2009 Vienna - European Society of Human Genetics

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Molecular basis of Mendelian disorders P12.086 Genetic heterogeneity of hereditary neuropathy with liability to pressure palsies at the Russian patients O. A. Schagina, T. B. Tiburkova, E. L. Dadali, G. E. Rudenskaya, A. V. Polyakov; Research centre for medical genetics RAMS, Moscow, Russian Federation. Hereditary neuropathy with liability to pressure palsies (HNPP) is an autosomal dominant painless peripheral neuropathy characterized by episodes of repeated focal pressure neuropathies at sites of entrapment/compression, with a considerable variability in the clinical course. Forty patients and twenty one healthy members from 26 unrelated families with a clinical history and examination suggestive of HNPP were observed. In 9 families HNPP were due to the common 1.5 Mb deletion. This mutation was detected on the basis of a PCR result that demonstrated loss of heterozygosity for each of four polymorphic markers in 17p11.2-12 region. Multiplex Ligation-dependent Probe Analysis (MLPA) was carried out for all patients and family members using a probes were designed to evaluate all PMP22 coding exons and five control genes: TBP, SIRT3, USP3, B2M and EEF. Disease-cause deletion was found at the three more unrelated families. At the three cases deletion de novo was the reason of disease and in the others families mutation persistence at several generations. At one patient the disease-cause duplication of 17p11.2-12 region were detect. In the absence of the deletion/duplication direct sequence analysis of the all PMP22 coding exons 2-5, including their intron/exon boundaries was undertaken. One c.353C>T (Thr118Met) the previously described mutation in a heterozygotic condition and one new mutation c.75_78+2delCAGCgt were detected in two families. Thereby exciting cause was found in total at 15 from 26 unrelated families. In summary, we were able to detect genetic lesions in over 60% of HNPP patients from Russia. P12.087 Huntington disease pathogenesis: molecular biomarker/s in human peripheral blood and clonally striata-derived rat cells R. I. Lonigro1 , E. Bregant1 , L. Temil1 , F. Marcuzzi1 , N. Passon1 , G. Siciliano2 , E. Unti2 , G. Damante1 ; 1Department of Science and Biomedical Technologies, University of Udine, Udine, Italy, 2Neuroscience Department, University of Pisa, Pisa, Italy. Huntington disease (HD) is an inherited neurodegenerative disease characterized by chorea and psychiatric disturbance. It is caused by the expansion of CAG repeats in the first exon of the gene encoding huntingtin (Htt). Normal people have a polymorphic repeat, up to 36 CAG, encoding for glutamine (Gln). The mutant protein, with a longer poly-Q tract, becomes harmful to cells, particularly to cortical and striatal neurons. Mutant Htt affects many cellular processes, calcium homeostasis and mitochondrial dysfunction between others, still investigated to unveil their cause and effect relationship. An important tool for HD management could be the identification of molecular markers related to disease progression, in syntomatic and pre-symptomatic people, useful to draw early therapeutic treatments. By using quantitative RT-PCR we investigate the expression level of genes involved in calcium homeostasis in the peripheral blood of HD subjects and ageand gender- matched healthy controls. The genes selected for this study were: a purinergic receptor, P2RY5, and three calcium pumps, SERCA2, SERCA3 and PMCA1. The results we obtained demonstrate that, with respect to the controls HD patients display: 1) similar levels of SERCA3 and PMCA1 mRNAs. 2) a significant reduction of P2RY5 mRNA level, in an age-related progression. 