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== Structural highlights ==
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<table><tr><td colspan='2'>[[3dtp]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Avicularia_avicularia Avicularia avicularia], [https://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus] and [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3DTP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3DTP FirstGlance]. <br>
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[https://www.uniprot.org/uniprot/MYH7_HUMAN MYH7_HUMAN] Defects in MYH7 are the cause of familial hypertrophic cardiomyopathy type 1 (CMH1) [MIM:[https://omim.org/entry/192600 192600]. Familial hypertrophic cardiomyopathy is a hereditary heart disorder characterized by ventricular hypertrophy, which is usually asymmetric and often involves the interventricular septum. The symptoms include dyspnea, syncope, collapse, palpitations, and chest pain. They can be readily provoked by exercise. The disorder has inter- and intrafamilial variability ranging from benign to malignant forms with high risk of cardiac failure and sudden cardiac death.<ref>PMID:1975517</ref> <ref>PMID:1417858</ref> <ref>PMID:1638703</ref> <ref>PMID:1552912</ref> <ref>PMID:8250038</ref> <ref>PMID:8343162</ref> <ref>PMID:8435239</ref> <ref>PMID:8268932</ref> <ref>PMID:8254035</ref> <ref>PMID:8483915</ref> <ref>PMID:7848441</ref> <ref>PMID:7874131</ref> <ref>PMID:8282798</ref> <ref>PMID:7581410</ref> <ref>PMID:7731997</ref> <ref>PMID:8655135</ref> <ref>PMID:8899546</ref> <ref>PMID:10065021</ref> <ref>PMID:9544842</ref> <ref>PMID:9829907</ref> <ref>PMID:9822100</ref> <ref>PMID:10521296</ref> <ref>PMID:10563488</ref> <ref>PMID:10329202</ref> <ref>PMID:10679957</ref> <ref>PMID:10862102</ref> <ref>PMID:11113006</ref> <ref>PMID:11214007</ref> <ref>PMID:11733062</ref> <ref>PMID:11424919</ref> <ref>PMID:11133230</ref> <ref>PMID:12081993</ref> <ref>PMID:11861413</ref> <ref>PMID:11968089</ref> <ref>PMID:12951062</ref> <ref>PMID:12566107</ref> <ref>PMID:12707239</ref> <ref>PMID:12974739</ref> <ref>PMID:12820698</ref> <ref>PMID:12975413</ref> <ref>PMID:12590187</ref> <ref>PMID:12818575</ref> <ref>PMID:15358028</ref> <ref>PMID:15563892</ref> <ref>PMID:15483641</ref> <ref>PMID:15858117</ref> <ref>PMID:16199542</ref> <ref>PMID:15856146</ref> <ref>PMID:16650083</ref> <ref>PMID:16938236</ref> <ref>PMID:17372140</ref> <ref>PMID:18403758</ref> Defects in MYH7 are the cause of myopathy myosin storage (MYOMS) [MIM:[https://omim.org/entry/608358 608358]. In this disorder, muscle biopsy shows type 1 fiber predominance and increased interstitial fat and connective tissue. Inclusion bodies consisting of the beta cardiac myosin heavy chain are present in the majority of type 1 fibers, but not in type 2 fibers.<ref>PMID:14520662</ref> <ref>PMID:15136674</ref> <ref>PMID:17336526</ref> Defects in MYH7 are the cause of scapuloperoneal myopathy MYH7-related (SPMM) [MIM:[https://omim.org/entry/181430 181430]; also known as scapuloperoneal syndrome myopathic type. SPMM is a progressive muscular atrophia beginning in the lower legs and affecting the shoulder region earlier and more severely than distal arm.<ref>PMID:17336526</ref> Defects in MYH7 are a cause of cardiomyopathy dilated type 1S (CMD1S) [MIM:[https://omim.org/entry/613426 613426]. Dilated cardiomyopathy is a disorder characterized by ventricular dilation and impaired systolic function, resulting in congestive heart failure and arrhythmia. Patients are at risk of premature death.<ref>PMID:11106718</ref> <ref>PMID:12379228</ref> <ref>PMID:15769782</ref> <ref>PMID:21846512</ref> Defects in MYH7 are the cause of myopathy distal type 1 (MPD1) [MIM:[https://omim.org/entry/160500 160500]. MPD1 is a muscular disorder characterized by early-onset selective weakness of the great toe and ankle dorsiflexors, followed by weakness of the finger extensors. Mild proximal weakness occasionally develops years later after the onset of the disease.<ref>PMID:15322983</ref> <ref>PMID:17548557</ref>
<text>to colour the structure by Evolutionary Conservation</text>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3dtp ConSurf].
