12183616

Source:http://linkedlifedata.com/resource/pubmed/id/12183616

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Predicate	Object
rdf:type	pubmed:Citation
lifeskim:mentions	umls-concept:C0027910
pubmed:issue	5584
pubmed:dateCreated	2002-8-16
pubmed:commentsCorrections	http://linkedlifedata.com/resource/pubmed/commentcorrection/12183616-12089450
pubmed:language	eng
pubmed:journal	http://linkedlifedata.com/resource/pubmed/journal/0404511
pubmed:citationSubset	IM
pubmed:chemical	http://linkedlifedata.com/resource/pubmed/chemical/GPI-Linked Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Gangliosides, http://linkedlifedata.com/resource/pubmed/chemical/Myelin Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Myelin-Associated Glycoprotein, http://linkedlifedata.com/resource/pubmed/chemical/NEPI-40 protein, rat, http://linkedlifedata.com/resource/pubmed/chemical/Nogo protein, http://linkedlifedata.com/resource/pubmed/chemical/Peptide Fragments, http://linkedlifedata.com/resource/pubmed/chemical/Receptor, Nerve Growth Factor, http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Cell Surface, http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Nerve Growth Factor, http://linkedlifedata.com/resource/pubmed/chemical/Rtn4r protein, mouse, http://linkedlifedata.com/resource/pubmed/chemical/Rtn4r protein, rat, http://linkedlifedata.com/resource/pubmed/chemical/myelin oligodendrocyte glycoprotein, http://linkedlifedata.com/resource/pubmed/chemical/rho GTP-Binding Proteins, http://linkedlifedata.com/resource/pubmed/chemical/trisialoganglioside GT1
pubmed:status	MEDLINE
pubmed:month	Aug
pubmed:issn	1095-9203
pubmed:author	pubmed-author:BloechlingerStefanS, pubmed-author:WoolfClifford JCJ
pubmed:issnType	Electronic
pubmed:day	16
pubmed:volume	297
pubmed:owner	NLM
pubmed:authorsComplete	Y
pubmed:pagination	1132-4
pubmed:dateRevised	2011-8-23
pubmed:meshHeading	pubmed-meshheading:12183616-Animals, pubmed-meshheading:12183616-Astrocytes, pubmed-meshheading:12183616-Axons, pubmed-meshheading:12183616-Binding, Competitive, pubmed-meshheading:12183616-Binding Sites, pubmed-meshheading:12183616-Central Nervous System, pubmed-meshheading:12183616-GPI-Linked Proteins, pubmed-meshheading:12183616-Gangliosides, pubmed-meshheading:12183616-Growth Cones, pubmed-meshheading:12183616-Models, Neurological, pubmed-meshheading:12183616-Myelin Proteins, pubmed-meshheading:12183616-Myelin-Associated Glycoprotein, pubmed-meshheading:12183616-Nerve Regeneration, pubmed-meshheading:12183616-Neurons, pubmed-meshheading:12183616-Oligodendroglia, pubmed-meshheading:12183616-Peptide Fragments, pubmed-meshheading:12183616-Protein Structure, Tertiary, pubmed-meshheading:12183616-Receptor, Nerve Growth Factor, pubmed-meshheading:12183616-Receptors, Cell Surface, pubmed-meshheading:12183616-Receptors, Nerve Growth Factor, pubmed-meshheading:12183616-Signal Transduction, pubmed-meshheading:12183616-Spinal Cord Injuries, pubmed-meshheading:12183616-rho GTP-Binding Proteins
pubmed:year	2002
pubmed:articleTitle	Neuroscience. It takes more than two to Nogo.
pubmed:affiliation	Neural Plasticity Research Group, Department of Anesthesia, Massachusetts General Hospital and Harvard Medical School, Boston, MA 02129, USA. woolf.clifford@mgh.harvard.edu
pubmed:publicationType	Journal Article, Comment