3) a significant reduction of SERCA2 mRNA level at all ages. Furthermore, we propose SERCA2 reduction as an early event in HD pathogenesis, since this pump is down-regulated at the protein level in clonally striata-derived rat cells expressing a doxycycline-inducible mutant Htt. P12.088 Huntington disease pathogenesis: molecular biomarker/s in human peripheral blood and clonally striata-derived rat cells R. I. Lonigro 1 , E. Bregant 1 , L. Temil 1 , F. Marcuzzi 1 , N. Passon 1 , G. Siciliano 2 , E. Unti 2 , G. Damante 1 ; 1 University, Udine, Italy, 2 University, Neuroscience Department, Pisa, Italy. Huntington disease (HD) is an inherited neurodegenerative disease characterized by chorea and psychiatric disturbance. It is caused by the expansion of CAG repeats in the first exon of the gene encoding huntingtin (Htt). Normal people have a polymorphic repeat, up to 36 CAG, encoding for glutamine (Gln). The mutant protein, with a longer poly-Q tract, becomes harmful to cells, particularly to cortical and striatal neurons. Mutant Htt affects many cellular processes, calcium homeostasis and mitochondrial dysfunction between others, still investigated to unveil their cause and effect relationship. An important tool for HD management could be the identification of molecular markers related to disease progression, in syntomatic and pre-symptomatic people, useful to draw early therapeutic treatments. By using quantitative RT-PCR we investigate the expression level of genes involved in calcium homeostasis in the peripheral blood of HD subjects and age- and gender- matched healthy controls. The genes selected for this study were: a purinergic receptor, P2RY5, and three calcium pumps, SERCA2, SERCA3 and PMCA1. The results we obtained demonstrate that, with respect to the controls HD patients display: 1) similar levels of SERCA3 and PMCA1 mRNAs. 2) a significant reduction of P2RY5 mRNA level, in an age-related progression. 3) a significant reduction of SERCA2 mRNA level at all ages. Furthermore, we propose SERCA2 reduction as an early event in HD pathogenesis, since this pump is down-regulated at the protein level in clonally striata-derived rat cells expressing a doxycycline-inducible mutant Htt. P12.089 Exclusion of trinucleotide repeat expansions in JPH3 gene causing disease in italian patients with Huntington-like phenotype A. Patitucci, A. Magariello, T. Sprovieri, L. Citrigno, C. Ungaro, A. L. Gabriele, F. L. Conforti, R. Mazzei, M. Muglia; Institute of Neurological Sciences, CNR, Mangone (CS), Italy. Huntington disease-like 2 (HDL2) is a rare autosomal dominant disorder of the nervous system, apparently indistinguishable from Huntington disease (HD). HDL2 belongs to a group of HDL disorders, also including Huntington disease-like 1 (HDL1), an autosomal dominant disease caused by an extra octapeptide repeat in the prion protein gene (PRNP), on chromosome 20p12; and Huntington disease-like 3 (HDL3), an autosomal recessive disease, mapped to 4p15.3. Furthermore, dentatorubral-pallidoluysian atrophy (DRPLA) and spinocerebellar ataxia type 17 (SCA17), may also have overlapping symptoms with HD. HDL2 is caused by the expansion above 40 CAG repeats, in a variably spliced exon of the junctophilin-3 gene (JPH3), on chromosome 16q24.3. The pathogenic mechanism underlying HDL2 remains unknown. Different JPH3 transcripts caused by alternative splicing and different polyadenylation sites have been described. To date, the expansion in JPH3 gene has been found only in patients with African ancestry. A very recent paper reports the first HDL2 case with an apparent European ancestry. In order to find a new founder effect on Caucasian population, we performed a mutational analysis in JPH3 gene in 132 Italian patients negative for HD disease. All patients tested were negative for the expansion on JPH3 according to the available data on Polish, Yugoslavian and Portuguese populations. Further investigations for HDL1 and HDL3 forms, as well as DRPLA and SCA17, will be performed on our patients. However, the diagnosis of HDL2 should always be considered, regardless of the apparent origin of the family, particularly in populations of mixed ancestry. P12.090 PcR of (cAG)n repeats in Bulgarian Huntington Horea patients A. Todorova 1 , T. Todorov 1 , B. Georgieva 1 , A. Kirov 1 , L. Angelova 2 , S. Kalenderova 1 , V. Mitev 1 ; 1 Department of Medical Chemistry and Biochemistry, Medical University, Sofia, Bulgaria, 2 Laboratory of Medical Genetics, Medical University, Varna, Bulgaria. Huntington disease (HD) is an autosomal dominant neurodegenerative disorder that gives rise to progressive, selective (localized) neural cell death associated with choreic movements, rigidity and dementia frequently associated with seizures. The disease is associated with increases in the length of a CAG triplet repeat in IT15 gene called ‘huntingtin’ located on chromosome 4p16.3. The normal size of the CAG triplet of the HD is ≤35 repeats, the pathological number of the CAG triplet is larger than 36 repeats with different penetrance (36-39 repeats -
