about
Hyperekplexia associated with compound heterozygote mutations in the beta-subunit of the human inhibitory glycine receptor (GLRB)Sox-2 is expressed by glial and progenitor cells and Pax-6 is expressed by neuroblasts in the human subventricular zoneThe GDP-GTP exchange factor collybistin: an essential determinant of neuronal gephyrin clusteringMutations in the gene encoding GlyT2 (SLC6A5) define a presynaptic component of human startle disease.Functional variants of antioxidant genes in smokers with COPD and in those with normal lung functionFurther evidence of autosomal dominant congenital zonular pulverulent cataracts linked to 13q11 (CZP3) and a novel mutation in connexin 46 (GJA3)Isoform heterogeneity of the human gephyrin gene (GPHN), binding domains to the glycine receptor, and mutation analysis in hyperekplexiaDistribution of gephyrin in the human brain: an immunohistochemical analysisEvidence for recessive as well as dominant forms of startle disease (hyperekplexia) caused by mutations in the alpha 1 subunit of the inhibitory glycine receptorStartle disease in Irish wolfhounds associated with a microdeletion in the glycine transporter GlyT2 gene.A novel dominant hyperekplexia mutation Y705C alters trafficking and biochemical properties of the presynaptic glycine transporter GlyT2Mutations in the GlyT2 gene (SLC6A5) are a second major cause of startle disease.The glycinergic system in human startle disease: a genetic screening approach.A critical role for glycine transporters in hyperexcitability disorders.Localization of glycine receptors in the human forebrain, brainstem, and cervical spinal cord: an immunohistochemical reviewEpilepsy and deprivation, a data linkage study.QT interval prolongation associated with sibutramine treatmentMisdiagnosis of long QT syndrome as epilepsy at first presentation.Biophysical properties of 9 KCNQ1 mutations associated with long-QT syndrome.Symptoms and signs associated with syncope in young people with primary cardiac arrhythmias.Association of gephyrin and glycine receptors in the human brainstem and spinal cord: an immunohistochemical analysis.Immunohistochemical staining of post-mortem adult human brain sections.An ovine transgenic Huntington's disease model.TUBA1A mutations cause wide spectrum lissencephaly (smooth brain) and suggest that multiple neuronal migration pathways converge on alpha tubulins.TBP, a polyglutamine tract containing protein, accumulates in Alzheimer's disease.A novel GABRG2 mutation, p.R136*, in a family with GEFS+ and extended phenotypes.Recognizable cerebellar dysplasia associated with mutations in multiple tubulin genes.PICK1 interacts with alpha7 neuronal nicotinic acetylcholine receptors and controls their clustering.Pathogenic copy number variants and SCN1A mutations in patients with intellectual disability and childhood-onset epilepsyGenome-wide Polygenic Burden of Rare Deleterious Variants in Sudden Unexpected Death in Epilepsy.Novel missense mutations in the glycine receptor β subunit gene (GLRB) in startle diseaseComplement is activated in progressive multiple sclerosis cortical grey matter lesions.The genetics of hyperekplexia: more than startle!New hyperekplexia mutations provide insight into glycine receptor assembly, trafficking, and activation mechanisms.De novo mutations in the beta-tubulin gene TUBB2A cause simplified gyral patterning and infantile-onset epilepsy.Identifying and prioritising epilepsy treatment uncertainties.The genetics of epilepsy--the past, the present and future.Implications for families of advances in understanding the genetic basis of epilepsy.Next generation sequencing methodologies--an overview.Translation of genetic findings to clinical practice in juvenile myoclonic epilepsy.
P50
Q24293103-55B1146A-C997-4821-9668-801419F0A0CDQ24296665-95497F71-05CC-459F-888C-D76A2BC3BC0CQ24297620-3128D5DD-B470-4724-BB66-18AA85C2E713Q24338670-0EC8CF64-4F9B-4DE7-8D36-12201DB086F3Q24681700-D4196D61-1B2E-45D1-8939-2295E936D043Q28140425-1B65AE84-261A-4C98-BA12-6ACC9EA0C57BQ28189818-D99F7DD8-C1B8-4BE2-AC72-404B41A2027AQ28204151-F80446F4-D884-4509-9AB0-F6BD6C4B44FEQ28235848-3F9C4C71-729C-4B13-9C95-68AEC38AD15EQ30436113-3885599A-E699-41B2-985B-64D4C0743784Q30450700-990E205D-6F68-446C-96BD-0A4356CAA980Q30450702-3BABC8DF-82CC-4418-A8DE-41BE21C5137FQ30481905-4D0E6929-9474-4488-A553-CCC6C9FA17EBQ30492982-EDDC5E1C-01CA-4E31-88DF-6D4DD9475CFFQ30886039-16395A5A-A825-4166-91F4-9A5595355CD2Q30931856-A708D41A-640B-4EC8-B8A0-5BB0C0320F42Q33153640-84B78F2A-0B08-4538-A8DB-CF675E1ACEDBQ33157207-73080D41-59F4-4DFA-8DCC-EBA772BC8F12Q33157910-3FD6CBF9-1A4E-4709-A53C-E594FC53D312Q33160071-582000A8-C729-4DBB-B1FC-2BA418AC2DC8Q33195106-23EAD2DB-A16B-46DE-9B56-03C81F67A927Q33280976-11978863-9B12-4181-91E7-0284985638B1Q33815561-D5BE0BC3-3F17-462B-8026-3FBBC201EAEBQ33947860-0923B509-2933-491B-947C-24AB8B9D025BQ34326548-F27B06E3-4ACA-413B-8B51-D80E240CCD67Q34464870-F8EDD6C4-F17E-4799-A5E2-76F0203DE196Q35679363-572ADF0C-05F1-4F2B-8457-01E2D37974EBQ35848221-6EDFDF85-DC20-4166-96F0-82F7924197A9Q35998816-DC7B6EA1-C6B3-4DD6-8FEB-B7538E56B267Q36106276-3B2238E0-ACE6-4FE0-BF64-1964538477E4Q36636926-9AD42B04-6746-4742-B965-52EA698AAD3AQ37031176-F518334F-512E-4C5A-81F6-9086949BB6DCQ37245313-7381975C-3C7B-4AE4-9564-B4793E6A58CEQ37333728-F345EF93-ED10-4894-968A-603786BDA2ACQ37693218-12AC5D2F-2DA1-495C-A2D4-D0EFF6DD19D5Q37766394-5F4B9A10-FE32-4454-8962-8C271283D73EQ37811360-4855CF4F-1C0A-4439-9BE0-207CB9268A22Q37811446-F739A7E9-A402-4183-AF47-D8D0518E8C53Q38050573-C665A105-8FA3-43E5-A0FA-78D137FA4ADEQ38053744-AF525BEB-8112-4DA1-9991-B831178FAEF6
P50
description
hulumtues
@sq
researcher
@en
ricercatore
@it
wetenschapper
@nl
հետազոտող
@hy
name
Mark I Rees
@ast
Mark I Rees
@en
Mark I Rees
@es
Mark I Rees
@nl
Mark I Rees
@sl
type
label
Mark I Rees
@ast
Mark I Rees
@en
Mark I Rees
@es
Mark I Rees
@nl
Mark I Rees
@sl
altLabel
Mark Rees
@en
prefLabel
Mark I Rees
@ast
Mark I Rees
@en
Mark I Rees
@es
Mark I Rees
@nl
Mark I Rees
@sl
P108
P214
P1053
J-3129-2012
P106
P21
P214
P31
P3829
P496
0000-0003-3570-5986