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== Publication Abstract from PubMed ==
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Muscle contraction involves the interaction of the myosin heads of the thick filaments with actin subunits of the thin filaments. Relaxation occurs when this interaction is blocked by molecular switches on these filaments. In many muscles, myosin-linked regulation involves phosphorylation of the myosin regulatory light chains (RLCs). Electron microscopy of vertebrate smooth muscle myosin molecules (regulated by phosphorylation) has provided insight into the relaxed structure, revealing that myosin is switched off by intramolecular interactions between its two heads, the free head and the blocked head. Three-dimensional reconstruction of frozen-hydrated specimens revealed that this asymmetric head interaction is also present in native thick filaments of tarantula striated muscle. Our goal in this study was to elucidate the structural features of the tarantula filament involved in phosphorylation-based regulation. A new reconstruction revealed intra- and intermolecular myosin interactions in addition to those seen previously. To help interpret the interactions, we sequenced the tarantula RLC and fitted an atomic model of the myosin head that included the predicted RLC atomic structure and an S2 (subfragment 2) crystal structure to the reconstruction. The fitting suggests one intramolecular interaction, between the cardiomyopathy loop of the free head and its own S2, and two intermolecular interactions, between the cardiac loop of the free head and the essential light chain of the blocked head and between the Leu305-Gln327 interaction loop of the free head and the N-terminal fragment of the RLC of the blocked head. These interactions, added to those previously described, would help switch off the thick filament. Molecular dynamics simulations suggest how phosphorylation could increase the helical content of the RLC N-terminus, weakening these interactions, thus releasing both heads and activating the thick filament.
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===Tarantula heavy meromyosin obtained by flexible docking to Tarantula muscle thick filament Cryo-EM 3D-MAP===
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Three-dimensional reconstruction of tarantula myosin filaments suggests how phosphorylation may regulate myosin activity.,Alamo L, Wriggers W, Pinto A, Bartoli F, Salazar L, Zhao FQ, Craig R, Padron R J Mol Biol. 2008 Dec 26;384(4):780-97. Epub 2008 Oct 14. PMID:18951904<ref>PMID:18951904</ref>
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{{ABSTRACT_PUBMED_18951904}}
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==About this Structure==
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[[3dtp]] is a 6 chain structure of [[Myosin]] with sequence from [http://en.wikipedia.org/wiki/Avicularia_avicularia Avicularia avicularia], [http://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus] and [http://en.wikipedia.org/wiki/Gallus_gallus,_homo_sapiens Gallus gallus, homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3DTP OCA].
