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    • Hirotomo Saitsu
    • Hirotomo Saitsu

      Hirotomo Saitsu

      Department of Biochemistry, Hamamatsu University School of Medicine, Shizuoka, Japan | Department of Biochemistry, Hamamatsu University School of Medicine, Japan. Electronic ...



      KOL Resume for Hirotomo Saitsu


      Department of Biochemistry, Hamamatsu University School of Medicine, Shizuoka, Japan


      Department of Biochemistry, Hamamatsu University School of Medicine, Hamamatsu, 431-3192 Japan


      Department of Pediatrics (H.K.), Minamata City General Hospital & Medical Center, Kumamoto; Department of Mental Retardation and Birth Defect Research (H.L., K.I.), National Institute of Neuroscience, National Center of Neurology and Psychiatry, Kodaira, Tokyo; Department of Biochemistry (S.M., H.S.), Hamamatsu University School of Medicine, Shizuoka; Department of Pediatrics (H.U.), Kumamoto Takumadai Rehabilitation Hospital; Kanagawa Children's Medical Center (Y.T., Y.E.), Clinical Research Institute, Yokohama, Kanagawa; Department of Pediatrics (C.I., H.K., T.O., T.S., H.I.), National Hospital Organization Kumamoto Saishun Medical Center, Koshi; Clinical Research Institute, Kanagawa Children's Medical Center, (Y.E.), Yokohama, Kanagawa; Department of Pediatric Neurology (J.T.), Tokyo Women's Medical University Yachiyo Medical Center, Chiba; and Division of Medical Genetics (K.K.), Kanagawa Children's Medical Center, Yokohama, Japan.


      Hamamatsu University School of Medicine, Department of Biochemistry, 1-20-1 Handayama, Higashi-ku, Hamamatsu-shi, Shizuoka, 431-3192, Japan

      Yokohama City University Graduate School of Medicine, Department of Human Genetics, Yokohama


      Department of Human Genetics, Yokohama City University Graduate School of Medicine, Japan


      Department of Human Genetics Yokohama City University Graduate School of Medicine YokohamaJapan


      Department of Human Genetics, Graduate School of Medicine, Yokohama City University, Yokohama, Japan.

      These authors contributed equally to this work.


      Department of Human Genetics Graduate School of Medicine Yokohama City University Yokohama Japan.


      Department of Human Genetics, Yokohama City University Graduate School of Medicine


      From the Department of Human Genetics (K. Nakamura, K. Nishiyama, H.K., M.N., Y.T., N. Miyake, N. Matsumoto, H.S.), Yokohama City University Graduate School of Medicine, Yokohama; Department of Pediatrics (K. Nakamura, M.K., K. Hayasaka), Yamagata University Faculty of Medicine, Yamagata; Division of Neurology (H.O., S.Y., M. Okuda, T.W.), Clinical Research Institute, Kanagawa Children's Medical Center, Yokohama; Department of Child Neurology (E.N.), National Center Hospital, National Center of Neurology and Psychiatry, Tokyo; Department of Pediatric Neurology (K. Haginoya), Takuto Rehabilitation Center for Children, Sendai; Department of Pediatrics (J.T.), Epilepsy Center, Nishi-Niigata Chuo National Hospital, Niigata; Department of Pediatrics (S.S.), Osaka Medical College Hospital, Osaka; National Epilepsy Center (K.I.), Shizuoka Institute of Epilepsy and Neurological Disorders, Shizuoka; Department of Pediatrics (S.T.), Yokohama City University Medical Center, Yokohama; Department of Pediatrics (H.I.), Tokyo Metropolitan Bokuto Hospital, Tokyo, Japan; Metabolic Neurogenetic Clinic (D.L., T.L.-S.), Wolfson Medical Center, Holon, Israel; Department of Human Genetics (D.E.C.-B., C.E.V.), National Institute of Pediatrics, Mexico City, Mexico; Division of Child Neurology (M. Ohfu), Okinawa Nanbu Medical Center and Children's Medical Center, Okinawa, Japan; Institute of Medical Genetics (K.W.), University Medical Center Ljubljana; Department of Child, Adolescent and Developmental Neurology (B.G.S.), University Children's Hospital, Ljubljana, Slovenia; Department of Neurology (S.H.), Nagano Children's Hospital, Nagano, Japan; Department of Obstetrics and Gynecology (D.C.), The Prenatal Diagnosis and Medical Genetics Program, Mount Sinai Hospital, University of Toronto; and Division of Clinical and Metabolic Genetics (D.C., D.M.R.), The Hospital for Sick Children, University of Toronto, Canada.

