Results 131 to 140 of about 2,739 (166)

Novel lissencephaly-associated NDEL1 variant reveals distinct roles of NDE1 and NDEL1 in nucleokinesis and human cortical malformations. [PDF]

open access: yesActa Neuropathol
Tsai MH   +20 more
europepmc   +1 more source

Fra Gaza til LIS1-tjeneste

open access: yesTidsskrift for Den norske legeforening
openaire   +1 more source

Min vei til LIS1-stilling

open access: yesTidsskrift for Den norske legeforening
openaire   +1 more source

LIS1-tiden ble til bok

open access: yesTidsskrift for Den norske legeforening
openaire   +1 more source

Two microtubule-plus-end binding proteins LIS1-1 and LIS1-2, homologues of human LIS1 in Neurospora crassa [PDF]

open access: yesFungal Genetics and Biology, 2015
LIS1 is a microtubule (Mt) plus-end binding protein that interacts with the dynein/dynactin complex. In humans, LIS1 is required for proper nuclear and organelle migration during cell growth. Although gene duplication is absent from Neurospora crassa, we found two paralogues of human LIS1.
Genaro Pimienta   +2 more
exaly   +5 more sources
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LIS1 is a microtubule-associated phosphoprotein

FEBS Journal, 1999
Lissencephaly, a severe brain malformation, may be caused by mutations in the LIS1 gene. LIS1 encodes a microtubule‐associated protein (MAP) that is also part of the enzyme complex, platelet‐activating factor acetylhydrolase. LIS1 is also found in a complex with two protein kinases; a T‐cell Tat‐associated kinase, which contains casein‐dependant kinase
Orly Reiner   +2 more
exaly   +3 more sources

LIS1 Duplication

Journal of Child Neurology, 2011
Disruptions to LIS1 gene expression result in neuronal migration abnormalities. LIS1 heterozygosity is a significant cause of lissencephaly, while overexpression has recently been noted in cases of microcephaly, ventriculomegaly, and dysgenesis of the corpus callosum with normal cortical gyration.
Jason P, Lockrow   +4 more
openaire   +2 more sources

LIS1 cracks open dynein

Nature Cell Biology, 2020
Active transport along microtubules by molecular motors is a crucial cellular process that is disrupted in human diseases. Single-molecule studies from three independent groups reveal a new molecular mechanism for how cells control the activity of the complex microtubule motor cytoplasmic dynein via the neurodevelopmental protein LIS1.
openaire   +2 more sources

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