Search Results - "Mutation physiology"

1

KDM3A coordinates actin dynamics with intraflagellar transport to regulate cilia stability

Authors: Yeyati, Patricia L., Schiller, Rachel, Mali, Girish, Kasioulis, Ioannis, Kawamura, Akane, Adams, Ian R., Playfoot, Christopher, Gilbert, Nick, van Heyningen, Veronica, Wills, Jimi, von Kriegsheim, Alex, Finch, Andrew, Sakai, Juro, Schofield, Christopher J., Jackson, Ian J., Mill, Pleasantine

Source: Yeyati, P L, Schiller, R, Mali, G, Kasioulis, I, Kawamura, A, Adams, I R, Playfoot, C, Gilbert, N, van Heyningen, V, Wills, J, von Kriegsheim, A, Finch, A, Sakai, J, Schofield, C J, Jackson, I J & Mill, P 2017, ' KDM3A coordinates actin dynamics with intraflagellar transport to regulate cilia stability ', The Journal of cell biology, vol. 216, no. 4, pp. 999-1013 . https://doi.org/10.1083/jcb.201607032
The Journal of Cell Biology
Yeyati, P L, Schiller, R, Mali, G, Kasioulis, I, Kawamura, A, Adams, I R, Playfoot, C, Gilbert, N, van Heyningen, V, Wills, J, von Kriegsheim, A, Finch, A, Sakai, J, Schofield, C J, Jackson, I J & Mill, P 2017, ' KDM3A coordinates actin dynamics with intraflagellar transport to regulate cilia stability ', Journal of Cell Biology, vol. 216, no. 4, pp. 999-1013 . https://doi.org/10.1083/jcb.201607032

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https://hdl.handle.net/1983/99296957-df16-4da2-9a4a-5d8e37197796

2

Association of the M1VPRKAR1AMutation with Primary Pigmented Nodular Adrenocortical Disease in Two Large Families

Authors: Anelia Horvath, Eirini I. Bimpaki, Alberto M. Pereira, Constantine A. Stratakis, Johannes W. A. Smit, Elizabeth Greene, Johannes A. Romijn, Maria Nesterova, Sosipatros Boikos, Anton Alatsatianos, Sanne A. Woortman, Frederik J. Hes

Contributors: Clinical sciences, General Internal Medicine

Source: Journal of Clinical Endocrinology and Metabolism, 95(1), 338-342
Journal of clinical endocrinology and metabolism, 95(1), 338-342. The Endocrine Society

Subject Terms: Adrenal Cortex Diseases, Adult, Male, medicine.medical_specialty, Genetic Linkage, Cyclic AMP-Dependent Protein Kinase RIalpha Subunit, Endocrinology, Diabetes and Metabolism, Clinical Biochemistry, Point Mutation/physiology, Biology, medicine.disease_cause, Cyclic AMP-Dependent Protein Kinase RIalpha Subunit/genetics, Biochemistry, Adrenal Cortex Diseases/genetics, Methionine/genetics, Germline, Young Adult, Methionine, Endocrinology, Germline mutation, subunit type 1a dependent protein-kinase carney complex regulatory subunit cushings-syndrome a pka gene endocrine tumors tissues, Internal medicine, medicine, Humans, Point Mutation, Family, Genetic Predisposition to Disease, Amino Acid Substitution/genetics, Carney complex, PRKAR1A, Medicine(all), Mutation, Brief Report, Point mutation, Biochemistry (medical), Valine, Valine/genetics, Middle Aged, medicine.disease, Pedigree, Amino Acid Substitution, Mutation testing, Female, Primary pigmented nodular adrenocortical disease

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https://doi.org/10.1210/jc.2009-0993

3

Les mutations du gène TMEM240 provoquent l'ataxie spinocérébelleuse 21 avec un retard mental et des troubles cognitifs sévères

