Abstract:
:The Alzheimer's disease amyloid protein precursor (APP) gene is part of a multi-gene super-family from which sixteen homologous amyloid precursor-like proteins (APLP) and APP species homologues have been isolated and characterised. Comparison of exon structure (including the uncharacterised APL-1 gene), construction of phylogenetic trees, and analysis of the protein sequence alignment of known homologues of the APP super-family were performed to reconstruct the evolution of the family and to assess the functional significance of conserved protein sequences between homologues. This analysis supports an adhesion function for all members of the APP super family, with specificity determined by those sequences which are not conserved between APLP lineages, and provides evidence for an increasingly complex APP superfamily during evolution. The analysis also suggests that Drosophila APPL and Caenorhabditis elegans APL-1 may be a fourth APLP lineage indicating that these proteins, while not functional homologues of human APP, are similarly likely to regulate cell adhesion. Furthermore, the betaA4 sequence is highly conserved only in APP orthologues, strongly suggesting this sequence is of significant functional importance in this lineage.
journal_name
Neurochem Intjournal_title
Neurochemistry internationalauthors
Coulson EJ,Paliga K,Beyreuther K,Masters CLdoi
10.1016/s0197-0186(99)00125-4subject
Has Abstractpub_date
2000-03-01 00:00:00pages
175-84issue
3eissn
0197-0186issn
1872-9754pii
S0197-0186(99)00125-4journal_volume
36pub_type
杂志文章,评审abstract::In the present investigation we address the question of whether one of the responses to increased neuronal activity is a modification of the expression of the different subunits of alpha-amino-3-hydroxy-5-methyl-4-isoxazole propionate (AMPA)-selective glutamate receptors (GluR-1, GluR-2, GluR-3). Thus, we used two dif...
journal_title:Neurochemistry international
pub_type: 杂志文章
doi:10.1016/0197-0186(94)90144-9
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abstract::Two puromycin-sensitive aminopeptidase isozymes (PSA-I and PSA-II) were isolated from chicken brain cytosol by ammonium sulfate fractionation followed by column chromatography on Cellex D and AH-Sepharose 4B and separated on Bio-Gel HTP. Each was purified to homogeneity on Sephadex G-200, Arg-Tyr-AH-Sepharose, Bio-Gel...
journal_title:Neurochemistry international
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journal_title:Neurochemistry international
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journal_title:Neurochemistry international
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journal_title:Neurochemistry international
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journal_title:Neurochemistry international
pub_type: 杂志文章
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journal_title:Neurochemistry international
pub_type: 杂志文章
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journal_title:Neurochemistry international
pub_type: 杂志文章
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journal_title:Neurochemistry international
pub_type: 杂志文章,评审
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journal_title:Neurochemistry international
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journal_title:Neurochemistry international
pub_type: 杂志文章
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journal_title:Neurochemistry international
pub_type: 杂志文章
doi:10.1016/j.neuint.2014.06.013
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journal_title:Neurochemistry international
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journal_title:Neurochemistry international
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journal_title:Neurochemistry international
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journal_title:Neurochemistry international
pub_type: 杂志文章,多中心研究
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journal_title:Neurochemistry international
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journal_title:Neurochemistry international
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journal_title:Neurochemistry international
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journal_title:Neurochemistry international
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journal_title:Neurochemistry international
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journal_title:Neurochemistry international
pub_type: 杂志文章
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journal_title:Neurochemistry international
pub_type: 杂志文章,评审
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journal_title:Neurochemistry international
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journal_title:Neurochemistry international
pub_type: 杂志文章
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journal_title:Neurochemistry international
pub_type: 杂志文章
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journal_title:Neurochemistry international
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