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http://purl.uniprot.org/citations/16093393http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/16093393http://www.w3.org/2000/01/rdf-schema#comment"PolyADP-ribosylation is a transient posttranslational modification of proteins, mainly catalyzed by poly(ADP-ribose)polymerase-1 (PARP-1). This highly conserved nuclear protein is activated rapidly in response to DNA nick formation and promotes a fast DNA repair. Here, we examine a possible association between polyADP-ribosylation and the activity of neurotrophins and neuroprotective peptides taking part in life-or-death decisions in mammalian neurons. The presented results indicate an alternative mode of PARP-1 activation in the absence of DNA damage by neurotrophin-induced signaling mechanisms. PARP-1 was activated in rat cerebral cortical neurons briefly exposed to NGF-related nerve growth factors and to the neuroprotective peptides NAP (the peptide NAPVSIPQ, derived from the activity-dependent neuroprotective protein ADNP) and ADNF-9 (the peptide SALLRSIPA, derived from the activity-dependent neurotrophic factor ADNF) In addition, polyADP-ribosylation was involved in the neurotrophic activity of NGF-induced and NAP-induced neurite outgrowth in differentiating pheochromocytoma 12 cells as well as in the neuroprotective activity of NAP in neurons treated with the Alzheimer's disease neurotoxin beta-amyloid. A fast loosening of the highly condensed chromatin structure by polyADP-ribosylation of histone H1, which renders DNA accessible to transcription and repair, may underlie the role of polyADP-ribosylation in neurotrophic activity."xsd:string
http://purl.uniprot.org/citations/16093393http://purl.org/dc/terms/identifier"doi:10.1523/jneurosci.0333-05.2005"xsd:string
http://purl.uniprot.org/citations/16093393http://purl.uniprot.org/core/author"Klein R."xsd:string
http://purl.uniprot.org/citations/16093393http://purl.uniprot.org/core/author"Gozes I."xsd:string
http://purl.uniprot.org/citations/16093393http://purl.uniprot.org/core/author"Steingart R.A."xsd:string
http://purl.uniprot.org/citations/16093393http://purl.uniprot.org/core/author"Cohen-Armon M."xsd:string
http://purl.uniprot.org/citations/16093393http://purl.uniprot.org/core/author"Priel E."xsd:string
http://purl.uniprot.org/citations/16093393http://purl.uniprot.org/core/author"Visochek L."xsd:string
http://purl.uniprot.org/citations/16093393http://purl.uniprot.org/core/author"Vulih-Shultzman I."xsd:string
http://purl.uniprot.org/citations/16093393http://purl.uniprot.org/core/date"2005"xsd:gYear
http://purl.uniprot.org/citations/16093393http://purl.uniprot.org/core/name"J Neurosci"xsd:string
http://purl.uniprot.org/citations/16093393http://purl.uniprot.org/core/pages"7420-7428"xsd:string
http://purl.uniprot.org/citations/16093393http://purl.uniprot.org/core/title"PolyADP-ribosylation is involved in neurotrophic activity."xsd:string
http://purl.uniprot.org/citations/16093393http://purl.uniprot.org/core/volume"25"xsd:string
http://purl.uniprot.org/citations/16093393http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/16093393
http://purl.uniprot.org/citations/16093393http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/16093393
http://purl.uniprot.org/uniprot/P27008#attribution-9F1F827237B4FE89DDD3A6E95CD9A0D0http://purl.uniprot.org/core/sourcehttp://purl.uniprot.org/citations/16093393
http://purl.uniprot.org/uniprot/#_P27008-mappedCitation-16093393http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/16093393
http://purl.uniprot.org/uniprot/#_Q9JKL8-mappedCitation-16093393http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/16093393
http://purl.uniprot.org/uniprot/Q9JKL8http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/16093393
http://purl.uniprot.org/uniprot/P27008http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/16093393