Contributors: Metabolic functional (epi)genomics and molecular mechanisms involved in type 2 diabetes and related diseases - UMR 8199 - UMR 1283 (EGENODIA (GI3M)), Institut Pasteur de Lille, Réseau International des Instituts Pasteur (RIIP)-Réseau International des Instituts Pasteur (RIIP)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Université de Lille-Centre National de la Recherche Scientifique (CNRS), Centre de Recherche Jean-Pierre AUBERT Neurosciences et Cancer - U837 (JPArc), Université Lille Nord de France (COMUE)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Université de Lille, Département de neurologie [Lille], Centre Hospitalier Régional Universitaire [Lille] (CHRU Lille), Centre de Biologie Pathologie [CHRU Lille] (Pôle de Pathologie), Maladies Rares - Génétique et Métabolisme (MRGM), Université Bordeaux Segalen - Bordeaux 2-Hôpital Pellegrin-Service de Génétique Médicale du CHU de Bordeaux, CHU Pitié-Salpêtrière [AP-HP], Assistance publique - Hôpitaux de Paris (AP-HP) (AP-HP)-Sorbonne Université (SU), Centre for Integrative Biology - CBI (Inserm U964 - CNRS UMR7104 - IGBMC), Institut de Génétique et de Biologie Moléculaire et Cellulaire (IGBMC), Université de Strasbourg (UNISTRA)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)-Université de Strasbourg (UNISTRA)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS), Departement de Neuroradiologie [Lille], Service de neuropédiatrie [CHU Lille], Institut du Cerveau = Paris Brain Institute (ICM), Assistance publique - Hôpitaux de Paris (AP-HP) (AP-HP)-Institut National de la Santé et de la Recherche Médicale (INSERM)-CHU Pitié-Salpêtrière [AP-HP], Assistance publique - Hôpitaux de Paris (AP-HP) (AP-HP)-Sorbonne Université (SU)-Sorbonne Université (SU)-Sorbonne Université (SU)-Centre National de la Recherche Scientifique (CNRS), École Pratique des Hautes Études (EPHE), Université Paris sciences et lettres (PSL), HESAM Université - Communauté d'universités et d'établissements Hautes écoles Sorbonne Arts et métiers université (HESAM), Metabolic functional (epi)genomics and molecular mechanisms involved in type 2 diabetes and related diseases - UMR 8199 - UMR 1283 (GI3M), Institut National de la Santé et de la Recherche Médicale (INSERM)-Université de Lille-Centre National de la Recherche Scientifique (CNRS)-Institut Pasteur de Lille, Réseau International des Instituts Pasteur (RIIP)-Réseau International des Instituts Pasteur (RIIP), Centre de Recherche Jean-Pierre AUBERT Neurosciences et Cancer - U1172 Inserm - U837 (JPArc), Institut National de la Santé et de la Recherche Médicale (INSERM)-Université Lille Nord de France (COMUE)-Université de Lille, Département de neurologie[Lille], Université de Lille, Droit et Santé-Centre Hospitalier Régional Universitaire [Lille] (CHRU Lille), Service de neurologie 1 [CHU Pitié-Salpétrière], Assistance publique - Hôpitaux de Paris (AP-HP) (AP-HP)-CHU Pitié-Salpêtrière [AP-HP], Assistance publique - Hôpitaux de Paris (AP-HP) (AP-HP)-Sorbonne Université (SU)-Sorbonne Université (SU), Service de Génétique Cytogénétique et Embryologie [CHU Pitié-Salpêtrière], Assistance publique - Hôpitaux de Paris (AP-HP) (AP-HP)-Sorbonne Université (SU)-Assistance publique - Hôpitaux de Paris (AP-HP) (AP-HP)-Sorbonne Université (SU), Institut du Cerveau et de la Moëlle Epinière = Brain and Spine Institute (ICM), Institut National de la Santé et de la Recherche Médicale (INSERM)-CHU Pitié-Salpêtrière [AP-HP], Assistance publique - Hôpitaux de Paris (AP-HP) (AP-HP)-Sorbonne Université (SU)-Assistance publique - Hôpitaux de Paris (AP-HP) (AP-HP)-Sorbonne Université (SU)-Sorbonne Université (SU)-Centre National de la Recherche Scientifique (CNRS), École pratique des hautes études (EPHE), HESAM Université (HESAM), HUIN, Vincent, Université de Lille-Centre Hospitalier Régional Universitaire [Lille] (CHRU Lille), Service de Neurologie [CHU Pitié-Salpêtrière], IFR70-CHU Pitié-Salpêtrière [AP-HP]

Source: Brain-A Journal of Neurology
Brain-A Journal of Neurology, 2014, 137 (10), pp.2657-2663. ⟨10.1093/brain/awu202⟩
Brain-A Journal of Neurology, Oxford University Press (OUP), 2014, 137 (10), pp.2657-2663. ⟨10.1093/brain/awu202⟩

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https://www.hal.inserm.fr/inserm-03017555/file/Delplanque.Brain.2014.Author.version.pdf

