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Volumn 134, Issue 4, 2015, Pages 405-421

Types and effects of protein variations

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID; PROTEIN VARIANT; PROTEIN;

EID: 84925520236     PISSN: 03406717     EISSN: 14321203     Source Type: Journal    
DOI: 10.1007/s00439-015-1529-6     Document Type: Article
Times cited : (28)

References (109)
  • 1
    • 0036280235 scopus 로고    scopus 로고
    • Bcr–Abl variants: biological and clinical aspects
    • COI: 1:CAS:528:DC%2BD38XksVShtL8%3D, PID: 12191565
    • Advani AS, Pendergast AM (2002) Bcr–Abl variants: biological and clinical aspects. Leuk Res 26:713–720.
    • (2002) Leuk Res , vol.26 , pp. 713-720
    • Advani, A.S.1    Pendergast, A.M.2
  • 3
    • 84858205858 scopus 로고    scopus 로고
    • Classification of mismatch repair gene missense variants with PON-MMR
    • COI: 1:CAS:528:DC%2BC38Xjs1ajsbw%3D, PID: 22290698
    • Ali H, Olatubosun A, Vihinen M (2012) Classification of mismatch repair gene missense variants with PON-MMR. Hum Mutat 33:642–650. doi:10.1002/humu.22038.
    • (2012) Hum Mutat , vol.33 , pp. 642-650
    • Ali, H.1    Olatubosun, A.2    Vihinen, M.3
  • 4
    • 84901984641 scopus 로고    scopus 로고
    • Performance of protein disorder prediction programs on amino acid substitutions
    • COI: 1:CAS:528:DC%2BC2cXpslKgsbk%3D, PID: 24753228
    • Ali H, Urolagin S, Gurarslan O, Vihinen M (2014) Performance of protein disorder prediction programs on amino acid substitutions. Hum Mutat 35:794–804. doi:10.1002/humu.22564.
    • (2014) Hum Mutat , vol.35 , pp. 794-804
    • Ali, H.1    Urolagin, S.2    Gurarslan, O.3    Vihinen, M.4
  • 5
    • 34547515589 scopus 로고    scopus 로고
    • Cryptic proteolytic activity of dihydrolipoamide dehydrogenase
    • COI: 1:CAS:528:DC%2BD2sXks1artbw%3D, PID: 17404228
    • Babady NE, Pang YP, Elpeleg O, Isaya G (2007) Cryptic proteolytic activity of dihydrolipoamide dehydrogenase. Proc Natl Acad Sci USA 104:6158–6163. doi:10.1073/pnas.0610618104.
    • (2007) Proc Natl Acad Sci USA , vol.104 , pp. 6158-6163
    • Babady, N.E.1    Pang, Y.P.2    Elpeleg, O.3    Isaya, G.4
  • 6
    • 0034610781 scopus 로고    scopus 로고
    • Crystal structure of the hereditary haemochromatosis protein HFE complexed with transferrin receptor
    • COI: 1:CAS:528:DC%2BD3cXlsl2hsw%3D%3D, PID: 10638746
    • Bennett MJ, Lebron JA, Bjorkman PJ (2000) Crystal structure of the hereditary haemochromatosis protein HFE complexed with transferrin receptor. Nature 403:46–53. doi:10.1038/47417.
    • (2000) Nature , vol.403 , pp. 46-53
    • Bennett, M.J.1    Lebron, J.A.2    Bjorkman, P.J.3
  • 7
    • 0034731382 scopus 로고    scopus 로고
    • Protein engineering of subtilisin
    • COI: 1:CAS:528:DC%2BD3MXitl2lsQ%3D%3D, PID: 11150607
    • Bryan PN (2000) Protein engineering of subtilisin. Biochim Biophys Acta 1543:203–222.
    • (2000) Biochim Biophys Acta , vol.1543 , pp. 203-222
    • Bryan, P.N.1
  • 8
    • 67749137351 scopus 로고    scopus 로고
    • Functional annotations improve the predictive score of human disease-related mutations in proteins
    • COI: 1:CAS:528:DC%2BD1MXhtVKrtrfM, PID: 19514061
    • Calabrese R, Capriotti E, Fariselli P, Martelli PL, Casadio R (2009) Functional annotations improve the predictive score of human disease-related mutations in proteins. Hum Mutat 30:1237–1244. doi:10.1002/humu.21047.
    • (2009) Hum Mutat , vol.30 , pp. 1237-1244
    • Calabrese, R.1    Capriotti, E.2    Fariselli, P.3    Martelli, P.L.4    Casadio, R.5
  • 9
    • 27544469800 scopus 로고    scopus 로고
    • Predicting protein stability changes from sequences using support vector machines
    • Capriotti E, Fariselli P, Calabrese R, Casadio R (2005) Predicting protein stability changes from sequences using support vector machines. Bioinformatics 21(Suppl 2):254–258. doi:10.1093/bioinformatics/bti1109.
    • (2005) Bioinformatics , vol.21 , pp. 254-258
    • Capriotti, E.1    Fariselli, P.2    Calabrese, R.3    Casadio, R.4
  • 10
    • 0030443398 scopus 로고    scopus 로고
    • Stability and folding of the SH3 domain of Bruton’s tyrosine kinase
    • COI: 1:CAS:528:DyaK2sXhvFOrsA%3D%3D, PID: 8990499
    • Chen YJ, Lin SC, Tzeng SR, Patel HV, Lyu PC, Cheng JW (1996) Stability and folding of the SH3 domain of Bruton’s tyrosine kinase. Proteins 26:465–471. doi:10.1002/(sici)1097-0134(199612)26:4<465:aid-prot7>3.0.co;2-a.
    • (1996) Proteins , vol.26 , pp. 465-471
    • Chen, Y.J.1    Lin, S.C.2    Tzeng, S.R.3    Patel, H.V.4    Lyu, P.C.5    Cheng, J.W.6
  • 11
    • 78149436073 scopus 로고    scopus 로고
    • Diverse effects on the native β-sheet of the human prion protein due to disease-associated mutations
    • COI: 1:CAS:528:DC%2BC3cXhtlalurrK, PID: 20949975
    • Chen W, van der Kamp MW, Daggett V (2010) Diverse effects on the native β-sheet of the human prion protein due to disease-associated mutations. Biochemistry 49:9874–9881. doi:10.1021/bi101449f.
    • (2010) Biochemistry , vol.49 , pp. 9874-9881
    • Chen, W.1    van der Kamp, M.W.2    Daggett, V.3
  • 12
    • 33644847172 scopus 로고    scopus 로고
    • Prediction of protein stability changes for single-site mutations using support vector machines
    • COI: 1:CAS:528:DC%2BD28XivVWnsrY%3D, PID: 16372356
    • Cheng J, Randall A, Baldi P (2006) Prediction of protein stability changes for single-site mutations using support vector machines. Proteins 62:1125–1132. doi:10.1002/prot.20810.