MYH7_HUMAN Defects in MYH7 are the cause of familial hypertrophic cardiomyopathy type 1 (CMH1) [MIM:192600. Familial hypertrophic cardiomyopathy is a hereditary heart disorder characterized by ventricular hypertrophy, which is usually asymmetric and often involves the interventricular septum. The symptoms include dyspnea, syncope, collapse, palpitations, and chest pain. They can be readily provoked by exercise. The disorder has inter- and intrafamilial variability ranging from benign to malignant forms with high risk of cardiac failure and sudden cardiac death.[1][2][3][4][5][6][7][8][9][10][11][12][13][14][15][16][17][18][19][20][21][22][23][24][25][26][27][28][29][30][31][32][33][34][35][36][37][38][39][40][41][42][43][44][45][46][47][48][49][50][51][52] Defects in MYH7 are the cause of myopathy myosin storage (MYOMS) [MIM:608358. In this disorder, muscle biopsy shows type 1 fiber predominance and increased interstitial fat and connective tissue. Inclusion bodies consisting of the beta cardiac myosin heavy chain are present in the majority of type 1 fibers, but not in type 2 fibers.[53][54][55] Defects in MYH7 are the cause of scapuloperoneal myopathy MYH7-related (SPMM) [MIM:181430; also known as scapuloperoneal syndrome myopathic type. SPMM is a progressive muscular atrophia beginning in the lower legs and affecting the shoulder region earlier and more severely than distal arm.[56] Defects in MYH7 are a cause of cardiomyopathy dilated type 1S (CMD1S) [MIM:613426. Dilated cardiomyopathy is a disorder characterized by ventricular dilation and impaired systolic function, resulting in congestive heart failure and arrhythmia. Patients are at risk of premature death.[57][58][59][60] Defects in MYH7 are the cause of myopathy distal type 1 (MPD1) [MIM:160500. MPD1 is a muscular disorder characterized by early-onset selective weakness of the great toe and ankle dorsiflexors, followed by weakness of the finger extensors. Mild proximal weakness occasionally develops years later after the onset of the disease.[61][62]
Checkto colour the structure by Evolutionary Conservation, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Muscle contraction involves the interaction of the myosin heads of the thick filaments with actin subunits of the thin filaments. Relaxation occurs when this interaction is blocked by molecular switches on these filaments. In many muscles, myosin-linked regulation involves phosphorylation of the myosin regulatory light chains (RLCs). Electron microscopy of vertebrate smooth muscle myosin molecules (regulated by phosphorylation) has provided insight into the relaxed structure, revealing that myosin is switched off by intramolecular interactions between its two heads, the free head and the blocked head. Three-dimensional reconstruction of frozen-hydrated specimens revealed that this asymmetric head interaction is also present in native thick filaments of tarantula striated muscle. Our goal in this study was to elucidate the structural features of the tarantula filament involved in phosphorylation-based regulation. A new reconstruction revealed intra- and intermolecular myosin interactions in addition to those seen previously. To help interpret the interactions, we sequenced the tarantula RLC and fitted an atomic model of the myosin head that included the predicted RLC atomic structure and an S2 (subfragment 2) crystal structure to the reconstruction. The fitting suggests one intramolecular interaction, between the cardiomyopathy loop of the free head and its own S2, and two intermolecular interactions, between the cardiac loop of the free head and the essential light chain of the blocked head and between the Leu305-Gln327 interaction loop of the free head and the N-terminal fragment of the RLC of the blocked head. These interactions, added to those previously described, would help switch off the thick filament. Molecular dynamics simulations suggest how phosphorylation could increase the helical content of the RLC N-terminus, weakening these interactions, thus releasing both heads and activating the thick filament.