4

Les mutations du gène TMEM240 provoquent l'ataxie spinocérébelleuse 21 avec un retard mental et des troubles cognitifs sévères

Contributors: Metabolic functional (epi)genomics and molecular mechanisms involved in type 2 diabetes and related diseases - UMR 8199 - UMR 1283 (GI3M), Institut National de la Santé et de la Recherche Médicale (INSERM)-Université de Lille-Centre National de la Recherche Scientifique (CNRS)-Institut Pasteur de Lille, Réseau International des Instituts Pasteur (RIIP)-Réseau International des Instituts Pasteur (RIIP), Centre de Recherche Jean-Pierre AUBERT Neurosciences et Cancer - U1172 Inserm - U837 (JPArc), Institut National de la Santé et de la Recherche Médicale (INSERM)-Université Lille Nord de France (COMUE)-Université de Lille, Département de neurologie[Lille], Université de Lille, Droit et Santé-Centre Hospitalier Régional Universitaire [Lille] (CHRU Lille), Centre de Biologie Pathologie [CHRU Lille] (Pôle de Pathologie), Centre Hospitalier Régional Universitaire [Lille] (CHRU Lille), Maladies Rares - Génétique et Métabolisme (MRGM), Université Bordeaux Segalen - Bordeaux 2-Hôpital Pellegrin-Service de Génétique Médicale du CHU de Bordeaux, Service de Neurologie [CHU Pitié-Salpêtrière], IFR70-CHU Pitié-Salpêtrière [AP-HP], Sorbonne Université (SU)-Assistance publique - Hôpitaux de Paris (AP-HP) (AP-HP)-Sorbonne Université (SU)-Assistance publique - Hôpitaux de Paris (AP-HP) (AP-HP), Centre for Integrative Biology - CBI (Inserm U964 - CNRS UMR7104 - IGBMC), Institut de Génétique et de Biologie Moléculaire et Cellulaire (IGBMC), Université de Strasbourg (UNISTRA)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)-Université de Strasbourg (UNISTRA)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS), Service de Génétique Cytogénétique et Embryologie [CHU Pitié-Salpêtrière], CHU Pitié-Salpêtrière [AP-HP], Departement de Neuroradiologie [Lille], Service de neuropédiatrie [CHU Lille], Institut du Cerveau et de la Moëlle Epinière = Brain and Spine Institute (ICM), Institut National de la Santé et de la Recherche Médicale (INSERM)-CHU Pitié-Salpêtrière [AP-HP], Sorbonne Université (SU)-Assistance publique - Hôpitaux de Paris (AP-HP) (AP-HP)-Sorbonne Université (SU)-Assistance publique - Hôpitaux de Paris (AP-HP) (AP-HP)-Sorbonne Université (SU)-Centre National de la Recherche Scientifique (CNRS), École pratique des hautes études (EPHE), Université Paris sciences et lettres (PSL), HESAM Université (HESAM)

Source: Brain-A Journal of Neurology
Brain-A Journal of Neurology, Oxford University Press (OUP), 2014, 137 (10), pp.2657-2663. ⟨10.1093/brain/awu202⟩

Subject Terms: Cerebellum, MESH: Intellectual Disability / genetics, MESH: Introns, MESH: Exome / genetics, MESH: Amino Acid Sequence, MESH: Membrane Proteins / genetics, MESH: Spinocerebellar Degenerations / pathology, Autosomal dominant cerebellar ataxia, MESH: Child, Missense mutation, MESH: DNA Mutational Analysis, Exome, MESH: Spinocerebellar Degenerations / psychology, MESH: Cohort Studies, Exome sequencing, Genetics, MESH: Conserved Sequence, MESH: Membrane Proteins / physiology, MESH: Neuropsychological Tests, MESH: Cognition Disorders / psychology, MESH: Infant, 3. Good health, medicine.anatomical_structure, MESH: Young Adult, Spinocerebellar ataxia, medicine.symptom, MESH: Spinocerebellar Degenerations / genetics, MESH: Mutation / physiology, congenital, hereditary, and neonatal diseases and abnormalities, Ataxia, MESH: Pedigree, MESH: Age of Onset, MESH: Genetic Linkage, Biology, MESH: Intellectual Disability / psychology, MESH: Chromosomes, Human, Pair 1 / genetics, [SDV.BBM.GTP]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Genomics [q-bio.GN], medicine, Quantitative Biology - Genomics, Genomics (q-bio.GN), MESH: Adolescent, [SDV.GEN]Life Sciences [q-bio]/Genetics, MESH: Humans, MESH: Molecular Sequence Data, Cerebellar ataxia, [SCCO.NEUR]Cognitive science/Neuroscience, MESH: Child, Preschool, MESH: Polymerase Chain Reaction, [SDV.BBM.BM]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Molecular biology, medicine.disease, MESH: Male, MESH: France, MESH: Cognition Disorders / genetics, [SDV.GEN.GH]Life Sciences [q-bio]/Genetics/Human genetics, FOS: Biological sciences, TMEM240, Neurology (clinical), MESH: Intelligence Tests, MESH: Female, exome