    • (2006) Proteins , vol.62 , pp. 1125-1132
    • Cheng, J.1    Randall, A.2    Baldi, P.3
  • 13
    • 0032708771 scopus 로고    scopus 로고
    • Mutational analysis of acylphosphatase suggests the importance of topology and contact order in protein folding
    • COI: 1:CAS:528:DyaK1MXnt1Grur0%3D, PID: 10542090
    • Chiti F, Taddei N, White PM, Bucciantini M, Magherini F, Stefani M, Dobson CM (1999) Mutational analysis of acylphosphatase suggests the importance of topology and contact order in protein folding. Nat Struct Biol 6:1005–1009. doi:10.1038/14890.
    • (1999) Nat Struct Biol , vol.6 , pp. 1005-1009
    • Chiti, F.1    Taddei, N.2    White, P.M.3    Bucciantini, M.4    Magherini, F.5    Stefani, M.6    Dobson, C.M.7
  • 14
    • 33947517558 scopus 로고    scopus 로고
    • AGGRESCAN: a server for the prediction and evaluation of “hot spots” of aggregation in polypeptides
    • Conchillo-Sole O, de Groot NS, Aviles FX, Vendrell J, Daura X, Ventura S (2007) AGGRESCAN: a server for the prediction and evaluation of “hot spots” of aggregation in polypeptides. BMC Bioinform 8:65. doi:10.1186/1471-2105-8-65.
    • (2007) BMC Bioinform , vol.8 , pp. 65
    • Conchillo-Sole, O.1    de Groot, N.S.2    Aviles, F.X.3    Vendrell, J.4    Daura, X.5    Ventura, S.6
  • 16
    • 84878402423 scopus 로고    scopus 로고
    • Conformational defects underlie proteasomal degradation of Dent’s disease-causing mutants of ClC-5
    • PID: 23566014
    • D’Antonio C, Molinski S, Ahmadi S, Huan LJ, Wellhauser L, Bear CE (2013) Conformational defects underlie proteasomal degradation of Dent’s disease-causing mutants of ClC-5. Biochem J 452:391–400. doi:10.1042/bj20121848.
    • (2013) Biochem J , vol.452 , pp. 391-400
    • D’Antonio, C.1    Molinski, S.2    Ahmadi, S.3    Huan, L.J.4    Wellhauser, L.5    Bear, C.E.6
  • 17
    • 84892739749 scopus 로고    scopus 로고
    • Amino acid changes in disease-associated variants differ radically from variants observed in the 1000 genomes project dataset
    • PID: 24348229
    • de Beer TA, Laskowski RA, Parks SL, Sipos B, Goldman N, Thornton JM (2013) Amino acid changes in disease-associated variants differ radically from variants observed in the 1000 genomes project dataset. PLoS Comput Biol 9:e1003382. doi:10.1371/journal.pcbi.1003382.
    • (2013) PLoS Comput Biol , vol.9 , pp. e1003382
    • de Beer, T.A.1    Laskowski, R.A.2    Parks, S.L.3    Sipos, B.4    Goldman, N.5    Thornton, J.M.6
  • 18
    • 0034908554 scopus 로고    scopus 로고
    • Nomenclature for the description of human sequence variations
    • den Dunnen JT, Antonarakis SE (2001) Nomenclature for the description of human sequence variations. Hum Genet 109:121–124.
    • (2001) Hum Genet , vol.109 , pp. 121-124
    • den Dunnen, J.T.1    Antonarakis, S.E.2
  • 20
    • 33845227579 scopus 로고    scopus 로고
    • Effects of the single point genetic mutation D54G on muscle creatine kinase activity, structure and stability
    • COI: 1:CAS:528:DC%2BD28Xht12ktLvE, PID: 17030001
    • Feng S, Zhao TJ, Zhou HM, Yan YB (2007) Effects of the single point genetic mutation D54G on muscle creatine kinase activity, structure and stability. Int J Biochem Cell Biol 39:392–401. doi:10.1016/j.biocel.2006.09.004.
    • (2007) Int J Biochem Cell Biol , vol.39 , pp. 392-401
    • Feng, S.1    Zhao, T.J.2    Zhou, H.M.3    Yan, Y.B.4
  • 21
    • 0036300807 scopus 로고    scopus 로고
    • Characterization of disease-associated single amino acid polymorphisms in terms of sequence and structure properties
    • COI: 1:CAS:528:DC%2BD38XntlKqtQ%3D%3D, PID: 11812146
    • Ferrer-Costa C, Orozco M, de la Cruz X (2002) Characterization of disease-associated single amino acid polymorphisms in terms of sequence and structure properties. J Mol Biol 315:771–786. doi:10.1006/jmbi.2001.5255.
    • (2002) J Mol Biol , vol.315 , pp. 771-786
    • Ferrer-Costa, C.1    Orozco, M.2    de la Cruz, X.3
  • 23
    • 79960904147 scopus 로고    scopus 로고
    • A novel proteolipid protein 1 gene mutation causing classical type Pelizaeus–Merzbacher disease
    • PID: 21177054
    • Fukumura S, Adachi N, Nagao M, Tsutsumi H (2011) A novel proteolipid protein 1 gene mutation causing classical type Pelizaeus–Merzbacher disease. Brain Dev 33:697–699. doi:10.1016/j.braindev.2010.11.010.
    • (2011) Brain Dev , vol.33 , pp. 697-699
    • Fukumura, S.1    Adachi, N.2    Nagao, M.3    Tsutsumi, H.4
  • 24
    • 84867747152 scopus 로고    scopus 로고
    • Current challenges in genome annotation through structural biology and bioinformatics
    • COI: 1:CAS:528:DC%2BC38XhtF2nsLbN, PID: 22884875
    • Furnham N, de Beer TA, Thornton JM (2012) Current challenges in genome annotation through structural biology and bioinformatics. Curr Opin Struct Biol 22:594–601. doi:10.1016/j.sbi.2012.07.005.
    • (2012) Curr Opin Struct Biol , vol.22 , pp. 594-601
    • Furnham, N.1    de Beer, T.A.2    Thornton, J.M.3
  • 25
    • 0034938535 scopus 로고    scopus 로고
    • Bruton’s tyrosine kinase is present in normal platelets and its absence identifies patients with X-linked agammaglobulinaemia and carrier females
    • COI: 1:CAS:528:DC%2BD3MXmtVyisrc%3D, PID: 11472359
    • Futatani T, Watanabe C, Baba Y, Tsukada S, Ochs HD (2001) Bruton’s tyrosine kinase is present in normal platelets and its absence identifies patients with X-linked agammaglobulinaemia and carrier females. Br J Haematol 114:141–149.
    • (2001) Br J Haematol , vol.114 , pp. 141-149
    • Futatani, T.1    Watanabe, C.2    Baba, Y.3    Tsukada, S.4    Ochs, H.D.5
  • 27
    • 84908504883 scopus 로고    scopus 로고
    • Protein engineering of the N-terminus of NEMO: structure stabilization and rescue of IKKβ binding
    • COI: 1:CAS:528:DC%2BC2cXhs1yju7bP, PID: 25286246
    • Guo B, Audu CO, Cochran JC, Mierke DF, Pellegrini M (2014) Protein engineering of the N-terminus of NEMO: structure stabilization and rescue of IKKβ binding. Biochemistry 53:6776–6785. doi:10.1021/bi500861x.
