffraction data. Kidera A, Go N, J Mol Biol 1992 225 2 457 475 10.1016/0022-2836(92)90932-A 1593630
    • (1992) J Mol Biol , vol.225 , Issue.2 , pp. 457-475
    • Kidera, A.1    Go, N.2
  • 31
    • 33745024278 scopus 로고    scopus 로고
    • Symmetry, form, and shape: Guiding principles for robustness in macromolecular machines
    • 10.1146/annurev.biophys.35.040405.102010 16689630
    • Symmetry, form, and shape: Guiding principles for robustness in macromolecular machines. Tama F, Brooks CL, Annual Review of Biophysics and Biomolecular Structure 2006 35 115 133 10.1146/annurev.biophys.35.040405.102010 16689630
    • (2006) Annual Review of Biophysics and Biomolecular Structure , vol.35 , pp. 115-133
    • Tama, F.1    Brooks, C.L.2
  • 32
    • 0032932341 scopus 로고    scopus 로고
    • Tertiary and quaternary conformational changes in aspartate transcarbamylase: A normal mode study
    • 10.1002/(SICI)1097-0134(19990101)34:1<96: AID-PROT8>3.0.CO;2-0
    • Tertiary and quaternary conformational changes in aspartate transcarbamylase: A normal mode study. Thomas A, Hinsen K, Field MJ, Perahia D, Proteins-Structure Function and Genetics 1999 34 1 96 112 10.1002/(SICI)1097- 0134(19990101)34:1<96::AID-PROT8>3.0.CO;2-0
    • (1999) Proteins-Structure Function and Genetics , vol.34 , Issue.1 , pp. 96-112
    • Thomas, A.1    Hinsen, K.2    Field, M.J.3    Perahia, D.4
  • 33
    • 33846189408 scopus 로고    scopus 로고
    • Interpreting correlated motions using normal mode analysis
    • 10.1016/j.str.2006.09.003 17098190
    • Interpreting correlated motions using normal mode analysis. Van Wynsberghe AW, Cui Q, Structure 2006 14 11 1647 1653 10.1016/j.str.2006.09.003 17098190
    • (2006) Structure , vol.14 , Issue.11 , pp. 1647-1653
    • Van Wynsberghe, A.W.1    Cui, Q.2
  • 34
    • 0017187837 scopus 로고
    • Exploring structural homology of proteins
    • 10.1016/0022-2836(76)90195-9 186608
    • Exploring structural homology of proteins. Rossmann MG, Argos P, J Mol Biol 1976 105 1 75 95 10.1016/0022-2836(76)90195-9 186608
    • (1976) J Mol Biol , vol.105 , Issue.1 , pp. 75-95
    • Rossmann, M.G.1    Argos, P.2
  • 35
    • 0015834475 scopus 로고
    • Comparison of super-secondary structures in proteins
    • 10.1016/0022-2836(73)90388-4 4737475
    • Comparison of super-secondary structures in proteins. Rao ST, Rosmann MG, J Mol Biol 1973 76 2 241 256 10.1016/0022-2836(73)90388-4 4737475
    • (1973) J Mol Biol , vol.76 , Issue.2 , pp. 241-256
    • Rao, S.T.1    Rosmann, M.G.2
  • 36
    • 0019443447 scopus 로고
    • The anatomy and taxonomy of protein structure
    • 7020376
    • The anatomy and taxonomy of protein structure. Richardson JS, Advances in Protein Chemistry 1981 34 167 339 7020376
    • (1981) Advances in Protein Chemistry , vol.34 , pp. 167-339
    • Richardson, J.S.1
  • 37
    • 0034854206 scopus 로고    scopus 로고
    • Sequence-structure analysis of FAD-containing proteins
    • 10.1110/ps.12801 11514662
    • Sequence-structure analysis of FAD-containing proteins. Dym O, Eisenberg D, Protein Science 2001 10 9 1712 1728 10.1110/ps.12801 11514662
    • (2001) Protein Science , vol.10 , Issue.9 , pp. 1712-1728
    • Dym, O.1    Eisenberg, D.2
  • 38
    • 0036396532 scopus 로고    scopus 로고
    • GXXXG and GXXXA motifs stabilize FAD and NAD(P)-binding Rossmann folds through C-alpha-H center dot center dot center dot O hydrogen bonds and van der Waals interactions
    • 10.1016/S0022-2836(02)00885-9 12368099
    • GXXXG and GXXXA motifs stabilize FAD and NAD(P)-binding Rossmann folds through C-alpha-H center dot center dot center dot O hydrogen bonds and van der Waals interactions. Kleiger G, Eisenberg D, J Mol Biol 2002 323 1 69 76 10.1016/S0022-2836(02)00885-9 12368099