      Yokohama City University, Graduate School of Medicine Department of Human Genetics Yokohama Japan


      From the Department of Human Genetics (S.M., N.M., A.N.-T., Y.K., I.O., Y.T., H.D., H.Sakai, H.Saitsu, N.M.), Yokohama City University Graduate School of Medicine, Yokohama; Touho Neurosurgical Clinic (H.T.), Osaka; Tokyo Women's Medical University Institute for Integrated Medical Sciences (K.S., T.Y.), Tokyo; Department of Neurosurgery (M.H., N.K.), Yokohama City University Graduate School of Medicine, Yokohama; Department of Neurosurgery (H.K., K.N.), Tone Chuo Hospital, Gunma; Division of Medical Genetics (N.O.), Osaka Medical Center and Research Institute for Maternal and Child Health, Osaka; Department of Rehabilitation Medicine (T.M.), Ichikawa City Rehabilitation Hospital, Ichikawa; Department of Clinical Neurology and Stroke Medicine (S.K., Y.K.), Yokohama City University Graduate School of Medicine, Yokohama; Department of Biostatistics and Epidemiology (M.T., S.M.), Yokohama City University Medical Center, Yokohama; Department of Medical Genetics (Y.M.), Tohoku University School of Medicine, Sendai; Department of Pediatrics (S.K.), Tohoku University School of Medicine, Sendai, Japan.

      Department of Human Genetics, Yokohama City University Graduate School of Medicine, Yokohama


      Department of Human Genetics, Yokohama City University Graduate School of Medicine, Fukuura 3‐9, Kanazawa‐ku, Yokohama 236‐0004, Japan


      Department of Human Genetics, Yokohama City University Graduate School of Medicine, Fukuura 3‐9, Kanazawa‐ku, Yokohama 236‐0004, Japan.



      Hirotomo Saitsu: Influence Statistics

      Sample of concepts for which Hirotomo Saitsu is among the top experts in the world.
      Concept World rank
      folr1 ntd #1
      gata4 variant #1
      enhancer fgf8 #1
      shh dorsal telencephalon #1
      tmem63a variants patients #1
      embryos myeloschisis #1
      gly784ser #1
      pax2 optic stalk #1
      tcf4 abnormalities ccas #1
      mouse enhancers mice #1
      cca etiologies #1
      shh signaling molecules #1
      principal mri phenotype #1
      families c17716c #1
      efficient diagnostic japan #1
      pro213leu #1
      closed neural tubes #1
      parg891 #1
      patient u2af2 #1
      scn8arelated dee case #1
      c386tg #1
      u2af2 variant #1
      camkiiβ pro213leu #1
      c187ct variant #1
      25 divisions #1
      patients tubb4a #1
      shh vax1 vax2 #1
      splicing polr1c variants #1
      generalized cyanosis #1
      tubb4a case #1
      scn8arelated dee #1
      neocortex shh #1
      setd1b domain #1
      triobased wholeexome sequencing #1
      polr1c variants splicing #1
      camkiiβ mouse model #1
      hydranencephaly incidence japan #1
      marked bradycardia seizures #1
      region schizencephaly #1
      novo u2af2 #1
      rare kcnj5 variant #1
      ntd developmental genes #1
      hydranencephaly miyagi prefecture #1
      ciselements conserved enhancers #1
      tortuosity intracranial veins #1
      novo missense variant #1
      top2b c187ct #1
      ohtahara stxbp1 #1
      mutations hypomyelinating #1
      polr3a polr3a variants #1


      Prominent publications by Hirotomo Saitsu

      KOL-Index: 13067

      Kabuki syndrome is a congenital anomaly syndrome characterized by developmental delay, intellectual disability, specific facial features including long palpebral fissures and ectropion of the lateral third of the lower eyelids, prominent digit pads, and skeletal and visceral abnormalities. Mutations in MLL2 and KDM6A cause Kabuki syndrome. We screened 81 individuals with Kabuki syndrome for mutations in these genes by conventional methods (n = 58) and/or targeted resequencing (n = 45) or ...

      Known for Kdm6a Mutations | Kabuki Syndrome | Mutation Mll2 | Facial Features | Intellectual Disability
      KOL-Index: 12650

      Congenital hypomyelinating disorders are a heterogeneous group of inherited leukoencephalopathies characterized by abnormal myelin formation. We have recently reported a hypomyelinating syndrome characterized by diffuse cerebral hypomyelination with cerebellar atrophy and hypoplasia of the corpus callosum (HCAHC). We performed whole-exome sequencing of three unrelated individuals with HCAHC and identified compound heterozygous mutations in POLR3B in two individuals. The mutations include ...