Molecular basis of Mendelian disorders We developed a new PCR protocol for precise calculation of (CAG)n repeats using high betaine concentration. The amplification products were separated by capillary electrophoresis on ABI 310 genetic analyzer (Applied Biosystems). Using this protocol the CAG triple repeats could be precisely measured by size. We analyzed 12 individuals from 5 unrelated Huntington families. Seven individuals were found to be affected. The expanded fragments were measured to have 39, 41, 42, 43, 46 and 49 CAG repeats respectively. In all families the CAG triplet expands further in the next generation. The proposed diagnostic method is very fast, cheap and easy to perform, which makes it very useful in routine laboratory work. It can totally substitute the utilized so far Southern blot analysis P12.091 structural analysis of the huntingtin protein N. Ersoy, N. H. Aydogan Catik; Halic University, Department of Molecular Biology and Genetics, Istanbul, Turkey. Huntington’s Disease (HD) is an autosomal dominant neurodegenerative disorder. The mutation underlying HD is the expansion of the polymorphic CAG tract in the first exon. Despite intensive research, molecular pathology of HD has not been fully understood. In this study, threading method is used is to model the huntingtin protein. By using the VMD programme, various glutamine expansion mutations are created and changes in the protein structures are analyzed. The most convenient five models of huntingtin indicated the dominance of α-helices. Where α-helices are less common, long turns, coils and β-sheets are recognized. In addition to that, mutant proteins with expanded glutamines are created in silico and their structures are compared to the most probable huntingtin structure, 1WA5_B. According to the results, mutant proteins with 33-38Q did not show any significant change, however 39 or more glutamines caused conformational changes like lengthened and increased turns and coils and shortened α-helices. In this situation, protein may gain non-covalent interactions within itself or with other proteins and aggregate in the form of twisted β-sheets. These changes may render the protein more prone to proteolysis. In this way, toxic protein fragments carrying the glutamine tract are favored. On the other hand, usual proteolysis may not take place, which may cause toxicity by increasing the half life of the protein. Also, conformational change may lead to misfolding and aggregation of the proteolysis-resistant protein in the cell. Thus, conformational changes in the mutant huntingtin give some clues about the neurodegenerative pathways in HD. P12.092 somatic instability of cAG repeats in Huntington‘s Disease: role of oxidative DNA damage and Base Excision Repair A. Goula 1 , D. Wilson 2 , Y. Trottier 1 , K. Merienne 1 ; 1 IGBMC, Strasbourg, France, 2 NIA/NIH, Baltimore, MD, United States. Huntington’s disease (HD) is a neurodegenerative disorder, caused by CAG repeats extension encoding a toxic polyglutamine expansion in the huntingtin protein. Instability of the HD mutation leads to age-dependent and tissue-specific somatic expansion. Interestingly, the brain region preferentially degenerating, the striatum, is highly unstable, while the disease-spared cerebellum is rather stable. Recently, the glycosylase Ogg1, which initiates Base Excision Repair (BER), was shown to promote somatic instability, suggesting that oxidative DNA damage and BER drive this process. We show that oxidative DNA damage is specifically increased at the CAG-expanded locus in R6/1 HD mice. Surprisingly, levels of oxidative lesions are similar in striatum and cerebellum, and in young and aged tissues. Thus, accumulation of oxidative lesions at the CAG repeats is neither tissue- nor age-dependent, indicating that oxidative DNA damage at the CAG-expanded locus is necessary but not sufficient to trigger somatic instability. Protein levels and activities of major