    • (2014) Biochemistry , vol.53 , pp. 6776-6785
    • Guo, B.1    Audu, C.O.2    Cochran, J.C.3    Mierke, D.F.4    Pellegrini, M.5
  • 29
    • 73249144328 scopus 로고    scopus 로고
    • Bothnia dystrophy is caused by domino-like rearrangements in cellular retinaldehyde-binding protein mutant R234W
    • COI: 1:CAS:528:DC%2BD1MXhsVKjtL%2FJ, PID: 19846785
    • He X, Lobsiger J, Stocker A (2009) Bothnia dystrophy is caused by domino-like rearrangements in cellular retinaldehyde-binding protein mutant R234W. Proc Natl Acad Sci USA 106:18545–18550. doi:10.1073/pnas.0907454106.
    • (2009) Proc Natl Acad Sci USA , vol.106 , pp. 18545-18550
    • He, X.1    Lobsiger, J.2    Stocker, A.3
  • 30
    • 0141853011 scopus 로고    scopus 로고
    • Genotype is an important determinant of phenotype in adenosine deaminase deficiency
    • COI: 1:CAS:528:DC%2BD3sXnt1Gqtb8%3D, PID: 14499267
    • Hershfield MS (2003) Genotype is an important determinant of phenotype in adenosine deaminase deficiency. Curr Opin Immunol 15:571–577.
    • (2003) Curr Opin Immunol , vol.15 , pp. 571-577
    • Hershfield, M.S.1
  • 32
    • 84888255102 scopus 로고    scopus 로고
    • wKinMut: an integrated tool for the analysis and interpretation of mutations in human protein kinases
    • Izarzugaza JM, Vazquez M, del Pozo A, Valencia A (2013) wKinMut: an integrated tool for the analysis and interpretation of mutations in human protein kinases. BMC Bioinform 14:345. doi:10.1186/1471-2105-14-345.
    • (2013) BMC Bioinform , vol.14 , pp. 345
    • Izarzugaza, J.M.1    Vazquez, M.2    del Pozo, A.3    Valencia, A.4
  • 33
    • 84868118712 scopus 로고    scopus 로고
    • Evidence of asymmetric cell division and centrosome inheritance in human neuroblastoma cells
    • COI: 1:CAS:528:DC%2BC38Xhsl2ktbbI, PID: 23064640
    • Izumi H, Kaneko Y (2012) Evidence of asymmetric cell division and centrosome inheritance in human neuroblastoma cells. Proc Natl Acad Sci USA 109:18048–18053. doi:10.1073/pnas.1205525109.
    • (2012) Proc Natl Acad Sci USA , vol.109 , pp. 18048-18053
    • Izumi, H.1    Kaneko, Y.2
  • 34
    • 10244243692 scopus 로고    scopus 로고
    • Mutations of the Wiskott–Aldrich Syndrome Protein (WASP): hotspots, effect on transcription, and translation and phenotype/genotype correlation
    • COI: 1:CAS:528:DC%2BD2cXhtFaju7jO, PID: 15284122
    • Jin Y, Mazza C, Christie JR, Giliani S, Fiorini M, Mella P, Gandellini F, Stewart DM, Zhu Q, Nelson DL, Notarangelo LD, Ochs HD (2004) Mutations of the Wiskott–Aldrich Syndrome Protein (WASP): hotspots, effect on transcription, and translation and phenotype/genotype correlation. Blood 104:4010–4019. doi:10.1182/blood-2003-05-1592.
    • (2004) Blood , vol.104 , pp. 4010-4019
    • Jin, Y.1    Mazza, C.2    Christie, J.R.3    Giliani, S.4    Fiorini, M.5    Mella, P.6    Gandellini, F.7    Stewart, D.M.8    Zhu, Q.9    Nelson, D.L.10    Notarangelo, L.D.11    Ochs, H.D.12
  • 35
    • 84856888538 scopus 로고    scopus 로고
    • Clinical phenotypes associated with type II collagen mutations
    • PID: 21332586
    • Kannu P, Bateman J, Savarirayan R (2012) Clinical phenotypes associated with type II collagen mutations. J Paediatr Child Health 48:E38–E43. doi:10.1111/j.1440-1754.2010.01979.x.
    • (2012) J Paediatr Child Health , vol.48 , pp. E38-E43
    • Kannu, P.1    Bateman, J.2    Savarirayan, R.3
  • 36
    • 34848835086 scopus 로고    scopus 로고
    • Spectrum of disease-causing mutations in protein secondary structures
    • PID: 17727703
    • Khan S, Vihinen M (2007) Spectrum of disease-causing mutations in protein secondary structures. BMC Struct Biol 7:56. doi:10.1186/1472-6807-7-56.
    • (2007) BMC Struct Biol , vol.7 , pp. 56
    • Khan, S.1    Vihinen, M.2
  • 37
    • 77952706843 scopus 로고    scopus 로고
    • Performance of protein stability predictors
    • COI: 1:CAS:528:DC%2BC3cXosl2lu70%3D, PID: 20232415
    • Khan S, Vihinen M (2010) Performance of protein stability predictors. Hum Mutat 31:675–684. doi:10.1002/humu.21242.
    • (2010) Hum Mutat , vol.31 , pp. 675-684
    • Khan, S.1    Vihinen, M.2
  • 38
    • 84895858942 scopus 로고    scopus 로고
    • A general framework for estimating the relative pathogenicity of human genetic variants
    • COI: 1:CAS:528:DC%2BC2cXhs1Sjt7g%3D, PID: 24487276
    • Kircher M, Witten DM, Jain P, O’Roak BJ, Cooper GM (2014) A general framework for estimating the relative pathogenicity of human genetic variants. Nat Genet 46:310–315. doi:10.1038/ng.2892.
    • (2014) Nat Genet , vol.46 , pp. 310-315
    • Kircher, M.1    Witten, D.M.2    Jain, P.3    O’Roak, B.J.4    Cooper, G.M.5
  • 39
    • 84901771117 scopus 로고    scopus 로고
    • Computational and experimental approaches to reveal the effects of single nucleotide polymorphisms with respect to disease diagnostics
    • COI: 1:CAS:528:DC%2BC2MXjtFymur4%3D, PID: 24886813
    • Kucukkal TG, Yang Y, Chapman SC, Cao W, Alexov E (2014) Computational and experimental approaches to reveal the effects of single nucleotide polymorphisms with respect to disease diagnostics. Int J Mol Sci 15:9670–9717. doi:10.3390/ijms15069670.
    • (2014) Int J Mol Sci , vol.15 , pp. 9670-9717
    • Kucukkal, T.G.1    Yang, Y.2    Chapman, S.C.3    Cao, W.4    Alexov, E.5
  • 40
    • 46449121011 scopus 로고    scopus 로고
    • Genome wide analysis of pathogenic SH2 domain mutations
    • COI: 1:CAS:528:DC%2BD1cXnvVWhtLk%3D, PID: 18260110
    • Lappalainen I, Thusberg J, Shen B, Vihinen M (2008) Genome wide analysis of pathogenic SH2 domain mutations. Proteins 72:779–792. doi:10.1002/prot.21970.