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https://www.hal.inserm.fr/inserm-03017555/file/Delplanque.Brain.2014.Author.version.pdf

5

Fast cerebellar oscillation associated with ataxia in a mouse model of angelman syndrome

Authors: Bernard Dan, Laurent Servais, Guy Cheron, Joseph Wagstaff

Source: Neuroscience, 130 (3

Subject Terms: Cerebellum, Guanine Nucleotide Exchange Factors -- genetics, Purkinje cell, Synaptic Transmission, GABA Antagonists, Mice, Purkinje Cells, Guanine Nucleotide Exchange Factors, Evoked Potentials, Mutation -- physiology, Mice, Knockout, General Neuroscience, Angelman Syndrome -- genetics, Gap Junctions, Evoked Potentials -- physiology, Sciences bio-médicales et agricoles, Pyridazines, medicine.anatomical_structure, Cerebellar cortex, Carbenoxolone, medicine.symptom, congenital, hereditary, and neonatal diseases and abnormalities, medicine.medical_specialty, Ataxia, Microinjections, Ataxia -- genetics, Receptors, GABA-A -- antagonists & inhibitors, Pyridazines -- pharmacology, Biology, Purkinje Cells -- physiology, Physical Stimulation, Internal medicine, Angelman syndrome, Happy puppet syndrome, medicine, UBE3A, Animals, Angelman Syndrome -- physiopathology, GABA-A Receptor Antagonists, Ataxia -- physiopathology, Cerebellar ataxia, Carbenoxolone -- pharmacology, medicine.disease, Mice, Inbred C57BL, Endocrinology, Cerebellum -- physiopathology, nervous system, Gap Junctions -- drug effects, Vibrissae, Mutation, Angelman Syndrome, GABA Antagonists -- pharmacology, Neuroscience

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https://doi.org/10.1016/j.neuroscience.2004.09.013

6

Experimental Models of Transcription Factor-Associated Maturity-Onset Diabetes of the Young

Authors: Benoit R. Gauthier, Luc A. Otten, Haiyan Wang, Kerstin A. Hagenfeldt-Johansson, Pedro Luis Herrera, Claes B. Wollheim

Source: Diabetes, Vol. 51, No Suppl 3 (2002) pp. S333-342

Subject Terms: medicine.medical_specialty, Endocrinology, Diabetes and Metabolism, medicine.medical_treatment, Biology, digestive system, Maturity onset diabetes of the young, Animals, Genetically Modified, Diabetes Mellitus, Type 2/ physiopathology, Internal medicine, Diabetes mellitus, Internal Medicine, medicine, Animals, Humans, Hepatocyte Nuclear Factor 1-alpha, Transcription factor, Mutation/physiology, Hepatocyte Nuclear Factor 1-beta, ddc:616, Glucokinase, Insulin, Nuclear Proteins, Transcription Factors/genetics/ metabolism, medicine.disease, DNA-Binding Proteins, Hepatocyte nuclear factors, Insulin receptor, Endocrinology, Diabetes Mellitus, Type 2, Hepatocyte Nuclear Factor 1, Mutation, Hepatocyte Nuclear Factor 1-Beta, biology.protein, Transcription Factors

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https://doi.org/10.2337/diabetes.51.2007.s333

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7

Mutations in FRMD7, a newly identified member of the FERM family, cause X-linked idiopathic congenital nystagmus