    • (2002) J Mol Biol , vol.323 , Issue.1 , pp. 69-76
    • Kleiger, G.1    Eisenberg, D.2
  • 39
    • 0016345760 scopus 로고
    • Chemical and biological evolution of a nucleotide-binding protein
    • 10.1038/250194a0 4368490
    • Chemical and biological evolution of a nucleotide-binding protein. Rossmann MG, Moras D, Olsen KW, Nature 1974 250 194 199 10.1038/250194a0 4368490
    • (1974) Nature , vol.250 , pp. 194-199
    • Rossmann, M.G.1    Moras, D.2    Olsen, K.W.3
  • 40
    • 12944300317 scopus 로고
    • Binding of nucleotides by proteins
    • 10.1016/0959-440X(92)90178-A
    • Binding of nucleotides by proteins. Schulz GE, Current Opinion in Structural Biology 1992 2 61 67 10.1016/0959-440X(92)90178-A
    • (1992) Current Opinion in Structural Biology , vol.2 , pp. 61-67
    • Schulz, G.E.1
  • 41
    • 0016354103 scopus 로고
    • Topological comparison of adenyl kinase with other proteins
    • 10.1038/250142a0 4367212
    • Topological comparison of adenyl kinase with other proteins. Schulz GE, Schirmer RH, Nature 1974 250 142 144 10.1038/250142a0 4367212
    • (1974) Nature , vol.250 , pp. 142-144
    • Schulz, G.E.1    Schirmer, R.H.2
  • 42
    • 0020414542 scopus 로고
    • FAD-binding site of glutathione-reductase
    • 10.1016/0022-2836(82)90177-2 7175934
    • FAD-binding site of glutathione-reductase. Schulz GE, Schirmer RH, Pai EF, J Mol Biol 1982 160 2 287 308 10.1016/0022-2836(82)90177-2 7175934
    • (1982) J Mol Biol , vol.160 , Issue.2 , pp. 287-308
    • Schulz, G.E.1    Schirmer, R.H.2    Pai, E.F.3
  • 43
    • 0028919340 scopus 로고
    • Isoalloxazine ring of FAD is required for the formation of the core in the Hsp60-assisted folding of medium-chain acyl-CoA dehydrogenase subunit into the assembly competent conformation in mitochondria
    • 10.1074/jbc.270.4.1899 7829528
    • Isoalloxazine ring of FAD is required for the formation of the core in the Hsp60-assisted folding of medium-chain acyl-CoA dehydrogenase subunit into the assembly competent conformation in mitochondria. Saijo T, Tanaka K, Journal of Biological Chemistry 1995 270 4 1899 1907 10.1074/jbc.270.4.1899 7829528
    • (1995) Journal of Biological Chemistry , vol.270 , Issue.4 , pp. 1899-1907
    • Saijo, T.1    Tanaka, K.2
  • 44
    • 0026783268 scopus 로고
    • FAD-dependent regulation of transcription, translation, posttranslational processing, and post-processing stability of various mitochondrial acyl-CoA dehydrogenases and of electron-transfer flavoprotein and the site of holoenzyme formation
    • 1517228
    • FAD-dependent regulation of transcription, translation, posttranslational processing, and post-processing stability of various mitochondrial acyl-CoA dehydrogenases and of electron-transfer flavoprotein and the site of holoenzyme formation. Nagao M, Tanaka K, Journal of Biological Chemistry 1992 267 25 17925 17932 1517228
    • (1992) Journal of Biological Chemistry , vol.267 , Issue.25 , pp. 17925-17932
    • Nagao, M.1    Tanaka, K.2
  • 45
    • 33745222319 scopus 로고    scopus 로고
    • Folding of Desulfovibrio desulfuricans flavodoxin is accelerated by cofactor fly-casting
    • 10.1016/j.abb.2006.03.032 16730634
    • Folding of Desulfovibrio desulfuricans flavodoxin is accelerated by cofactor fly-casting. Muralidhara BK, Rathinakumar R, Wittung-Stafshede P, Archives of Biochemistry and Biophysics 2006 451 1 51 58 10.1016/j.abb.2006.03. 032 16730634
    • (2006) Archives of Biochemistry and Biophysics , vol.451 , Issue.1 , pp. 51-58
    • Muralidhara, B.K.1    Rathinakumar, R.2    Wittung-Stafshede, P.3
  • 46
    • 8244255920 scopus 로고    scopus 로고
    • The molecular basis of medium-chain acyl-CoA dehydrogenase (MCAD) deficiency in compound heterozygous patients: Is there correlation between genotype and phenotype?
