@article {3550,
	title = {Mutations of cytochrome c identified in patients with thrombocytopenia THC4 affect both apoptosis and cellular bioenergetics.},
	journal = {Biochim Biophys Acta},
	volume = {1842},
	year = {2014},
	month = {2014 Feb},
	pages = {269-74},
	abstract = {<p>Inherited thrombocytopenias are heterogeneous diseases caused by at least 20 genes playing different role in the processes of megakaryopoiesis and platelet production. Some forms, such as thrombocytopenia 4 (THC4), are very rare and not well characterized. THC4 is an autosomal dominant mild thrombocytopenia described in only one large family from New Zealand and due to a mutation (G41S) of the somatic isoform of the cytochrome c (CYCS) gene. We report a novel CYCS mutation (Y48H) in patients from an Italian family. Similar to individuals carrying G41S, they have platelets of normal size and morphology, which are only partially reduced in number, but no prolonged bleeding episodes. In order to determine the pathogenetic consequences of Y48H, we studied the effects of the two CYCS mutations in yeast and mouse cellular models. In both cases, we found reduction of respiratory level and increased apoptotic rate, supporting the pathogenetic role of CYCS in thrombocytopenia.</p>},
	keywords = {Amino Acid Sequence, Animals, Apoptosis, Base Sequence, Cells, Cultured, Child, Preschool, Cytochromes c, DNA Mutational Analysis, Embryo, Mammalian, Energy Metabolism, Family Health, Female, Fibroblasts, Humans, Lung, Male, Mice, Molecular Sequence Data, Mutation, Missense, Oxygen Consumption, Pedigree, Saccharomyces cerevisiae, Sequence Homology, Amino Acid, Thrombocytopenia},
	issn = {0006-3002},
	doi = {10.1016/j.bbadis.2013.12.002},
	author = {De Rocco, Daniela and Cerqua, Cristina and Goffrini, Paola and Russo, Giovanna and Pastore, Annalisa and Meloni, Francesca and Nicchia, Elena and Moraes, Carlos T and Pecci, Alessandro and Salviati, Leonardo and Savoia, Anna}
}
@article {1993,
	title = {MYH9-related disease: five novel mutations expanding the spectrum of causative mutations and confirming genotype/phenotype correlations.},
	journal = {Eur J Med Genet},
	volume = {56},
	year = {2013},
	month = {2013 Jan},
	pages = {7-12},
	abstract = {<p>MYH9-related disease (MYH9-RD) is a rare autosomal dominant syndromic disorder caused by mutations in MYH9, the gene encoding for the heavy chain of non-muscle myosin IIA (myosin-9). MYH9-RD is characterized by congenital macrothrombocytopenia and typical inclusion bodies in neutrophils associated with a variable risk of developing sensorineural deafness, presenile cataract, and/or progressive nephropathy. The spectrum of mutations responsible for MYH9-RD is limited. We report five families, each with a novel MYH9 mutation. Two mutations, p.Val34Gly and p.Arg702Ser, affect the motor domain of myosin-9, whereas the other three, p.Met847_Glu853dup, p.Lys1048_Glu1054del, and p.Asp1447Tyr, hit the coiled-coil tail domain of the protein. The motor domain mutations were associated with more severe clinical phenotypes than those in the tail domain.</p>},
	keywords = {Adolescent, Adult, Amino Acid Sequence, Amino Acid Substitution, Base Sequence, Child, Child, Preschool, Exons, Female, Genes, Dominant, Genetic Association Studies, Humans, Male, Middle Aged, Models, Molecular, Molecular Motor Proteins, Molecular Sequence Data, Mutation, Myosin Heavy Chains, Pedigree, Protein Conformation, Sequence Alignment, Syndrome, Thrombocytopenia, Young Adult},
	issn = {1878-0849},
	doi = {10.1016/j.ejmg.2012.10.009},
	author = {De Rocco, Daniela and Zieger, Barbara and Platokouki, Helen and Heller, Paula G and Pastore, Annalisa and Bottega, Roberta and Noris, Patrizia and Barozzi, Serena and Glembotsky, Ana C and Pergantou, Helen and Balduini, Carlo L and Savoia, Anna and Pecci, Alessandro}
}