Source: Nature Genetics. 38:1242-1244

Subject Terms: Male, medicine.medical_specialty, Pathology, Nystagmus, Congenital/*genetics, Brain/embryology/metabolism, genetic structures, Genetic Linkage, Eye disease, Eye Movements/genetics/physiology, Genes, X-Linked, Cytoskeletal Proteins/*genetics/physiology, Nystagmus, Biology, Membrane Proteins/*genetics/physiology, medicine.disease_cause, 03 medical and health sciences, 0302 clinical medicine, Genetic linkage, Internal medicine, Genetics, medicine, Humans, Mutation/physiology, X chromosome, 030304 developmental biology, Chromosomes, Human, X, Retina/metabolism, 0303 health sciences, Retina, Mutation, Chromosome Mapping, Gene Expression Regulation, Developmental, Eye movement, medicine.disease, eye diseases, Pedigree, medicine.anatomical_structure, Endocrinology, 030221 ophthalmology & optometry, Female, medicine.symptom, Congenital nystagmus

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https://doi.org/10.1038/ng1893

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8

The clustering of telomeres and colocalization with Rap1, Sir3, and Sir4 proteins in wild-type Saccharomyces cerevisiae

Authors: Harry Scherthan, Susan M. Gasser, Laurent Maillet, Monica Gotta, Thierry Laroche, Andrea Formenton

Source: The Journal of Cell Biology
Journal of Cell Biology, vol. 134, no. 6, pp. 1349-1363

Subject Terms: Saccharomyces cerevisiae, Blotting, Western, Fluorescent Antibody Technique, In situ hybridization, Biology, Fungal Proteins, Silent Information Regulator Proteins, Antibody Specificity, GTP-Binding Proteins, medicine, RNA, Messenger, Nuclear pore, In Situ Hybridization, Fluorescence, Silent Information Regulator Proteins, Saccharomyces cerevisiae, Cell Nucleus, Colocalization, SIR proteins, Cell Biology, Articles, Telomere, biology.organism_classification, Subtelomere, Molecular biology, Cell nucleus, medicine.anatomical_structure, rap GTP-Binding Proteins, Cell Nucleus/chemistry, Fungal Proteins/analysis, Fungal Proteins/genetics, GTP-Binding Proteins/analysis, GTP-Binding Proteins/genetics, Mutation/physiology, RNA, Messenger/analysis, Saccharomyces cerevisiae/chemistry, Saccharomyces cerevisiae/physiology, Telomere/chemistry, Telomere/physiology, Trans-Activators/analysis, Trans-Activators/genetics, Transcription Factors/analysis, Transcription Factors/genetics, Mutation, Trans-Activators, Transcription Factors

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http://europepmc.org/articles/PMC2121006

9

Anomalies de la barrière cutanée dans la dermatite atopique: une piste pour de nouveaux traitements ?

Authors: Eigenmann, Philippe, Hauser, Conrad, Brüggen, Marie-Charlotte

Source: Revue médicale suisse, Vol. 7, No 321 (2011) pp. 2453-6

Subject Terms: ddc:618, integumentary system, Dermatitis, Atopic/etiology/genetics/metabolism/therapy, Skin Physiological Phenomena/genetics, Intermediate Filament Proteins/genetics/physiology, Humans, Skin Diseases, Infectious/complications/etiology/genetics/therapy, Environment, Models, Biological, Skin/injuries/metabolism, Mutation/physiology, Permeability, Serpins/genetics/physiology

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https://archive-ouverte.unige.ch/unige:25274

10

Splicing factor SF3a60 is the mammalian homologue of PRP9 of S.cerevisiae: the conserved zinc finger-like motif is functionally exchangeable in vivo

Authors: Angela Krämer, Frank Mulhauser, Pierre Legrain, Graeme Bilbe, Reto Brosi, Karsten Groöining

Source: Nucleic Acids Research, Vol. 22, No 24 (1994) pp. 5223-8

Subject Terms: RNA Splicing Factors, DNA, Complementary, Saccharomyces cerevisiae Proteins, Recombinant Fusion Proteins/biosynthesis, Recombinant Fusion Proteins, Genes, Fungal, Molecular Sequence Data, Exonic splicing enhancer, Sequence alignment, RNA-binding protein, Saccharomyces cerevisiae, Biology, Fungal Proteins, Splicing factor, Genes, Fungal/genetics, Protein splicing, ddc:570, Escherichia coli, Genetics, Humans, Genes/genetics, Amino Acid Sequence, Cloning, Molecular, Mutation/physiology, Zinc finger, Saccharomyces cerevisiae/chemistry, Base Sequence, Sequence Homology, Amino Acid, Zinc Fingers/genetics/physiology, RNA-Binding Proteins, DNA, Complementary/genetics, Zinc Fingers, Sequence Analysis, DNA, Ribonucleoprotein, U2 Small Nuclear, Molecular biology, Cell biology, Molecular Weight, Escherichia coli/genetics, Fungal Proteins/genetics, Phenotype, Genes, Hela Cells, RNA-Binding Proteins/chemistry/genetics/isolation & purification, Mutation, RNA splicing, Sequence Alignment, HeLa Cells