    • (2008) Proteins , vol.72 , pp. 779-792
    • Lappalainen, I.1    Thusberg, J.2    Shen, B.3    Vihinen, M.4
  • 42
    • 79954434760 scopus 로고    scopus 로고
    • PROlocalizer: integrated web service for protein subcellular localization prediction
    • COI: 1:CAS:528:DC%2BC3MXitFGqs7Y%3D, PID: 20811800
    • Laurila K, Vihinen M (2011) PROlocalizer: integrated web service for protein subcellular localization prediction. Amino Acids 40:975–980. doi:10.1007/s00726-010-0724-y.
    • (2011) Amino Acids , vol.40 , pp. 975-980
    • Laurila, K.1    Vihinen, M.2
  • 46
    • 70350671733 scopus 로고    scopus 로고
    • Automated inference of molecular mechanisms of disease from amino acid substitutions
    • COI: 1:CAS:528:DC%2BD1MXhtlWls7vL, PID: 19734154
    • Li B, Krishnan VG, Mort ME, Xin F, Kamati KK, Cooper DN, Mooney SD, Radivojac P (2009) Automated inference of molecular mechanisms of disease from amino acid substitutions. Bioinformatics 25:2744–2750. doi:10.1093/bioinformatics/btp528.
    • (2009) Bioinformatics , vol.25 , pp. 2744-2750
    • Li, B.1    Krishnan, V.G.2    Mort, M.E.3    Xin, F.4    Kamati, K.K.5    Cooper, D.N.6    Mooney, S.D.7    Radivojac, P.8
  • 47
    • 58149280217 scopus 로고    scopus 로고
    • Crystal structure of human adenylate kinase 4 (L171P) suggests the role of hinge region in protein domain motion
    • COI: 1:CAS:528:DC%2BD1MXosVSgtA%3D%3D, PID: 19073142
    • Liu R, Xu H, Wei Z, Wang Y, Lin Y, Gong W (2009) Crystal structure of human adenylate kinase 4 (L171P) suggests the role of hinge region in protein domain motion. Biochem Biophys Res Commun 379:92–97. doi:10.1016/j.bbrc.2008.12.012.
    • (2009) Biochem Biophys Res Commun , vol.379 , pp. 92-97
    • Liu, R.1    Xu, H.2    Wei, Z.3    Wang, Y.4    Lin, Y.5    Gong, W.6
  • 48
    • 77956912166 scopus 로고    scopus 로고
    • Disease variants of the human mitochondrial DNA helicase encoded by C10orf2 differentially alter protein stability, nucleotide hydrolysis, and helicase activity
    • COI: 1:CAS:528:DC%2BC3cXhtFKks7nE, PID: 20659899
    • Longley MJ, Humble MM, Sharief FS, Copeland WC (2010) Disease variants of the human mitochondrial DNA helicase encoded by C10orf2 differentially alter protein stability, nucleotide hydrolysis, and helicase activity. J Biol Chem 285:29690–29702. doi:10.1074/jbc.M110.151795.
    • (2010) J Biol Chem , vol.285 , pp. 29690-29702
    • Longley, M.J.1    Humble, M.M.2    Sharief, F.S.3    Copeland, W.C.4
  • 49
    • 84856729323 scopus 로고    scopus 로고
    • ClC-5 mutations associated with Dent’s disease: a major role of the dimer interface
    • COI: 1:CAS:528:DC%2BC38XpslylsQ%3D%3D, PID: 22083641
    • Lourdel S, Grand T, Burgos J, González W, Sepulveda FV, Teulon J (2012) ClC-5 mutations associated with Dent’s disease: a major role of the dimer interface. Pflugers Arch 463:247–256. doi:10.1007/s00424-011-1052-0.
    • (2012) Pflugers Arch , vol.463 , pp. 247-256
    • Lourdel, S.1    Grand, T.2    Burgos, J.3    González, W.4    Sepulveda, F.V.5    Teulon, J.6
  • 50
    • 70449356628 scopus 로고    scopus 로고
    • Missense mutations in the SH3TC2 protein causing Charcot–Marie–Tooth disease type 4C affect its localization in the plasma membrane and endocytic pathway
    • COI: 1:CAS:528:DC%2BD1MXhtlygs7jP, PID: 19744956
    • Lupo V, Galindo MI, Martinez-Rubio D, Sevilla T, Vilchez JJ, Palau F, Espinos C (2009) Missense mutations in the SH3TC2 protein causing Charcot–Marie–Tooth disease type 4C affect its localization in the plasma membrane and endocytic pathway. Hum Mol Genet 18:4603–4614. doi:10.1093/hmg/ddp427.
    • (2009) Hum Mol Genet , vol.18 , pp. 4603-4614
    • Lupo, V.1    Galindo, M.I.2    Martinez-Rubio, D.3    Sevilla, T.4    Vilchez, J.J.5    Palau, F.6    Espinos, C.7
  • 51
    • 0029087567 scopus 로고
    • Src family protein tyrosine kinases induce autoactivation of Bruton’s tyrosine kinase
    • COI: 1:CAS:528:DyaK2MXotlant74%3D, PID: 7565679
    • Mahajan S, Fargnoli J, Burkhardt AL, Kut SA, Saouaf SJ, Bolen JB (1995) Src family protein tyrosine kinases induce autoactivation of Bruton’s tyrosine kinase. Mol Cell Biol 15:5304–5311.
    • (1995) Mol Cell Biol , vol.15 , pp. 5304-5311
    • Mahajan, S.1    Fargnoli, J.2    Burkhardt, A.L.3    Kut, S.A.4    Saouaf, S.J.5    Bolen, J.B.6
  • 52
    • 0035798646 scopus 로고    scopus 로고
    • Crystal structure of Bruton’s tyrosine kinase domain suggests a novel pathway for activation and provides insights into the molecular basis of X-linked agammaglobulinemia
    • COI: 1:CAS:528:DC%2BD3MXosVKgtLc%3D, PID: 11527964
    • Mao C, Zhou M, Uckun FM (2001) Crystal structure of Bruton’s tyrosine kinase domain suggests a novel pathway for activation and provides insights into the molecular basis of X-linked agammaglobulinemia. J Biol Chem 276:41435–41443. doi:10.1074/jbc.M104828200.
    • (2001) J Biol Chem , vol.276 , pp. 41435-41443
    • Mao, C.1    Zhou, M.2    Uckun, F.M.3
  • 54
    • 0034655206 scopus 로고    scopus 로고
    • Six X-linked agammaglobulinemia-causing missense mutations in the Src homology 2 domain of Bruton’s tyrosine kinase: phosphotyrosine-binding and circular dichroism analysis
    • COI: 1:CAS:528:DC%2BD3cXis1Wksrk%3D, PID: 10754312
    • Mattsson PT, Lappalainen I, Bäckesjö CM, Brockmann E, Lauren S, Vihinen M, Smith CIE (2000) Six X-linked agammaglobulinemia-causing missense mutations in the Src homology 2 domain of Bruton’s tyrosine kinase: phosphotyrosine-binding and circular dichroism analysis. J Immunol 164:4170–4177.