Three-dimensional reconstruction of tarantula myosin filaments suggests how phosphorylation may regulate myosin activity.,Alamo L, Wriggers W, Pinto A, Bartoli F, Salazar L, Zhao FQ, Craig R, Padron R J Mol Biol. 2008 Dec 26;384(4):780-97. Epub 2008 Oct 14. PMID:18951904[63]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
↑ Geisterfer-Lowrance AA, Kass S, Tanigawa G, Vosberg HP, McKenna W, Seidman CE, Seidman JG. A molecular basis for familial hypertrophic cardiomyopathy: a beta cardiac myosin heavy chain gene missense mutation. Cell. 1990 Sep 7;62(5):999-1006. PMID:1975517
↑ Nishi H, Kimura A, Harada H, Toshima H, Sasazuki T. Novel missense mutation in cardiac beta myosin heavy chain gene found in a Japanese patient with hypertrophic cardiomyopathy. Biochem Biophys Res Commun. 1992 Oct 15;188(1):379-87. PMID:1417858
↑ Epstein ND, Cohn GM, Cyran F, Fananapazir L. Differences in clinical expression of hypertrophic cardiomyopathy associated with two distinct mutations in the beta-myosin heavy chain gene. A 908Leu----Val mutation and a 403Arg----Gln mutation. Circulation. 1992 Aug;86(2):345-52. PMID:1638703
↑ Watkins H, Rosenzweig A, Hwang DS, Levi T, McKenna W, Seidman CE, Seidman JG. Characteristics and prognostic implications of myosin missense mutations in familial hypertrophic cardiomyopathy. N Engl J Med. 1992 Apr 23;326(17):1108-14. PMID:1552912
↑ Watkins H, Thierfelder L, Anan R, Jarcho J, Matsumori A, McKenna W, Seidman JG, Seidman CE. Independent origin of identical beta cardiac myosin heavy-chain mutations in hypertrophic cardiomyopathy. Am J Hum Genet. 1993 Dec;53(6):1180-5. PMID:8250038
↑ Harada H, Kimura A, Nishi H, Sasazuki T, Toshima H. A missense mutation of cardiac beta-myosin heavy chain gene linked to familial hypertrophic cardiomyopathy in affected Japanese families. Biochem Biophys Res Commun. 1993 Jul 30;194(2):791-8. PMID:8343162 doi:http://dx.doi.org/10.1006/bbrc.1993.1891
↑ al-Mahdawi S, Chamberlain S, Cleland J, Nihoyannopoulos P, Gilligan D, French J, Choudhury L, Williamson R, Oakley C. Identification of a mutation in the beta cardiac myosin heavy chain gene in a family with hypertrophic cardiomyopathy. Br Heart J. 1993 Feb;69(2):136-41. PMID:8435239
↑ Moolman JC, Brink PA, Corfield VA. Identification of a new missense mutation at Arg403, a CpG mutation hotspot, in exon 13 of the beta-myosin heavy chain gene in hypertrophic cardiomyopathy. Hum Mol Genet. 1993 Oct;2(10):1731-2. PMID:8268932
↑ Dausse E, Komajda M, Fetler L, Dubourg O, Dufour C, Carrier L, Wisnewsky C, Bercovici J, Hengstenberg C, al-Mahdawi S, et al.. Familial hypertrophic cardiomyopathy. Microsatellite haplotyping and identification of a hot spot for mutations in the beta-myosin heavy chain gene. J Clin Invest. 1993 Dec;92(6):2807-13. PMID:8254035 doi:http://dx.doi.org/10.1172/JCI116900
↑ Fananapazir L, Dalakas MC, Cyran F, Cohn G, Epstein ND. Missense mutations in the beta-myosin heavy-chain gene cause central core disease in hypertrophic cardiomyopathy. Proc Natl Acad Sci U S A. 1993 May 1;90(9):3993-7. PMID:8483915
↑ Consevage MW, Salada GC, Baylen BG, Ladda RL, Rogan PK. A new missense mutation, Arg719Gln, in the beta-cardiac heavy chain myosin gene of patients with familial hypertrophic cardiomyopathy. Hum Mol Genet. 1994 Jun;3(6):1025-6. PMID:7848441
↑ Greve G, Bachinski L, Friedman DL, Czernuzewicz G, Anan R, Towbin J, Seidman CE, Roberts R. Isolation of a de novo mutant myocardial beta MHC protein in a pedigree with hypertrophic cardiomyopathy. Hum Mol Genet. 1994 Nov;3(11):2073-5. PMID:7874131