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https://doi.org/10.1093/nar/22.24.5223

11

Thyroxine treatments do not correct inner ear defects in tmprss1 mutant mice

Authors: Michel Guipponi, Justin Tan, Hamish S. Scott, P E Crewther, Syazana Hanifa

Contributors: Hanifa, Syazana, Scott, Hamish S, Crewther, Pauline, Guipponi, Michel, Tan, Justin

Source: Neuroreport, Vol. 21, No 13 (2010) pp. 897-901

Subject Terms: medicine.medical_specialty, Hearing loss, Tectorial membrane, Ratón, Hepsin, cochlea, Thyroxine/*therapeutic use, resistance to thyroid hormones, Biology, Article, Hearing/physiology, 03 medical and health sciences, Mice, 0302 clinical medicine, Hearing, In vivo, Internal medicine, medicine, otorhinolaryngologic diseases, Animals, Inner ear, ddc:576.5, Ear Diseases, Cochlea, Mutation/physiology, 030304 developmental biology, Mice, Knockout, 0303 health sciences, Reverse Transcriptase Polymerase Chain Reaction, General Neuroscience, Hearing Tests, Serine Endopeptidases, Ear Diseases/congenital/*drug therapy/pathology, Transmembrane protein, 3. Good health, Thyroxine, medicine.anatomical_structure, Endocrinology, Serine Endopeptidases/*genetics/physiology, Ear, Inner, Mutation, Ear, Inner/*abnormalities/pathology, hypothyroidism, sense organs, medicine.symptom, hepsin, 030217 neurology & neurosurgery

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https://europepmc.org/articles/PMC2950264/

12

Endoplasmic reticulum Ca2+ measurements reveal that the cardiac ryanodine receptor mutations linked to cardiac arrhythmia and sudden death alter the threshold for store-overload-induced Ca2+ release

Authors: Peter P. Jones, Nicolas Demaurex, S.R. Wayne Chen, Lin Zhang, Jeff Bolstad, Donald J. Hunt, Dawei Jiang

Source: Biochemical Journal, Vol. 412, No 1 (2008) pp. 171-178

Subject Terms: medicine.medical_specialty, Ryanodine Receptor Calcium Release Channel/*genetics/metabolism, Myocardium/metabolism, Mutant, Tacrolimus Binding Protein 1A/metabolism, Point Mutation/physiology, Tacrolimus Binding Protein 1A, Gating, Biology, Endoplasmic Reticulum, medicine.disease_cause, Biochemistry, Sudden death, Ryanodine receptor 2, Internal medicine, medicine, Point Mutation, Protein Isoforms, Humans, Death, Sudden, Cardiac/*etiology, ddc:612, Molecular Biology, Cells, Cultured, Mutation, Endoplasmic Reticulum/*chemistry/metabolism, Ryanodine receptor, Arrhythmias, Cardiac/*genetics/metabolism, Myocardium, Endoplasmic reticulum, Cardiac arrhythmia, Arrhythmias, Cardiac, Biological Transport, Ryanodine Receptor Calcium Release Channel, Cell Biology, Biological Transport/genetics, Cell biology, Death, Sudden, Cardiac, Endocrinology, Calcium/*analysis/*metabolism, cardiovascular system, Calcium, Protein Isoforms/metabolism, Protein Binding

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https://archive-ouverte.unige.ch/unige:19059

13

Two novel mitochondrial DNA mutations in muscle tissue of a patient with limb-girdle myopathy

Authors: A Meulemans, Sara Seneca, Linda De Meirleir, Joél Smet, Willy Lissens, Jan De Bleecker, Rudy Van Coster, Boel De Paepe

Contributors: Faculty of Medicine and Pharmacy, Department of Embryology and Genetics, Pediatrics