    • 10.1093/hmg/6.5.695 9158144
    • The molecular basis of medium-chain acyl-CoA dehydrogenase (MCAD) deficiency in compound heterozygous patients: Is there correlation between genotype and phenotype? Andresen BS, Bross P, Udvari S, Kirk J, Gray G, Kmoch S, Chamoles N, Knudsen I, Winter V, Wilcken B, et al. Human Molecular Genetics 1997 6 5 695 707 10.1093/hmg/6.5.695 9158144
    • (1997) Human Molecular Genetics , vol.6 , Issue.5 , pp. 695-707
    • Andresen, B.S.1    Bross, P.2    Udvari, S.3    Kirk, J.4    Gray, G.5    Kmoch, S.6    Chamoles, N.7    Knudsen, I.8    Winter, V.9    Wilcken, B.10
  • 47
    • 46949109490 scopus 로고    scopus 로고
    • The ACADS gene variation spectrum in 114 patients with short-chain acyl-CoA dehydrogenase (SCAD) deficiency is dominated by missense variations leading to protein misfolding at the cellular level
    • 10.1007/s00439-008-0521-9 18523805
    • The ACADS gene variation spectrum in 114 patients with short-chain acyl-CoA dehydrogenase (SCAD) deficiency is dominated by missense variations leading to protein misfolding at the cellular level. Pedersen CB, Kolvraa S, Kolvraa A, Stenbroen V, Kjeldsen M, Ensenauer R, Tein I, Matern D, Rinaldo P, Vianey-Saban C, et al. Human Genetics 2008 124 1 43 56 10.1007/s00439-008-0521-9 18523805
    • (2008) Human Genetics , vol.124 , Issue.1 , pp. 43-56
    • Pedersen, C.B.1    Kolvraa, S.2    Kolvraa, A.3    Stenbroen, V.4    Kjeldsen, M.5    Ensenauer, R.6    Tein, I.7    Matern, D.8    Rinaldo, P.9    Vianey-Saban, C.10
  • 49
    • 0036396930 scopus 로고    scopus 로고
    • Glutaric acidemia type II: Gene structure and mutations of the electron transfer flavoprotein:ubiquinone oxidoreductase (ETF: QO) gene
    • 10.1016/S1096-7192(02)00138-5 12359134
    • Glutaric acidemia type II: gene structure and mutations of the electron transfer flavoprotein:ubiquinone oxidoreductase (ETF: QO) gene. Goodman SI, Binard RJ, Woontner MR, Frerman FE, Molecular Genetics and Metabolism 2002 77 1-2 86 90 10.1016/S1096-7192(02)00138-5 12359134
    • (2002) Molecular Genetics and Metabolism , vol.77 , Issue.1-2 , pp. 86-90
    • Goodman, S.I.1    Binard, R.J.2    Woontner, M.R.3    Frerman, F.E.4
  • 51
    • 80655131811 scopus 로고    scopus 로고
    • PyMOL. http://www.pymol.org/


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