    • (2000) J Immunol , vol.164 , pp. 4170-4177
    • Mattsson, P.T.1    Lappalainen, I.2    Bäckesjö, C.M.3    Brockmann, E.4    Lauren, S.5    Vihinen, M.6    Smith, C.I.E.7
  • 56
    • 0027363264 scopus 로고
    • Transthyretin mutation Leu-55-Pro significantly alters tetramer stability and increases amyloidogenicity
    • COI: 1:CAS:528:DyaK3sXmsVOitLo%3D, PID: 8218290
    • McCutchen SL, Colon W, Kelly JW (1993) Transthyretin mutation Leu-55-Pro significantly alters tetramer stability and increases amyloidogenicity. Biochemistry 32:12119–12127.
    • (1993) Biochemistry , vol.32 , pp. 12119-12127
    • McCutchen, S.L.1    Colon, W.2    Kelly, J.W.3
  • 57
    • 84872123748 scopus 로고    scopus 로고
    • On the molecular basis of D-bifunctional protein deficiency type III
    • PID: 23308274
    • Mehtälä ML, Lensink MF, Pietikäinen LP, Hiltunen JK, Glumoff T (2013) On the molecular basis of D-bifunctional protein deficiency type III. PLoS One 8:e53688. doi:10.1371/journal.pone.0053688.
    • (2013) PLoS One , vol.8 , pp. e53688
    • Mehtälä, M.L.1    Lensink, M.F.2    Pietikäinen, L.P.3    Hiltunen, J.K.4    Glumoff, T.5
  • 58
    • 84922351308 scopus 로고    scopus 로고
    • Niroula A, Urolagin S, Vihinen M (2015) PON-P2: prediction method for fast and reliable identification of harmful variants. PLoS One (in press)
    • Niroula A, Urolagin S, Vihinen M (2015) PON-P2: prediction method for fast and reliable identification of harmful variants. PLoS One (in press).
  • 59
    • 4444329802 scopus 로고    scopus 로고
    • A novel mutation (I143NT) in guanylate cyclase-activating protein 1 (GCAP1) associated with autosomal dominant cone degeneration
    • PID: 15505030
    • Nishiguchi KM, Sokal I, Yang L, Roychowdhury N, Palczewski K, Berson EL, Dryja TP, Baehr W (2004) A novel mutation (I143NT) in guanylate cyclase-activating protein 1 (GCAP1) associated with autosomal dominant cone degeneration. Invest Ophthalmol Vis Sci 45:3863–3870. doi:10.1167/iovs.04-0590.
    • (2004) Invest Ophthalmol Vis Sci , vol.45 , pp. 3863-3870
    • Nishiguchi, K.M.1    Sokal, I.2    Yang, L.3    Roychowdhury, N.4    Palczewski, K.5    Berson, E.L.6    Dryja, T.P.7    Baehr, W.8
  • 61
    • 84872360566 scopus 로고    scopus 로고
    • Skeletal muscle α-actin diseases (actinopathies): pathology and mechanisms
    • COI: 1:CAS:528:DC%2BC3sXktVyrug%3D%3D, PID: 22825594
    • Nowak KJ, Ravenscroft G, Laing NG (2013) Skeletal muscle α-actin diseases (actinopathies): pathology and mechanisms. Acta Neuropathol 125:19–32. doi:10.1007/s00401-012-1019-z.
    • (2013) Acta Neuropathol , vol.125 , pp. 19-32
    • Nowak, K.J.1    Ravenscroft, G.2    Laing, N.G.3
  • 62
    • 0033547358 scopus 로고    scopus 로고
    • Pleckstrin homology domains of tec family protein kinases
    • COI: 1:CAS:528:DyaK1MXntVCnurY%3D, PID: 10548506
    • Okoh MP, Vihinen M (1999) Pleckstrin homology domains of tec family protein kinases. Biochem Biophys Res Commun 265:151–157. doi:10.1006/bbrc.1999.1407.
    • (1999) Biochem Biophys Res Commun , vol.265 , pp. 151-157
    • Okoh, M.P.1    Vihinen, M.2
  • 63
  • 64
    • 84863875423 scopus 로고    scopus 로고
    • PON-P: integrated predictor for pathogenicity of missense variants
    • COI: 1:CAS:528:DC%2BC38XhtVeju7nP, PID: 22505138
    • Olatubosun A, Väliaho J, Härkönen J, Thusberg J, Vihinen M (2012) PON-P: integrated predictor for pathogenicity of missense variants. Hum Mutat 33:1166–1174. doi:10.1002/humu.22102.
    • (2012) Hum Mutat , vol.33 , pp. 1166-1174
    • Olatubosun, A.1    Väliaho, J.2    Härkönen, J.3    Thusberg, J.4    Vihinen, M.5
  • 65
    • 40949117264 scopus 로고    scopus 로고
    • Flexible nets: disorder and induced fit in the associations of p53 and 14-3-3 with their partners
    • Oldfield CJ, Meng J, Yang JY, Yang MQ, Uversky VN, Dunker AK (2008) Flexible nets: disorder and induced fit in the associations of p53 and 14-3-3 with their partners. BMC Genom 9(Suppl 1):S1. doi:10.1186/1471-2164-9-s1-s1.
    • (2008) BMC Genom , vol.9 , pp. S1
    • Oldfield, C.J.1    Meng, J.2    Yang, J.Y.3    Yang, M.Q.4    Uversky, V.N.5    Dunker, A.K.6
  • 66
    • 56249084550 scopus 로고    scopus 로고
    • Mutation of the IFNAR-1 receptor binding site of human IFN-α2 generates type I IFN competitive antagonists
    • COI: 1:CAS:528:DC%2BD1cXhtlGrs73E, PID: 18937499
    • Pan M, Kalie E, Scaglione BJ, Raveche ES, Schreiber G, Langer JA (2008) Mutation of the IFNAR-1 receptor binding site of human IFN-α2 generates type I IFN competitive antagonists. Biochemistry 47:12018–12027. doi:10.1021/bi801588g.
    • (2008) Biochemistry , vol.47 , pp. 12018-12027
    • Pan, M.1    Kalie, E.2    Scaglione, B.J.3    Raveche, E.S.4    Schreiber, G.5    Langer, J.A.6
  • 67
    • 84891339888 scopus 로고    scopus 로고
    • The biophysical and biochemical properties of the autoimmune regulator (AIRE) protein
    • COI: 1:CAS:528:DC%2BC2cXksFOntg%3D%3D, PID: 24275490
    • Perniola R, Musco G (2014) The biophysical and biochemical properties of the autoimmune regulator (AIRE) protein. Biochim Biophys Acta 1842:326–337. doi:10.1016/j.bbadis.2013.11.020.
    • (2014) Biochim Biophys Acta , vol.1842 , pp. 326-337
    • Perniola, R.1    Musco, G.2
  • 68
    • 33751011339 scopus 로고    scopus 로고
    • Immunodeficiency mutation databases (IDbases)
    • PID: 17004234
    • Piirilä H, Väliaho J, Vihinen M (2006) Immunodeficiency mutation databases (IDbases). Hum Mutat 27:1200–1208. doi:10.1002/humu.20405.