↑ Anan R, Greve G, Thierfelder L, Watkins H, McKenna WJ, Solomon S, Vecchio C, Shono H, Nakao S, Tanaka H, et al.. Prognostic implications of novel beta cardiac myosin heavy chain gene mutations that cause familial hypertrophic cardiomyopathy. J Clin Invest. 1994 Jan;93(1):280-5. PMID:8282798 doi:http://dx.doi.org/10.1172/JCI116957
↑ Moolman JC, Brink PA, Corfield VA. Identification of a novel Ala797Thr mutation in exon 21 of the beta-myosin heavy chain gene in hypertrophic cardiomyopathy. Hum Mutat. 1995;6(2):197-8. PMID:7581410 doi:http://dx.doi.org/10.1002/humu.1380060219
↑ Rayment I, Holden HM, Sellers JR, Fananapazir L, Epstein ND. Structural interpretation of the mutations in the beta-cardiac myosin that have been implicated in familial hypertrophic cardiomyopathy. Proc Natl Acad Sci U S A. 1995 Apr 25;92(9):3864-8. PMID:7731997
↑ Ko YL, Chen JJ, Tang TK, Cheng JJ, Lin SY, Liou YC, Kuan P, Wu CW, Lien WP, Liew CC. Malignant familial hypertrophic cardiomyopathy in a family with a 453Arg-->Cys mutation in the beta-myosin heavy chain gene: coexistence of sudden death and end-stage heart failure. Hum Genet. 1996 May;97(5):585-90. PMID:8655135
↑ Kuang SQ, Yu JD, Lu L, He LM, Gong LS, Chen SJ, Chen Z. Identification of a novel missense mutation in the cardiac beta-myosin heavy chain gene in a Chinese patient with sporadic hypertrophic cardiomyopathy. J Mol Cell Cardiol. 1996 Sep;28(9):1879-83. PMID:8899546 doi:S0022-2828(96)90180-7
↑ Arbustini E, Fasani R, Morbini P, Diegoli M, Grasso M, Dal Bello B, Marangoni E, Banfi P, Banchieri N, Bellini O, Comi G, Narula J, Campana C, Gavazzi A, Danesino C, Vigano M. Coexistence of mitochondrial DNA and beta myosin heavy chain mutations in hypertrophic cardiomyopathy with late congestive heart failure. Heart. 1998 Dec;80(6):548-58. PMID:10065021
↑ Jeschke B, Uhl K, Weist B, Schroder D, Meitinger T, Dohlemann C, Vosberg HP. A high risk phenotype of hypertrophic cardiomyopathy associated with a compound genotype of two mutated beta-myosin heavy chain genes. Hum Genet. 1998 Mar;102(3):299-304. PMID:9544842
↑ Tesson F, Richard P, Charron P, Mathieu B, Cruaud C, Carrier L, Dubourg O, Lautie N, Desnos M, Millaire A, Isnard R, Hagege AA, Bouhour JB, Bennaceur M, Hainque B, Guicheney P, Schwartz K, Komajda M. Genotype-phenotype analysis in four families with mutations in beta-myosin heavy chain gene responsible for familial hypertrophic cardiomyopathy. Hum Mutat. 1998;12(6):385-92. PMID:9829907 doi:<385::AID-HUMU4>3.0.CO;2-E 10.1002/(SICI)1098-1004(1998)12:6<385::AID-HUMU4>3.0.CO;2-E
↑ Jaaskelainen P, Soranta M, Miettinen R, Saarinen L, Pihlajamaki J, Silvennoinen K, Tikanoja T, Laakso M, Kuusisto J. The cardiac beta-myosin heavy chain gene is not the predominant gene for hypertrophic cardiomyopathy in the Finnish population. J Am Coll Cardiol. 1998 Nov 15;32(6):1709-16. PMID:9822100
↑ Moolman-Smook JC, De Lange WJ, Bruwer EC, Brink PA, Corfield VA. The origins of hypertrophic cardiomyopathy-causing mutations in two South African subpopulations: a unique profile of both independent and founder events. Am J Hum Genet. 1999 Nov;65(5):1308-20. PMID:10521296 doi:S0002-9297(07)62137-5
↑ Andersen PS, Havndrup O, Bundgaard H, Larsen LA, Vuust J, Kjeldsen K, Christiansen M. Adult-onset familial hypertrophic cardiomyopathy caused by a novel mutation, R694C, in the MYH7 gene. Clin Genet. 1999 Sep;56(3):244-6. PMID:10563488
↑ Bundgaard H, Havndrup O, Andersen PS, Larsen LA, Brandt NJ, Vuust J, Kjeldsen K, Christiansen M. Familial hypertrophic cardiomyopathy associated with a novel missense mutation affecting the ATP-binding region of the cardiac beta-myosin heavy chain. J Mol Cell Cardiol. 1999 Apr;31(4):745-50. PMID:10329202 doi:S0022-2828(98)90911-7
