Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
2002-6-21
pubmed:abstractText
Lissencephaly, which means 'smooth cortex', is caused by defective neuronal migration during development of the cerebral cortex and has devastating clinical consequences. 'Classical' lissencephaly seems to reflect mutations in regulators of the microtubule cytoskeleton, whereas 'cobblestone' lissencephaly is caused by mutations in genes needed for the integrity of the basal lamina of the central nervous system. Reelin, which is mutated in a third type of lissencephaly, may represent a unifying link because it encodes an extracellular protein that regulates neuronal migration and may also regulate the microtubule cytoskeleton.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/1-Alkyl-2-acetylglycerophosphocholin..., http://linkedlifedata.com/resource/pubmed/chemical/Cell Adhesion Molecules, Neuronal, http://linkedlifedata.com/resource/pubmed/chemical/Extracellular Matrix Proteins, http://linkedlifedata.com/resource/pubmed/chemical/FKTN protein, human, http://linkedlifedata.com/resource/pubmed/chemical/Membrane Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Microtubule-Associated Proteins, http://linkedlifedata.com/resource/pubmed/chemical/N-Acetylglucosaminyltransferases, http://linkedlifedata.com/resource/pubmed/chemical/Nerve Tissue Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Neuropeptides, http://linkedlifedata.com/resource/pubmed/chemical/PAFAH1B1 protein, human, http://linkedlifedata.com/resource/pubmed/chemical/Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Cytoadhesin, http://linkedlifedata.com/resource/pubmed/chemical/Serine Endopeptidases, http://linkedlifedata.com/resource/pubmed/chemical/doublecortin protein, http://linkedlifedata.com/resource/pubmed/chemical/protein O-mannose..., http://linkedlifedata.com/resource/pubmed/chemical/reelin protein
pubmed:status
MEDLINE
pubmed:month
Jun
pubmed:issn
0959-437X
pubmed:author
pubmed:issnType
Print
pubmed:volume
12
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
320-7
pubmed:dateRevised
2008-5-6
pubmed:meshHeading
pubmed-meshheading:12076676-1-Alkyl-2-acetylglycerophosphocholine Esterase, pubmed-meshheading:12076676-Animals, pubmed-meshheading:12076676-Basement Membrane, pubmed-meshheading:12076676-Cell Adhesion Molecules, Neuronal, pubmed-meshheading:12076676-Extracellular Matrix, pubmed-meshheading:12076676-Extracellular Matrix Proteins, pubmed-meshheading:12076676-Humans, pubmed-meshheading:12076676-Membrane Proteins, pubmed-meshheading:12076676-Microtubule-Associated Proteins, pubmed-meshheading:12076676-Microtubules, pubmed-meshheading:12076676-N-Acetylglucosaminyltransferases, pubmed-meshheading:12076676-Neocortex, pubmed-meshheading:12076676-Nerve Tissue Proteins, pubmed-meshheading:12076676-Neuropeptides, pubmed-meshheading:12076676-Proteins, pubmed-meshheading:12076676-Receptors, Cytoadhesin, pubmed-meshheading:12076676-Serine Endopeptidases, pubmed-meshheading:12076676-Signal Transduction
pubmed:year
2002
pubmed:articleTitle
Smooth, rough and upside-down neocortical development.
pubmed:affiliation
Department of Neurology, Beth Israel Deaconess Medical Center and Harvard Medical School, Boston, Massachusetts 02115, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Review, Research Support, Non-U.S. Gov't