    • (2006) Hum Mutat , vol.27 , pp. 1200-1208
    • Piirilä, H.1    Väliaho, J.2    Vihinen, M.3
  • 69
    • 0346729697 scopus 로고    scopus 로고
    • Neuroprotective functions of prion protein
    • COI: 1:CAS:528:DC%2BD2cXjvV2muw%3D%3D, PID: 14705136
    • Roucou X, Gains M, LeBlanc AC (2004) Neuroprotective functions of prion protein. J Neurosci Res 75:153–161. doi:10.1002/jnr.10864.
    • (2004) J Neurosci Res , vol.75 , pp. 153-161
    • Roucou, X.1    Gains, M.2    LeBlanc, A.C.3
  • 70
    • 84922011086 scopus 로고    scopus 로고
    • VariSNP, a benchmark database for variations from dbSNP. Hum Mutat
    • Schaafsma G, Vihinen M (2014) VariSNP, a benchmark database for variations from dbSNP. Hum Mutat. doi:10.1002/humu.22727.
    • (2014) doi:10.1002/humu.22727
    • Schaafsma, G.1    Vihinen, M.2
  • 71
    • 84882448815 scopus 로고    scopus 로고
    • Rapid degradation of an active formylglycine generating enzyme variant leads to a late infantile severe form of multiple sulfatase deficiency
    • COI: 1:CAS:528:DC%2BC3sXhtlSit77M, PID: 23321616
    • Schlotawa L, Radhakrishnan K, Baumgartner M, Schmid R, Schmidt B, Dierks T, Gartner J (2013) Rapid degradation of an active formylglycine generating enzyme variant leads to a late infantile severe form of multiple sulfatase deficiency. Eur J Hum Genet 21:1020–1023. doi:10.1038/ejhg.2012.291.
    • (2013) Eur J Hum Genet , vol.21 , pp. 1020-1023
    • Schlotawa, L.1    Radhakrishnan, K.2    Baumgartner, M.3    Schmid, R.4    Schmidt, B.5    Dierks, T.6    Gartner, J.7
  • 72
    • 84897456458 scopus 로고    scopus 로고
    • MutationTaster2: mutation prediction for the deep-sequencing age
    • COI: 1:CAS:528:DC%2BC2cXltFaisb0%3D, PID: 24681721
    • Schwarz JM, Cooper DN, Schuelke M, Seelow D (2014) MutationTaster2: mutation prediction for the deep-sequencing age. Nat Methods 11:361–362. doi:10.1038/nmeth.2890.
    • (2014) Nat Methods , vol.11 , pp. 361-362
    • Schwarz, J.M.1    Cooper, D.N.2    Schuelke, M.3    Seelow, D.4
  • 73
    • 0032544408 scopus 로고    scopus 로고
    • 55 → Pro transthyretin variant reveals a possible pathway for transthyretin polymerization into amyloid fibrils
    • PID: 9733771
    • 55 → Pro transthyretin variant reveals a possible pathway for transthyretin polymerization into amyloid fibrils. J Biol Chem 273:24715–24722.
    • (1998) J Biol Chem , vol.273 , pp. 24715-24722
    • Sebastião, M.P.1    Saraiva, M.J.2    Damas, A.M.3
  • 75
    • 2942689385 scopus 로고    scopus 로고
    • Conservation and covariance in PH domain sequences: physicochemical profile and information theoretical analysis of XLA-causing mutations in the Btk PH domain
    • COI: 1:CAS:528:DC%2BD2cXksVahsbY%3D, PID: 15082835
    • Shen B, Vihinen M (2004) Conservation and covariance in PH domain sequences: physicochemical profile and information theoretical analysis of XLA-causing mutations in the Btk PH domain. Protein Eng Des Sel 17:267–276. doi:10.1093/protein/gzh030.
    • (2004) Protein Eng Des Sel , vol.17 , pp. 267-276
    • Shen, B.1    Vihinen, M.2
  • 76
    • 77951902249 scopus 로고    scopus 로고
    • Elimination of the native structure and solubility of the hVAPB MSP domain by the Pro56Ser mutation that causes amyotrophic lateral sclerosis
    • COI: 1:CAS:528:DC%2BC3cXkslKku70%3D, PID: 20377183
    • Shi J, Lua S, Tong JS, Song J (2010) Elimination of the native structure and solubility of the hVAPB MSP domain by the Pro56Ser mutation that causes amyotrophic lateral sclerosis. Biochemistry 49:3887–3897. doi:10.1021/bi902057a.
    • (2010) Biochemistry , vol.49 , pp. 3887-3897
    • Shi, J.1    Lua, S.2    Tong, J.S.3    Song, J.4
  • 77
    • 84885173246 scopus 로고    scopus 로고
    • Exploring the structural insights on human laforin mutation K87A in Lafora disease—a molecular dynamics study
    • COI: 1:CAS:528:DC%2BC3sXht1ShsbjP, PID: 23904258
    • Srikumar PS, Rohini K (2013) Exploring the structural insights on human laforin mutation K87A in Lafora disease—a molecular dynamics study. Appl Biochem Biotechnol 171:874–882. doi:10.1007/s12010-013-0393-x.
    • (2013) Appl Biochem Biotechnol , vol.171 , pp. 874-882
    • Srikumar, P.S.1    Rohini, K.2
  • 78
    • 84885184466 scopus 로고    scopus 로고
    • Molecular mechanisms of disease-causing missense mutations
    • COI: 1:CAS:528:DC%2BC3sXht1GmtbfF, PID: 23871686
    • Stefl S, Nishi H, Petukh M, Panchenko AR, Alexov E (2013) Molecular mechanisms of disease-causing missense mutations. J Mol Biol 425:3919–3936. doi:10.1016/j.jmb.2013.07.014.
    • (2013) J Mol Biol , vol.425 , pp. 3919-3936
    • Stefl, S.1    Nishi, H.2    Petukh, M.3    Panchenko, A.R.4    Alexov, E.5
  • 79
    • 0042830297 scopus 로고    scopus 로고
    • Molecular basis of inherited diseases: a structural perspective
    • COI: 1:CAS:528:DC%2BD3sXmvVKlur0%3D, PID: 12957544
    • Steward RE, MacArthur MW, Laskowski RA, Thornton JM (2003) Molecular basis of inherited diseases: a structural perspective. Trends Genet 19:505–513. doi:10.1016/s0168-9525(03)00195-1.
    • (2003) Trends Genet , vol.19 , pp. 505-513
    • Steward, R.E.1    MacArthur, M.W.2    Laskowski, R.A.3    Thornton, J.M.4
  • 80
    • 84857206020 scopus 로고    scopus 로고
    • Experimental approaches to evaluate the contributions of candidate protein-coding mutations to phenotypic evolution
    • COI: 1:CAS:528:DC%2BC38XmsFeqtb0%3D, PID: 22065450
    • Storz JF, Zera AJ (2011) Experimental approaches to evaluate the contributions of candidate protein-coding mutations to phenotypic evolution. Methods Mol Biol 772:377–396. doi:10.1007/978-1-61779-228-1_22.