↑ Enjuto M, Francino A, Navarro-Lopez F, Viles D, Pare JC, Ballesta AM. Malignant hypertrophic cardiomyopathy caused by the Arg723Gly mutation in beta-myosin heavy chain gene. J Mol Cell Cardiol. 2000 Dec;32(12):2307-13. PMID:11113006 doi:10.1006/jmcc.2000.1260
↑ Havndrup O, Bundgaard H, Andersen PS, Larsen LA, Vuust J, Kjeldsen K, Christiansen M. A novel missense mutation, Leu390Val, in the cardiac beta-myosin heavy chain associated with pronounced septal hypertrophy in two families with hypertrophic cardiomyopathy. Scand Cardiovasc J. 2000 Dec;34(6):558-63. PMID:11214007
↑ Davis JS, Hassanzadeh S, Winitsky S, Lin H, Satorius C, Vemuri R, Aletras AH, Wen H, Epstein ND. The overall pattern of cardiac contraction depends on a spatial gradient of myosin regulatory light chain phosphorylation. Cell. 2001 Nov 30;107(5):631-41. PMID:11733062
↑ Blair E, Price SJ, Baty CJ, Ostman-Smith I, Watkins H. Mutations in cis can confound genotype-phenotype correlations in hypertrophic cardiomyopathy. J Med Genet. 2001 Jun;38(6):385-8. PMID:11424919
↑ Greber-Platzer S, Marx M, Fleischmann C, Suppan C, Dobner M, Wimmer M. Beta-myosin heavy chain gene mutations and hypertrophic cardiomyopathy in Austrian children. J Mol Cell Cardiol. 2001 Jan;33(1):141-8. PMID:11133230 doi:10.1006/jmcc.2000.1287
↑ Ho CY, Sweitzer NK, McDonough B, Maron BJ, Casey SA, Seidman JG, Seidman CE, Solomon SD. Assessment of diastolic function with Doppler tissue imaging to predict genotype in preclinical hypertrophic cardiomyopathy. Circulation. 2002 Jun 25;105(25):2992-7. PMID:12081993
↑ Blair E, Redwood C, de Jesus Oliveira M, Moolman-Smook JC, Brink P, Corfield VA, Ostman-Smith I, Watkins H. Mutations of the light meromyosin domain of the beta-myosin heavy chain rod in hypertrophic cardiomyopathy. Circ Res. 2002 Feb 22;90(3):263-9. PMID:11861413
↑ Waldmuller S, Freund P, Mauch S, Toder R, Vosberg HP. Low-density DNA microarrays are versatile tools to screen for known mutations in hypertrophic cardiomyopathy. Hum Mutat. 2002 May;19(5):560-9. PMID:11968089 doi:10.1002/humu.10074
↑ Nanni L, Pieroni M, Chimenti C, Simionati B, Zimbello R, Maseri A, Frustaci A, Lanfranchi G. Hypertrophic cardiomyopathy: two homozygous cases with "typical" hypertrophic cardiomyopathy and three new mutations in cases with progression to dilated cardiomyopathy. Biochem Biophys Res Commun. 2003 Sep 19;309(2):391-8. PMID:12951062
↑ Havndrup O, Bundgaard H, Andersen PS, Allan Larsen L, Vuust J, Kjeldsen K, Christiansen M. Outcome of clinical versus genetic family screening in hypertrophic cardiomyopathy with focus on cardiac beta-myosin gene mutations. Cardiovasc Res. 2003 Feb;57(2):347-57. PMID:12566107
↑ Richard P, Charron P, Carrier L, Ledeuil C, Cheav T, Pichereau C, Benaiche A, Isnard R, Dubourg O, Burban M, Gueffet JP, Millaire A, Desnos M, Schwartz K, Hainque B, Komajda M. Hypertrophic cardiomyopathy: distribution of disease genes, spectrum of mutations, and implications for a molecular diagnosis strategy. Circulation. 2003 May 6;107(17):2227-32. Epub 2003 Apr 21. PMID:12707239 doi:10.1161/01.CIR.0000066323.15244.54
↑ Erdmann J, Daehmlow S, Wischke S, Senyuva M, Werner U, Raible J, Tanis N, Dyachenko S, Hummel M, Hetzer R, Regitz-Zagrosek V. Mutation spectrum in a large cohort of unrelated consecutive patients with hypertrophic cardiomyopathy. Clin Genet. 2003 Oct;64(4):339-49. PMID:12974739
↑ Mohiddin SA, Begley DA, McLam E, Cardoso JP, Winkler JB, Sellers JR, Fananapazir L. Utility of genetic screening in hypertrophic cardiomyopathy: prevalence and significance of novel and double (homozygous and heterozygous) beta-myosin mutations. Genet Test. 2003 Spring;7(1):21-7. PMID:12820698 doi:10.1089/109065703321560895