BER players were analyzed in the striatum and in the cerebellum of R6/1 mice. We show in particular that FEN1, the flappy endonuclease involved in Long-Patch BER (LP-BER) subpathway, is much less active in the striatum than in the cerebellum of R6/1 mice. Using chromatin immunoprecipitation, we finally show that POLβ is specifically enriched at the CAG-expanded locus in the striatum of aged R6/1 mice, but not in their cerebellum. This supports that LP-BER triggers somatic CAG expansion in the aging striatum, the inappropriate stoichiometry of POLβ and FEN1 resulting in poor coordination of polymerase strand displacement and flappy endonuclease activities. P12.093 sporadic in Utero Generalized Edema caused by mutations in the Lymphangiogenic Genes VEGFR3 and FOXc2 A. Mendola 1 , A. Ghalamkarpour 1 , C. Debauche 2 , E. Haan 3 , N. Van Regemorter 4 , Y. Sznajer 5 , D. Thomas 6 , N. Revencu 1 , Y. Gillerot 7 , L. Boon 8 , M. Vikkula 1 ; 1 Laboratory of Human Molecular Genetics, de Duve Institute, UCL, Brussels, Belgium, 2 Department of Neonatalogy, Cliniques universitaires Saint-Luc, Brussels, Belgium, 3 Women’s and Children’s Hospital and Department of Paediatrics, University of Adelaide, North Adelaide, Australia, 4 Centre de Génétique ULB, Hôpital Erasme, Brussels, Belgium, 5 Centre de Génétique ULB, Hôpital Erasme and Unité de Génétique Clinique Pédiatrique, ULB, Brussels, Belgium, 6 Unité de diagnostic anténatal, Hôpitaux Iris Sud, Brussels, Belgium, 7 Center for Human Genetics, Cliniques universitaires Saint-Luc, Brussels, Belgium, 8 Laboratory of Human Molecular Genetics, de Duve Institute, UCL and Centre for Vascular Anomalies, Cliniques universitaires Saint-Luc, Brussels, Belgium. Hydrops fetalis is a serious fetal condition with high mortality rate. It is mostly sporadic; the etiology is unknown in about 25% of cases. In this study, we investigated the genetic causes of idiopathic sporadic prenatal generalized edema. In a series of 12 patients, in whom in utero generalized skin edema or hydrops fetalis had been diagnosed, three lymphangiogenic genes, VEGFR3, FOXC2 and SOX18, were screened. In three of the patients, we identified a mutation: two in VEGFR3 and one in FOXC2. Two of the mutations were de novo and one was either de novo or non-penetrant inherited. In these patients, the generalized edema resorbed spontaneously, either in utero or after birth. In the two individuals with a VEGFR3 mutation, edema remained limited to lower limbs. Therefore, mutations in the VEGFR3 and FOXC2 genes account for a subset of patients with unexplained in utero generalized subcutaneous edema and hydrops fetalis without family history of lymphedema. These data expand our understanding of the etiology of these phenotypes and suggest that lymphangiogenic genes should be screened for mutations in sporadic patients diagnosed with fetal edema. P12.094 Hyperferritinémia and mutations in the promoter of HAmP S. Pissard1,2 , V. Koubi1 , F. Houriez1 , G. Legac3,4 ; 1 2 aphp, Hop H. mondor, Creteil, France, University Paris 12, Creteil, France, 3 4 Inserm U613, Brest, France, EFS, chu de Brest, Brest, France. Hepcidin (gene HAMP , 19q13) is a protein which is supposed to regulate iron uptake or recycling through binding to the iron export protein : the ferroportin (gene SLC 40 A1, 2q32).It is secreted by the liver and considered as a key iron-regulatory hormone linking the liver’s “iron sensor” to bowel absorption. High iron storage induce the expression of hepcidin and thus the decrease of absorption. The Molecular defects of its gene are associated with a class of hyperferritinemia called hemochromatosis type 2b (OMIM : 606464). We have screened the HAMP gene in patients displaying abnormal iron parameters not linked to a mutation in HFE or SCL40 A1 genes. We found two new mutations in the promoter : c. -153 C>G and c. -188 C>T. The first variant affects a binding site for BMP which was described to control hepcidin promoter activation. Functional studies of other mutations located in this binding site confirmed its’ functional importance (G. Legac and J. Rochette, personal communication).The second one was found several time in patients originated from Africa and screened for iron metabolism disorders. As it