    • (2011) Methods Mol Biol , vol.772 , pp. 377-396
    • Storz, J.F.1    Zera, A.J.2
  • 82
    • 0032006595 scopus 로고    scopus 로고
    • Molecular basis of selective IgG2 deficiency. The mutated membrane-bound form of gamma2 heavy chain caused complete IGG2 deficiency in two Japanese siblings
    • COI: 1:CAS:528:DyaK1cXosVamsg%3D%3D, PID: 9449702
    • Tashita H, Fukao T, Kaneko H, Teramoto T, Inoue R, Kasahara K, Kondo N (1998) Molecular basis of selective IgG2 deficiency. The mutated membrane-bound form of gamma2 heavy chain caused complete IGG2 deficiency in two Japanese siblings. J Clin Invest 101:677–681. doi:10.1172/jci1672.
    • (1998) J Clin Invest , vol.101 , pp. 677-681
    • Tashita, H.1    Fukao, T.2    Kaneko, H.3    Teramoto, T.4    Inoue, R.5    Kasahara, K.6    Kondo, N.7
  • 83
    • 33750971454 scopus 로고    scopus 로고
    • Bioinformatic analysis of protein structure–function relationships: case study of leukocyte elastase (ELA2) missense mutations
    • COI: 1:CAS:528:DC%2BD28Xhtlans77P, PID: 16986121
    • Thusberg J, Vihinen M (2006) Bioinformatic analysis of protein structure–function relationships: case study of leukocyte elastase (ELA2) missense mutations. Hum Mutat 27:1230–1243. doi:10.1002/humu.20407.
    • (2006) Hum Mutat , vol.27 , pp. 1230-1243
    • Thusberg, J.1    Vihinen, M.2
  • 84
    • 65649108490 scopus 로고    scopus 로고
    • Pathogenic or not? And if so, then how? Studying the effects of missense mutations using bioinformatics methods
    • COI: 1:CAS:528:DC%2BD1MXmtVymtrY%3D, PID: 19267389
    • Thusberg J, Vihinen M (2009) Pathogenic or not? And if so, then how? Studying the effects of missense mutations using bioinformatics methods. Hum Mutat 30:703–714. doi:10.1002/humu.20938.
    • (2009) Hum Mutat , vol.30 , pp. 703-714
    • Thusberg, J.1    Vihinen, M.2
  • 85
    • 79952764520 scopus 로고    scopus 로고
    • Performance of mutation pathogenicity prediction methods on missense variants
    • PID: 21412949
    • Thusberg J, Olatubosun A, Vihinen M (2011) Performance of mutation pathogenicity prediction methods on missense variants. Hum Mutat 32:358–368. doi:10.1002/humu.21445.
    • (2011) Hum Mutat , vol.32 , pp. 358-368
    • Thusberg, J.1    Olatubosun, A.2    Vihinen, M.3
  • 86
    • 80052370584 scopus 로고    scopus 로고
    • Lys98 substitution in human AP endonuclease 1 affects the kinetic mechanism of enzyme action in base excision and nucleotide incision repair pathways
    • COI: 1:CAS:528:DC%2BC3MXht1Wrtb%2FP, PID: 21912662
    • Timofeyeva NA, Koval VV, Ishchenko AA, Saparbaev MK, Fedorova OS (2011) Lys98 substitution in human AP endonuclease 1 affects the kinetic mechanism of enzyme action in base excision and nucleotide incision repair pathways. PLoS One 6:e24063. doi:10.1371/journal.pone.0024063.
    • (2011) PLoS One , vol.6 , pp. e24063
    • Timofeyeva, N.A.1    Koval, V.V.2    Ishchenko, A.A.3    Saparbaev, M.K.4    Fedorova, O.S.5
  • 87
    • 36248964819 scopus 로고    scopus 로고
    • The PASTA server for protein aggregation prediction
    • COI: 1:CAS:528:DC%2BD2sXhsVCmtr3I, PID: 17720750
    • Trovato A, Seno F, Tosatto SC (2007) The PASTA server for protein aggregation prediction. Protein Eng Des Sel 20:521–523. doi:10.1093/protein/gzm042.
    • (2007) Protein Eng Des Sel , vol.20 , pp. 521-523
    • Trovato, A.1    Seno, F.2    Tosatto, S.C.3
  • 88
    • 84884776927 scopus 로고    scopus 로고
    • A constitutively activating mutation alters the dynamics and energetics of a key conformational change in a ligand-free G protein-coupled receptor
    • COI: 1:CAS:528:DC%2BC3sXhsFemsL3M, PID: 23940032
    • Tsukamoto H, Farrens DL (2013) A constitutively activating mutation alters the dynamics and energetics of a key conformational change in a ligand-free G protein-coupled receptor. J Biol Chem 288:28207–28216. doi:10.1074/jbc.M113.472464.
    • (2013) J Biol Chem , vol.288 , pp. 28207-28216
    • Tsukamoto, H.1    Farrens, D.L.2
  • 90
    • 84880047467 scopus 로고    scopus 로고
    • DEF pocket in p38α facilitates substrate selectivity and mediates autophosphorylation
    • COI: 1:CAS:528:DC%2BC3sXhtVKms7%2FF, PID: 23671282
    • Tzarum N, Komornik N, Ben Chetrit D, Engelberg D, Livnah O (2013) DEF pocket in p38α facilitates substrate selectivity and mediates autophosphorylation. J Biol Chem 288:19537–19547. doi:10.1074/jbc.M113.464511.
    • (2013) J Biol Chem , vol.288 , pp. 19537-19547
    • Tzarum, N.1    Komornik, N.2    Ben Chetrit, D.3    Engelberg, D.4    Livnah, O.5
  • 91
    • 0023557882 scopus 로고
    • Relationship of protein flexibility to thermostability
    • COI: 1:CAS:528:DyaL1cXhtVynsLc%3D, PID: 3508295
    • Vihinen M (1987) Relationship of protein flexibility to thermostability. Protein Eng 1:477–480.
    • (1987) Protein Eng , vol.1 , pp. 477-480
    • Vihinen, M.1
  • 92
    • 84893636595 scopus 로고    scopus 로고
    • Variation ontology for annotation of variation effects and mechanisms
    • COI: 1:CAS:528:DC%2BC2cXisVKjsr0%3D, PID: 24162187
    • Vihinen M (2014a) Variation ontology for annotation of variation effects and mechanisms. Genome Res 24:356–364. doi:10.1101/gr.157495.113.
    • (2014) Genome Res , vol.24 , pp. 356-364
    • Vihinen, M.1
  • 93
    • 84925504770 scopus 로고    scopus 로고
    • Variation ontology: annotator guide
    • Vihinen M (2014b) Variation ontology: annotator guide. J Biomed Semant 5:9. doi:10.1186/2041-1480-5-9.
    • (2014) J Biomed Semant , vol.5 , pp. 9
    • Vihinen, M.1
  • 95
    • 1542577828 scopus 로고    scopus 로고
    • The amino-acid mutational spectrum of human genetic disease
    • PID: 14611658
    • Vitkup D, Sander C, Church GM (2003) The amino-acid mutational spectrum of human genetic disease. Genome Biol 4:R72. doi:10.1186/gb-2003-4-11-r72.