↑ Woo A, Rakowski H, Liew JC, Zhao MS, Liew CC, Parker TG, Zeller M, Wigle ED, Sole MJ. Mutations of the beta myosin heavy chain gene in hypertrophic cardiomyopathy: critical functional sites determine prognosis. Heart. 2003 Oct;89(10):1179-85. PMID:12975413
↑ Moric E, Mazurek U, Polonska J, Domal-Kwiatkowska D, Smolik S, Kozakiewicz K, Tendera M, Wilczok T. Three novel mutations in exon 21 encoding beta-cardiac myosin heavy chain. J Appl Genet. 2003;44(1):103-9. PMID:12590187
↑ Morner S, Richard P, Kazzam E, Hellman U, Hainque B, Schwartz K, Waldenstrom A. Identification of the genotypes causing hypertrophic cardiomyopathy in northern Sweden. J Mol Cell Cardiol. 2003 Jul;35(7):841-9. PMID:12818575
↑ Van Driest SL, Jaeger MA, Ommen SR, Will ML, Gersh BJ, Tajik AJ, Ackerman MJ. Comprehensive analysis of the beta-myosin heavy chain gene in 389 unrelated patients with hypertrophic cardiomyopathy. J Am Coll Cardiol. 2004 Aug 4;44(3):602-10. PMID:15358028 doi:10.1016/j.jacc.2004.04.039
↑ Song L, Zou Y, Wang J, Wang Z, Zhen Y, Lou K, Zhang Q, Wang X, Wang H, Li J, Hui R. Mutations profile in Chinese patients with hypertrophic cardiomyopathy. Clin Chim Acta. 2005 Jan;351(1-2):209-16. PMID:15563892 doi:10.1016/j.cccn.2004.09.016
↑ Hougs L, Havndrup O, Bundgaard H, Kober L, Vuust J, Larsen LA, Christiansen M, Andersen PS. One third of Danish hypertrophic cardiomyopathy patients with MYH7 mutations have mutations [corrected] in MYH7 rod region. Eur J Hum Genet. 2005 Feb;13(2):161-5. PMID:15483641 doi:10.1038/sj.ejhg.5201310
↑ Yu B, Sawyer NA, Caramins M, Yuan ZG, Saunderson RB, Pamphlett R, Richmond DR, Jeremy RW, Trent RJ. Denaturing high performance liquid chromatography: high throughput mutation screening in familial hypertrophic cardiomyopathy and SNP genotyping in motor neurone disease. J Clin Pathol. 2005 May;58(5):479-85. PMID:15858117 doi:10.1136/jcp.2004.021642
↑ Ingles J, Doolan A, Chiu C, Seidman J, Seidman C, Semsarian C. Compound and double mutations in patients with hypertrophic cardiomyopathy: implications for genetic testing and counselling. J Med Genet. 2005 Oct;42(10):e59. PMID:16199542 doi:10.1136/jmg.2005.033886
↑ Perrot A, Schmidt-Traub H, Hoffmann B, Prager M, Bit-Avragim N, Rudenko RI, Usupbaeva DA, Kabaeva Z, Imanov B, Mirrakhimov MM, Dietz R, Wycisk A, Tendera M, Gessner R, Osterziel KJ. Prevalence of cardiac beta-myosin heavy chain gene mutations in patients with hypertrophic cardiomyopathy. J Mol Med. 2005 Jun;83(6):468-77. Epub 2005 Apr 22. PMID:15856146 doi:10.1007/s00109-005-0635-7
↑ Tanjore RR, Sikindlapuram AD, Calambur N, Thakkar B, Kerkar PG, Nallari P. Genotype-phenotype correlation of R870H mutation in hypertrophic cardiomyopathy. Clin Genet. 2006 May;69(5):434-6. PMID:16650083 doi:10.1111/j.1399-0004.2006.00599.x
↑ Mora R, Merino JL, Peinado R, Olias F, Garcia-Guereta L, del Cerro MJ, Tarin MN, Molano J. [Hypertrophic cardiomyopathy: infrequent mutation of the cardiac beta-myosin heavy-chain gene] Rev Esp Cardiol. 2006 Aug;59(8):846-9. PMID:16938236
↑ Tajsharghi H, Oldfors A, Macleod DP, Swash M. Homozygous mutation in MYH7 in myosin storage myopathy and cardiomyopathy. Neurology. 2007 Mar 20;68(12):962. PMID:17372140 doi:10.1212/01.wnl.0000257131.13438.2c
↑ Morita H, Rehm HL, Menesses A, McDonough B, Roberts AE, Kucherlapati R, Towbin JA, Seidman JG, Seidman CE. Shared genetic causes of cardiac hypertrophy in children and adults. N Engl J Med. 2008 May 1;358(18):1899-908. doi: 10.1056/NEJMoa075463. Epub 2008, Apr 9. PMID:18403758 doi:10.1056/NEJMoa075463
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