M. Brooke, Congenital fiber type disproportion Clinical studies in myology, Proceedings of the 2nd International Congress on Muscle Diseases, pp.147-159, 1971.

N. Clarke and K. North, Congenital Fiber Type Disproportion???30 Years On, Journal of Neuropathology & Experimental Neurology, vol.62, issue.10, pp.977-989, 2003.
DOI : 10.1093/jnen/62.10.977

C. Imoto and I. Nonaka, The significance of type 1 fiber atrophy (hypotrophy) in childhood neuromuscular disorders, Brain and Development, vol.23, issue.5, pp.298-302, 2001.
DOI : 10.1016/S0387-7604(01)00213-3

N. Laing, N. Clarke, and D. Dye, Actin mutations are one cause of congenital fibre type disproportion, Annals of Neurology, vol.400, issue.5, pp.689-694, 2004.
DOI : 10.1002/ana.20260

N. Clarke, R. Smith, and M. Bahlo, A novel X-linked form of congenital fiber-type disproportion, Annals of Neurology, vol.85, issue.5, pp.767-772, 2005.
DOI : 10.1002/ana.20644

N. Clarke, W. Kidson, and S. Quijano-roy, : Associated with congenital fiber-type disproportion and insulin resistance, Annals of Neurology, vol.61, issue.3, pp.546-552, 2006.
DOI : 10.1002/ana.20761

N. Laing, S. Wilton, and P. Akkari, A mutation in the ?? tropomyosin gene TPM3 associated with autosomal dominant nemaline myopathy, Nature Genetics, vol.328, issue.1, pp.75-79, 1995.
DOI : 10.1038/ng0195-75

K. Donner, M. Ollikainen, and M. Ridanpaa, Mutations in the ??-tropomyosin (TPM2) gene ??? a rare cause of nemaline myopathy, Neuromuscular Disorders, vol.12, issue.2, pp.151-158, 2002.
DOI : 10.1016/S0960-8966(01)00252-8

S. Sung, A. Brassington, and K. Grannatt, Mutations in Genes Encoding Fast-Twitch Contractile Proteins Cause Distal Arthrogryposis Syndromes, The American Journal of Human Genetics, vol.72, issue.3, pp.681-690, 2003.
DOI : 10.1086/368294

V. Lehtokari, C. Ceuterick-de-groote, and P. De-jonghe, Cap disease caused by heterozygous deletion of the ??-tropomyosin gene TPM2, Neuromuscular Disorders, vol.17, issue.6, pp.433-442, 2007.
DOI : 10.1016/j.nmd.2007.02.015

L. Thierfelder, H. Watkins, and C. Macrae, ??-tropomyosin and cardiac troponin T mutations cause familial hypertrophic cardiomyopathy: A disease of the sarcomere, Cell, vol.77, issue.5, pp.701-712, 1994.
DOI : 10.1016/0092-8674(94)90054-X

N. Laing, B. Majda, and P. Akkari, Assignment of a gene (NEMI) for autosomal dominant nemaline myopathy to chromosome I, Am J Hum Genet, vol.50, pp.576-583, 1992.

P. Tan, J. Briner, and E. Boltshauser, Homozygosity for a nonsense mutation in the alpha-tropomyosin slow gene TPM3 in a patient with severe infantile nemaline myopathy, Neuromuscular Disorders, vol.9, issue.8, pp.573-579, 1999.
DOI : 10.1016/S0960-8966(99)00053-X

H. Durling, P. Reilich, and J. Muller-hocker, De novo missense mutation in a constitutively expressed exon of the slow alpha-tropomyosin gene TPM3 associated with an atypical, sporadic case of nemaline myopathy, Neuromuscular Disorders, vol.12, issue.10, pp.947-951, 2002.
DOI : 10.1016/S0960-8966(02)00182-7

D. Wattanasirichaigoon, K. Swoboda, and F. Takada, Mutations of the slow muscle ??-tropomyosin gene, TPM3, are a rare cause of nemaline myopathy, Neurology, vol.59, issue.4, pp.613-617, 2002.
DOI : 10.1212/WNL.59.4.613

I. Penisson-besnier, N. Monnier, and A. Toutain, A second pedigree with autosomal dominant nemaline myopathy caused by TPM3 mutation: A clinical and pathological study, Neuromuscular Disorders, vol.17, issue.4, pp.330-337, 2007.
DOI : 10.1016/j.nmd.2007.01.017
URL : https://hal.archives-ouvertes.fr/inserm-00381952

F. Whitby, G. Phillips, and . Jr, Crystal structure of tropomyosin at 7 ??ngstroms resolution, Proteins: Structure, Function, and Genetics, vol.38, issue.1, pp.49-59, 2000.
DOI : 10.1002/(SICI)1097-0134(20000101)38:1<49::AID-PROT6>3.3.CO;2-2

J. Den-dunnen and S. Antonarakis, Nomenclature for the description of human sequence variations, Human Genetics, vol.109, issue.1, pp.121-124, 2001.
DOI : 10.1007/s004390100505

C. Vogler and K. Bove, Morphology of skeletal muscle in children. An assessment of normal growth and differentiation, Arch Pathol Lab Med, vol.109, pp.238-242, 1985.

G. Oertel, Morphometric analysis of normal skeletal muscles in infancy, childhood and adolescence, Journal of the Neurological Sciences, vol.88, issue.1-3, pp.303-313, 1988.
DOI : 10.1016/0022-510X(88)90227-4

K. Wagschal, B. Tripet, and P. Lavigne, The role of position a in determining the stability and oligomerization state of ??-helical coiled coils: 20 amino acid stability coefficients in the hydrophobic core of proteins, Protein Science, vol.2, issue.11, pp.2312-2329, 1999.
DOI : 10.1110/ps.8.11.2312

B. Tripet, K. Wagschal, and P. Lavigne, Effects of side-chain characteristics on stability and oligomerization state of a de Novo-designed model coiled-coil: 20 amino acid substitutions in position ???d???, Journal of Molecular Biology, vol.300, issue.2, pp.377-402, 2000.
DOI : 10.1006/jmbi.2000.3866

N. Clarke, B. Ilkovski, and S. Cooper, The pathogenesis ofACTA1-related congenital fiber type disproportion, Annals of Neurology, vol.62, issue.6, pp.552-561, 2007.
DOI : 10.1002/ana.21112

D. Bronson and F. Schachat, Heterogeneity of contractile proteins Differences in tropomyosin in fast, mixed, and slow skeletal muscles of the rabbit, J Biol Chem, vol.257, pp.3937-3944, 1982.

S. Lu and R. Hodges, Defining the minimum size of a hydrophobic cluster in two-stranded ??-helical coiled-coils: Effects on protein stability, Protein Science, vol.13, issue.3, pp.714-726, 2004.
DOI : 10.1110/ps.03443204

M. Corbett, P. Akkari, and A. Domazetovska, An ?tropomyosin mutation alters dimer preference in nemaline myopathy, Annals of Neurology, vol.271, issue.1, pp.42-49, 2005.
DOI : 10.1002/ana.20305

J. Brown, Z. Zhou, and L. Reshetnikova, Structure of the mid-region of tropomyosin: Bending and binding sites for actin, Proceedings of the National Academy of Sciences, vol.102, issue.52, pp.18878-18883, 2005.
DOI : 10.1073/pnas.0509269102