    • (2003) Genome Biol , vol.4 , pp. R72
    • Vitkup, D.1    Sander, C.2    Church, G.M.3
  • 97
    • 0035065485 scopus 로고    scopus 로고
    • SNPs, protein structure, and disease
    • PID: 11295823
    • Wang Z, Moult J (2001) SNPs, protein structure, and disease. Hum Mutat 17:263–270. doi:10.1002/humu.22.
    • (2001) Hum Mutat , vol.17 , pp. 263-270
    • Wang, Z.1    Moult, J.2
  • 98
    • 82755189530 scopus 로고    scopus 로고
    • Biochemical characterization of the M712T-mutation of the UDP-N-acetylglucosamine 2-epimerase/N-acetyl-mannosaminekinase in hereditary inclusion body myopathy
    • PID: 21873062
    • Weidemann W, Reinhardt A, Thate A, Horstkorte R (2011) Biochemical characterization of the M712T-mutation of the UDP-N-acetylglucosamine 2-epimerase/N-acetyl-mannosaminekinase in hereditary inclusion body myopathy. Neuromuscul Disord 21:824–831. doi:10.1016/j.nmd.2011.06.004.
    • (2011) Neuromuscul Disord , vol.21 , pp. 824-831
    • Weidemann, W.1    Reinhardt, A.2    Thate, A.3    Horstkorte, R.4
  • 99
    • 62449145670 scopus 로고    scopus 로고
    • Centriole inheritance
    • PID: 19164929
    • Wilson PG (2008) Centriole inheritance. Prion 2:9–16.
    • (2008) Prion , vol.2 , pp. 9-16
    • Wilson, P.G.1
  • 100
    • 0036137007 scopus 로고    scopus 로고
    • A cavity-forming mutation in insulin induces segmental unfolding of a surrounding α-helix
    • COI: 1:CAS:528:DC%2BD38XltlOl, PID: 11742127
    • Xu B, Hua QX, Nakagawa SH, Jia W, Chu YC, Katsoyannis PG, Weiss MA (2002) A cavity-forming mutation in insulin induces segmental unfolding of a surrounding α-helix. Protein Sci 11:104–116. doi:10.1110/ps.32102.
    • (2002) Protein Sci , vol.11 , pp. 104-116
    • Xu, B.1    Hua, Q.X.2    Nakagawa, S.H.3    Jia, W.4    Chu, Y.C.5    Katsoyannis, P.G.6    Weiss, M.A.7
  • 101
    • 84870857654 scopus 로고    scopus 로고
    • The congenital cataract-linked A2V mutation impairs tetramer formation and promotes aggregation of βB2-crystallin
    • COI: 1:CAS:528:DC%2BC38XhvV2jsL7M, PID: 23236454
    • Xu J, Wang S, Zhao WJ, Xi YB, Yan YB, Yao K (2012) The congenital cataract-linked A2V mutation impairs tetramer formation and promotes aggregation of βB2-crystallin. PLoS One 7:e51200. doi:10.1371/journal.pone.0051200.
    • (2012) PLoS One , vol.7 , pp. e51200
    • Xu, J.1    Wang, S.2    Zhao, W.J.3    Xi, Y.B.4    Yan, Y.B.5    Yao, K.6
  • 102
    • 84888823769 scopus 로고    scopus 로고
    • Disease-associated single amino acid mutation in the calf-1 domain of integrin α3 leads to defects in its processing and cell surface expression
    • COI: 1:CAS:528:DC%2BC3sXhvVSlu77J, PID: 24220332
    • Yamada M, Sekiguchi K (2013) Disease-associated single amino acid mutation in the calf-1 domain of integrin α3 leads to defects in its processing and cell surface expression. Biochem Biophys Res Commun 441:988–993. doi:10.1016/j.bbrc.2013.11.003.
    • (2013) Biochem Biophys Res Commun , vol.441 , pp. 988-993
    • Yamada, M.1    Sekiguchi, K.2
  • 103
    • 84885190937 scopus 로고    scopus 로고
    • The effects of non-synonymous single nucleotide polymorphisms (nsSNPs) on protein–protein interactions
    • COI: 1:CAS:528:DC%2BC3sXht1aqtrbK, PID: 23867278
    • Yates CM, Sternberg MJ (2013) The effects of non-synonymous single nucleotide polymorphisms (nsSNPs) on protein–protein interactions. J Mol Biol 425:3949–3963. doi:10.1016/j.jmb.2013.07.012.
    • (2013) J Mol Biol , vol.425 , pp. 3949-3963
    • Yates, C.M.1    Sternberg, M.J.2
  • 104
    • 34249777526 scopus 로고    scopus 로고
    • Eris: an automated estimator of protein stability
    • COI: 1:CAS:528:DC%2BD2sXlvVykurg%3D, PID: 17538626
    • Yin S, Ding F, Dokholyan NV (2007) Eris: an automated estimator of protein stability. Nat Methods 4:466–467. doi:10.1038/nmeth0607-466.
    • (2007) Nat Methods , vol.4 , pp. 466-467
    • Yin, S.1    Ding, F.2    Dokholyan, N.V.3
  • 105
    • 84876273572 scopus 로고    scopus 로고
    • Structural and mechanistic insights into LEOPARD syndrome-associated SHP2 mutations
    • COI: 1:CAS:528:DC%2BC3sXlvV2qsrg%3D, PID: 23457302
    • Yu ZH, Xu J, Walls CD, Chen L, Zhang S, Zhang R, Wu L, Wang L, Liu S, Zhang ZY (2013) Structural and mechanistic insights into LEOPARD syndrome-associated SHP2 mutations. J Biol Chem 288:10472–10482. doi:10.1074/jbc.M113.450023.
    • (2013) J Biol Chem , vol.288 , pp. 10472-10482
    • Yu, Z.H.1    Xu, J.2    Walls, C.D.3    Chen, L.4    Zhang, S.5    Zhang, R.6    Wu, L.7    Wang, L.8    Liu, S.9    Zhang, Z.Y.10
  • 107
    • 25144523127 scopus 로고    scopus 로고
    • Loss of protein structure stability as a major causative factor in monogenic disease
    • COI: 1:CAS:528:DC%2BD2MXhtVGrtrfL, PID: 16169011
    • Yue P, Li Z, Moult J (2005) Loss of protein structure stability as a major causative factor in monogenic disease. J Mol Biol 353:459–473. doi:10.1016/j.jmb.2005.08.020.
    • (2005) J Mol Biol , vol.353 , pp. 459-473
    • Yue, P.1    Li, Z.2    Moult, J.3
  • 108
    • 84861052952 scopus 로고    scopus 로고
    • Analyzing effects of naturally occurring missense mutations
    • PID: 22577471
    • Zhang Z, Miteva MA, Wang L, Alexov E (2012) Analyzing effects of naturally occurring missense mutations. Comput Math Methods Med 2012:805827. doi:10.1155/2012/805827.
    • (2012) Comput Math Methods Med , vol.2012 , pp. 805827
    • Zhang, Z.1    Miteva, M.A.2    Wang, L.3    Alexov, E.4


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