Title : Cellular oligomerization of alpha-synuclein is determined by the interaction of oxidized catechols with a C-terminal sequence.

Pub. Date : 2007 Oct 26

PMID : 17785456






6 Functional Relationships(s)
Download
Sentence
Compound Name
Protein Name
Organism
1 Cellular oligomerization of alpha-synuclein is determined by the interaction of oxidized catechols with a C-terminal sequence. Catechols synuclein alpha Homo sapiens
2 A critically important modulator of alpha-syn aggregation in vitro is dopamine and other catechols, which can prevent the formation of alpha-syn aggregates in cell-free and cellular model systems. Catechols synuclein alpha Homo sapiens
3 A critically important modulator of alpha-syn aggregation in vitro is dopamine and other catechols, which can prevent the formation of alpha-syn aggregates in cell-free and cellular model systems. Catechols synuclein alpha Homo sapiens
4 Despite the profound importance of this interaction for the pathogenesis of PD, the processes by which catechols alter alpha-syn aggregation are unclear. Catechols synuclein alpha Homo sapiens
5 The data show that the intracellular inhibition of alpha-syn aggregation requires the oxidation of catechols and the specific noncovalent interaction of the oxidized catechols with residues (125)YEMPS(129) in the C-terminal region of the protein. Catechols synuclein alpha Homo sapiens
6 The data show that the intracellular inhibition of alpha-syn aggregation requires the oxidation of catechols and the specific noncovalent interaction of the oxidized catechols with residues (125)YEMPS(129) in the C-terminal region of the protein. Catechols synuclein alpha Homo sapiens