Source: Vrije Universiteit Brussel

Subject Terms: Muscle tissue, Mitochondrial DNA, Muscle Fibers, Skeletal, oxidative phosphorylation, Biology, DNA, Mitochondrial, law.invention, Restriction fragment, DNA, Mitochondrial/genetics, Electron Transport Complex IV, RNA, Transfer, Arts and Humanities (miscellaneous), law, Electron Transport Complex IV/genetics, medicine, Cytochrome c oxidase, oxidative phosphorylation system, Humans, Muscle, Skeletal, Myopathy, Muscle Fibers, Skeletal/pathology, Gene, Polymerase chain reaction, Mutation/physiology, Polymorphism, Single-Stranded Conformational, Genetics, mt disorders, Muscular Dystrophies, Limb-Girdle/genetics, Middle Aged, Molecular biology, Immunohistochemistry, Heteroplasmy, Blotting, Southern, medicine.anatomical_structure, Muscular Dystrophies, Limb-Girdle, Muscle, Skeletal/pathology, Mutation, biology.protein, Electrophoresis, Polyacrylamide Gel, Female, Neurology (clinical), medicine.symptom, DNA mutations, RNA, Transfer/genetics

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https://doi.org/10.1001/archneur.64.9.1339

14

ATM gene and lymphoid malignancies

Authors: Gumy Pause, Fabienne, Wacker, Pierre, Sappino, Pascal

Source: Leukemia, Vol. 18, No 2 (2004) pp. 238-42

Subject Terms: DNA-Binding Proteins, ddc:618, Lymphoma/etiology/genetics, Phenotype, Protein-Serine-Threonine Kinases/genetics, Tumor Suppressor Proteins, Humans, Cell Cycle Proteins, Genetic Predisposition to Disease, Ataxia Telangiectasia Mutated Proteins, Mutation/physiology

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https://archive-ouverte.unige.ch/unige:55542

15

How mutations in the nAChRs can cause ADNFLE epilepsy

Authors: S. Le Hellard, Sigrid Weiland, H.A. Phillips, Fabienne Picard, Alain Malafosse, Sonia Bertrand, Samuel F. Berkovic, Daniel Bertrand, John C. Mulley, I. Favre

Source: Epilepsia, Vol. 43, No Suppl 5 (2002) pp. 112-122

Subject Terms: Agonist, Receptors, Nicotinic / drug effects, medicine.medical_specialty, Acetylcholine / pharmacology, medicine.drug_class, Xenopus, Mutant, Autosomal dominant nocturnal frontal lobe epilepsy, Biology, Receptors, Nicotinic, Nerve Net / physiopathology, ddc:616.89, Epilepsy, Temporal Lobe / genetics, Epilepsy, Temporal Lobe / physiopathology, Receptors, Nicotinic / genetics, Internal medicine, medicine, Animals, Humans, Receptor, ddc:612, Alleles, Acetylcholine receptor, Genes, Dominant, Mutation / physiology, Electric Conductivity, medicine.disease, Acetylcholine, Cell biology, Circadian Rhythm, Nicotinic acetylcholine receptor, Endocrinology, Nicotinic agonist, Neurology, Epilepsy, Temporal Lobe, Mutation, Oocytes, Receptors, Nicotinic / metabolism, Neurology (clinical), Nerve Net, medicine.drug

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https://pubmed.ncbi.nlm.nih.gov/12121305

16

The kinetically dominant assembly pathway for centrosomal asters in Caenorhabditis elegans is gamma-tubulin dependent

Authors: Hannak, E., Oegema, K., Kirkham, M., Gönczy, P., Habermann, B., Hyman, A. A.

Source: The Journal of cell biology, vol 157, iss 4

Subject Terms: Helminth Proteins/genetics/metabolism, Dynein ATPase/genetics/metabolism, Fluorescent Antibody Technique, Sequence Homology, tbg-1, Centrosome/*metabolism, Microtubules, Medical and Health Sciences, Mitotic Spindle Apparatus, Tubulin, Tubulin/*deficiency/genetics, grip, Non-U.S. Gov't, Phylogeny, Microtubules/genetics/*metabolism, Helminth Proteins, Biological Sciences, Amino Acid, Phenotype, Mitotic Spindle Apparatus/genetics/*metabolism, Microtubule-Associated Proteins, Signal Transduction, microtubule, 1.1 Normal biological development and functioning, Molecular Sequence Data, Mitosis, Down-Regulation, RNA/genetics, macromolecular substances, Spindle Apparatus, Mutation/*physiology, Research Support, Down-Regulation/physiology, Genetics, Animals, Point Mutation, Point Mutation/genetics, Mitosis/*physiology, Caenorhabditis elegans, Caenorhabditis elegans Proteins, Centrosome, Dyneins, Caenorhabditis elegans/*genetics/metabolism, Kinetics, Caenorhabditis elegans Proteins/genetics/metabolism, Mutation, Signal Transduction/genetics, RNA, Spc, Microtubule-Associated Proteins/genetics/metabolism, Generic health relevance, Developmental Biology