      Known for Rna Polymerase | Pol Iii | Corpus Callosum | Recessive Genetic Predisposition | Missense Mutations
      KOL-Index: 12449

      Sotos syndrome is characterized by prenatal and postnatal overgrowth, characteristic craniofacial features and mental retardation. Haploinsufficiency of NSD1 causes Sotos syndrome. Recently, two microdeletions encompassing Nuclear Factor I-X (NFIX) and a nonsense mutation in NFIX have been found in three individuals with Sotos-like overgrowth features, suggesting possible involvements of NFIX abnormalities in Sotos-like features. Interestingly, seven frameshift and two splice site ...

      Known for Missense Mutations | Sotos Syndrome | Nfix Protein | Dimerization Domain | Nsd1 Abnormalities
      KOL-Index: 12391

      OBJECTIVE: Recently, COL4A1 mutations have been reported in porencephaly and other cerebral vascular diseases, often associated with ocular, renal, and muscular features. In this study, we aimed to clarify the phenotypic spectrum and incidence of COL4A1 mutations.

      METHODS: We screened for COL4A1 mutations in 61 patients with porencephaly and 10 patients with schizencephaly, which may be similarly caused by disturbed vascular supply leading to cerebral degeneration, but can be ...

      Known for Col4a1 Mutations | Phenotypic Spectrum | Porencephaly Schizencephaly | Hemolytic Anemia | Intracranial Calcification
      KOL-Index: 12246

      Glycosylphosphatidylinositol (GPI) is a glycolipid that anchors >150 various proteins to the cell surface. At least 27 genes are involved in biosynthesis and transport of GPI-anchored proteins (GPI-APs). To date, mutations in 13 of these genes are known to cause inherited GPI deficiencies (IGDs), and all are inherited as recessive traits. IGDs mainly manifest as intellectual disability, epilepsy, coarse facial features, and multiple organ anomalies. These symptoms are caused by the ...

      Known for Intellectual Disability | Pathogenic Variants | Gpi Pigg | Consanguineous Families | Cell Surface
      KOL-Index: 12096

      OBJECTIVE: Focal cortical dysplasia (FCD) type IIb is a cortical malformation characterized by cortical architectural abnormalities, dysmorphic neurons, and balloon cells. It has been suggested that FCDs are caused by somatic mutations in cells in the developing brain. Here, we explore the possible involvement of somatic mutations in FCD type IIb.

      METHODS: We collected a total of 24 blood-brain paired samples with FCD, including 13 individuals with FCD type IIb, 5 with type IIa, and 6 ...

      Known for Somatic Mutations | Type Iib | Focal Cortical Dysplasia | Cortical Development | Mtor Fcd
      KOL-Index: 11857

      Mutations in the components of the SWItch/sucrose nonfermentable (SWI/SNF)-like chromatin remodeling complex have recently been reported to cause Coffin-Siris syndrome (CSS), Nicolaides-Baraitser syndrome (NCBRS), and ARID1B-related intellectual disability (ID) syndrome. We detail here the genotype-phenotype correlations for 85 previously published and one additional patient with mutations in the SWI/SNF complex: four with SMARCB1 mutations, seven with SMARCA4 mutations, 37 with SMARCA2 ...

      Known for Arid1b Mutations | Disassembly Chromosomal Proteins | Congenital Humans | Swi Snf Complex | Ncbrs Css
      KOL-Index: 11801

      Sonic hedgehog (Shh) is a secreted molecule that is thought to regulate tissue growth and patterning in vertebrate embryos. Although it has been reported that Gli transcription factors mediate Shh signaling to the nucleus, little is known about developmental target genes of Gli. In the previous genetic study, we showed that Shh is required for Fgf15 expression in the diencephalon and midbrain. Here, we examined whether Fgf15 is a direct target of Shh signaling through Gli. Shh was ...

      Known for Sonic Hedgehog | Fgf15 Gene | Transcription Factors | Zinc Finger | Diencephalon Midbrain
      KOL-Index: 11686

      OBJECTIVE: Recently, de novo mutations in GRIN1 have been identified in patients with nonsyndromic intellectual disability and epileptic encephalopathy. Whole exome sequencing (WES) analysis of patients with genetically unsolved epileptic encephalopathies identified four patients with GRIN1 mutations, allowing us to investigate the phenotypic spectrum of GRIN1 mutations.

      METHODS: Eighty-eight patients with unclassified early onset epileptic encephalopathies (EOEEs) with an age of onset ...