was recently published [J. Mol Med, (2008) 86:531-540], the proximal part of the promoter plays a crucial role in the regulation of hepcidin expression. These observations could represent natural variants of hepcidin expression allowing to understand the regulation pathway of this gene and consequences of its perturbation. Functional study of the second mutation is ongoing P12.095 Probing the oligogenic nature of idiopathic chronic pancreatitis: first analysis of five susceptibility genes in a large cohort of young patients E. Masson 1,2 , J. M. Chen 1,3,4 , M. P. Audrézet 1,2 , A. Dabricot 2 , V. Scotet 1,4 , C. Le Maréchal 1,2,4 , C. Férec 1,2,4 ; 1 Institut National de la Santé et de la Recherche Médicale (INSERM), U613, Brest, France, 2 Centre Hospitalier Universitaire (CHU) Brest, Hôpital Morvan,
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Volume 17 Supplement 2 May 2009 www
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European Society of Human Genetics
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Table of Contents spoken Presentati
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Plenary Lectures PL2.2 massive para
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Concurrent Symposia s01.1 Genome va
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Concurrent Symposia Monogenic diabe
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Concurrent Symposia invariable in t
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Concurrent Symposia s11.2 clinical,
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Concurrent Symposia s13.2 A novel g
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Concurrent Sessions c01.1 mRNA-seq
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Concurrent Sessions velopmental del
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Concurrent Sessions development of
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Concurrent Sessions c04.6 Duplicati
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Concurrent Sessions genes to be rec
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Concurrent Sessions c07.5 Prenatal
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Concurrent Sessions with familial h
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Concurrent Sessions University of W
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Concurrent Sessions with this, we f
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Concurrent Sessions had immotile ci
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Concurrent Sessions abnormal glycos
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Concurrent Sessions showers’ and
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Concurrent Sessions partial gene de
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Concurrent Sessions leads to distre
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Genetic counseling Genetics educati
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Clinical genetics and Dysmorphology
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Cytogenetics P03. cytogenetics Recu
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Cytogenetics use of metaphase analy
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Cytogenetics 2: mother’s age < fa
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Cytogenetics P03.028 HLA B27 allele
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Cytogenetics karyotype revealed a p
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Cytogenetics drome is estimated at
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Cytogenetics P03.057 Pathological c
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Cytogenetics grandmother and 2 mate
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Cytogenetics method used to detect
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Cytogenetics P03.082 High-resolutio
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Cytogenetics All detected anomalies
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Cytogenetics somy for chromosome 2.
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Cytogenetics cially in chromosome 4
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Cytogenetics (59.390.122 to 62.021.