File Description: application/pdf

Access URL: https://explore.openaire.eu/search/publication?articleId=dedup_wf_001::df1e572d1a5ff9b6c1aed93b87242633
https://escholarship.org/uc/item/6cz745f3

17

In vitro analyses of known and novel RUNX1/AML1 mutations in dominant familial platelet disorder with predisposition to acute myelogenous leukemia: implications for mechanisms of pathogenesis

Authors: Stylianos E. Antonarakis, Archie McNicol, Gregory M. Cottles, Yoshiaki Ito, Masatoshi Yanagida, Hamish S. Scott, Wendy H. Raskind, Feng Wu, Colette Rossier, Sara J. Israels, Kathleen F. Benson, Motomi Osato, Katsuya Shigesada, Norio Asou, Harvey J. Weiss, Joëlle Michaud, Marshall S. Horwitz

Source: Blood, Vol. 99, No 4 (2002) pp. 1364-1372

Subject Terms: Male, Chromosomes, Human, Pair 21, Genetic Linkage, DNA Mutational Analysis, medicine.disease_cause, Biochemistry, chemistry.chemical_compound, hemic and lymphatic diseases, Missense mutation, Genes, Dominant, ddc:616, Genetics, Mutation, Linkage (Genetics), Chromosomes, Human, Pair 21/genetics, Hematology, Pedigree, DNA-Binding Proteins, DNA-Binding Proteins/ genetics/metabolism, Leukemia, Myeloid, Acute, RUNX1, embryonic structures, Core Binding Factor Alpha 2 Subunit, Female, Haploinsufficiency, Leukemia, Myeloid, Acute/etiology/ genetics, Protein Binding, Transcriptional Activation, Platelet disorder, Immunology, Biology, Frameshift mutation, Blood Platelet Disorders/ genetics, Point Mutation/ physiology, Proto-Oncogene Proteins, medicine, Humans, Point Mutation, Genetic Predisposition to Disease, Transcription Factors/ genetics/metabolism, Family Health, Point mutation, Cell Biology, chemistry, Haplotypes, Transcription Factor AP-2, Cancer research, Transcriptional Activation/drug effects, Blood Platelet Disorders, Carcinogenesis, Transcription Factors

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https://pubmed.ncbi.nlm.nih.gov/11830488

18

[Molecular mechanisms of oncogenic transformation: what's new?]

Authors: Blanchard, J. M.

Contributors: Institut de Génétique Moléculaire de Montpellier (IGMM), Centre National de la Recherche Scientifique (CNRS)-Université de Montpellier (UM), Adele, Sarah

Source: Bulletin du Cancer
Bulletin du Cancer, John Libbey Eurotext, 2002, 89 (1), pp.9--16

Subject Terms: Pathologic/physiopathology Neural Cell Adhesion Molecules/physiology Paclitaxel/metabolism Protein-Serine-Threonine Kinases/physiology Radiation Tolerance Rats Thrombospondins/physiology Transforming Growth Factor beta/physiology Tuberous Sclerosis/genetics/pathology, Phytogenic/metabolism *CDC2-CDC28 Kinases Cell Cycle/*physiology Cell Division/physiology Cell Transformation, [SDV.BBM] Life Sciences [q-bio]/Biochemistry, Molecular Biology, [SDV.BBM]Life Sciences [q-bio]/Biochemistry, Molecular Biology, Animals Antineoplastic Agents, bcr-abl/physiology Humans Mice Mutation/*physiology Neoplasm Metastasis Neoplasm Proteins/physiology Neoplasms/*genetics/*pathology Neovascularization, Neoplastic/genetics/pathology Cyclin D1/physiology Cyclin E/physiology Cyclin-Dependent Kinase 2 Cyclin-Dependent Kinase Inhibitor p16/physiology Cyclin-Dependent Kinase Inhibitor p21 Cyclin-Dependent Kinases/physiology Cyclins/metabolism Disease Progression Drug Resistance Fusion Proteins