      Known for Grin1 Mutations | Movement Disorders | Patients Epileptic Encephalopathy | Intellectual Disability | Phenotypic Spectrum
      KOL-Index: 10768

      Defects of the human glycosylphosphatidylinositol (GPI) anchor biosynthetic pathway show a broad range of clinical phenotypes. A homozygous mutation in PIGN, a member of genes involved in the GPI anchor-synthesis pathway, was previously reported to cause dysmorphic features, multiple congenital anomalies, severe neurological impairment, and seizure in a consanguineous family. Here, we report two affected siblings with compound heterozygous PIGN mutations [c.808T >C (p.Ser270Pro) and ...

      Known for Congenital Anomalies | Developmental Delay | Pign Mutations | Hypotonia Epilepsy | Cerebellar Atrophy
      KOL-Index: 10656

      The nuclear pore complex (NPC) is a huge protein complex embedded in the nuclear envelope. It has central functions in nucleocytoplasmic transport, nuclear framework, and gene regulation. Nucleoporin 107 kDa (NUP107) is a component of the NPC central scaffold and is an essential protein in all eukaryotic cells. Here, we report on biallelic NUP107 mutations in nine affected individuals who are from five unrelated families and show early-onset steroid-resistant nephrotic syndrome (SRNS). ...

      Known for Nuclear Pore | Biallelic Mutations | Nephrotic Syndrome | Cultured Child Child | Complex Proteins
      KOL-Index: 10590

      OBJECTIVE: De novo SCN8A mutations have been reported in patients with epileptic encephalopathy. Herein we report seven patients with de novo heterozygous SCN8A mutations, which were found in our comprehensive genetic analysis (target capture or whole-exome sequencing) for early onset epileptic encephalopathies (EOEEs).

      METHODS: A total of 163 patients with EOEEs without mutations in known genes, including 6 with malignant migrating partial seizures in infancy (MMPSI), and 60 with ...

      Known for Scn8a Mutations | Epileptic Encephalopathy | Early Onset | Epilepsy Female Humans | 7 Patients
      KOL-Index: 10529

      Nemaline myopathy (NEM) is a common congenital myopathy. At the very severe end of the NEM clinical spectrum are genetically unresolved cases of autosomal-recessive fetal akinesia sequence. We studied a multinational cohort of 143 severe-NEM-affected families lacking genetic diagnosis. We performed whole-exome sequencing of six families and targeted gene sequencing of additional families. We identified 19 mutations in KLHL40 (kelch-like family member 40) in 28 apparently unrelated NEM ...

      Known for Klhl40 Mutations | Nemaline Myopathy | Skeletal Mutation | Missense Myopathies | Fetal Akinesia
      KOL-Index: 10414

      Weaver syndrome (WS) is a rare congenital overgrowth disorder caused by heterozygous mutations in EZH2 (enhancer of zeste homolog 2) or EED (embryonic ectoderm development). EZH2 and EED are core components of the polycomb repressive complex 2 (PRC2), which possesses histone methyltransferase activity and catalyzes trimethylation of histone H3 at lysine 27. Here, we analyzed eight probands with clinically suspected WS by whole-exome sequencing and identified three mutations: a 25.4-kb ...

      Known for Weaver Syndrome | Repressive Complex | Zeste Homolog | Mutations Suz12 | Ezh2 Eed
      KOL-Index: 10185

      Proteoglycans (PGs) are a major component of the extracellular matrix in many tissues and function as structural and regulatory molecules. PGs are composed of core proteins and glycosaminoglycan (GAG) side chains. The biosynthesis of GAGs starts with the linker region that consists of four sugar residues and is followed by repeating disaccharide units. By exome sequencing, we found that B3GALT6 encoding an enzyme involved in the biosynthesis of the GAG linker region is responsible for a ...

      Known for Linker Region | Connective Tissue | Danlos Syndrome | Extracellular Matrix | Exome Sequencing

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      Hirotomo Saitsu:Expert Impact

      Concepts for whichHirotomo Saitsuhas direct influence:Intellectual disability,  West syndrome,  Epileptic encephalopathy,  Exome sequencing,  Leigh syndrome,  Developmental delay,  Ohtahara syndrome,  Situ hybridization.

      Hirotomo Saitsu:KOL impact

      Concepts related to the work of other authors for whichfor which Hirotomo Saitsu has influence:Intellectual disability,  Moyamoya disease,  Exome sequencing,  Kabuki syndrome,  Neurodevelopmental disorders,  Developmental delay,  Epileptic encephalopathy.



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      Department of Biochemistry, Hamamatsu University School of Medicine, Shizuoka, Japan | Department of Biochemistry, Hamamatsu University School of Medicine, Japan. Electronic address: hsaitsu@hama-med.ac.jp. | Department of Biochemistry, Hamamatsu Uni

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