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Cytogenetics For further characteri
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Cytogenetics 9p duplication. This c
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Cytogenetics regions with mental /d
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Cytogenetics donation program of po
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Cytogenetics P03.165 interpretation
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Cytogenetics P03.174 Deletion of th
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Cytogenetics P03.183 An atypical 7q
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Cytogenetics spermia, 11 oligosperm
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Reproductive genetics and social fa
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Reproductive genetics mosomal chang
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Reproductive genetics two cohorts w
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Reproductive genetics the 147 SC ch
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Prenatal and perinatal genetics P05
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Prenatal and perinatal genetics and
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Prenatal and perinatal genetics fro
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Prenatal and perinatal genetics dev
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Prenatal and perinatal genetics in
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Prenatal and perinatal genetics obj
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Prenatal and perinatal genetics P05
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Cancer genetics P06.005 tiling reso
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Cancer genetics tient group in whic
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Cancer genetics chronic inflammatio
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Cancer genetics licular thyroid can
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Cancer genetics also studied. In 31
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Cancer genetics tile polyposis. We
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Cancer genetics Upon recombinant ex
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Cancer genetics variant allele was
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Cancer genetics from patients with
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Cancer genetics tion (PAX5 and GATA
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Cancer genetics scribed underexpres
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Cancer genetics of the ZIC gene fam
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Cancer genetics Materials and metho
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Cancer genetics the past and it is
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Cancer genetics P06.130 spectrum an
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Cancer genetics P06.139 the role of
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Cancer genetics and MSH2 germline m
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Cancer genetics P06.155 New roles f
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Cancer genetics screening was perfo
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Cancer genetics val (DFI) than pati
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Cancer genetics is hTERC gene ampli
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Cancer genetics on chromosome regio
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Cancer genetics preferentially dupl
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Cancer cytogenetics mutations in co
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Cancer cytogenetics P07.08 molecula
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Statistical genetics, includes Mapp
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Complex traits and polygenic disord
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Evolutionary and population genetic
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Page 281 and 282: Evolutionary and population genetic
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Page 285 and 286: Genomics, Genomic technology and Ep
Page 313 and 314: Molecular basis of Mendelian disord
Page 331: Molecular basis of Mendelian disord
Page 351 and 352: Metabolic disorders P12.167 Pattern
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Page 363 and 364: Therapy for genetic disorders in th
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Page 369 and 370: Laboratory and quality management P
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Molecular and biochemical basis of
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Genetic analysis, linkage ans assoc
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Author Index Allanson, J.: P02.140
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Author Index 0 Barbacioru, C.: C01.
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Author Index 0 Bonneau, D.: C16.2,
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Author Index 0 Chakravarti, A.: C13
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Author Index 0 Dan, D.: P01.39, P14
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Author Index 0 Duskova, J.: P06.012
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Author Index Franke, A.: P09.056 Fr
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Author Index Grasso, R.: P02.025 Gr
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Author Index Holder-Espinasse, M.:
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Author Index Jurkiewicz, E.: C14.5
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Author Index Kooper, A. J. A.: P05.
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Author Index Li, K. J.: P11.086 Li,
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Author Index Martinet, D.: P03.095
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Author Index Moorman, A. F. M.: P16
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Author Index P10.57, P10.82 Oguzkan
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Author Index P09.054, P09.085, P09.
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Author Index P16.01 Renieri, A.: P0
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Author Index Santorelli, F.: P08.55
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Author Index Sinke, R. J.: P02.020
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Author Index Taheri, M.: P04.33, P0
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Author Index Valentino, P.: P02.064
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Author Index Wiemer-Kruel, A.: P14.
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Keyword Index 1 10q22 deletions: P0
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Keyword Index autosomal dominant re
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Keyword Index CLA: P06.073 CLCN1 ge
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Keyword Index DMD: P16.40, P16.41,
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Keyword Index gene networks: S12.2
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Keyword Index hydrocephaly: P05.11
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Keyword Index malignant hyperthermi
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Keyword Index NAT2: P12.118 natridi
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Keyword Index Polymalformations: P0
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Keyword Index Sardinia: C09.6 Sardi
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Keyword Index TNFalpha: P08.61, P09
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