Matches in Nanopublications for { ?s ?p "[Although the complex formation with hDAT occurs through the NAC domain of the alpha-synuclein variants, it is the familial Parkinson's disease-linked missense mutations present in the amino-terminal lipid binding domain of the alpha-synuclein variants that dictate the extent of the regulation of hDAT function.]. Sentence from MEDLINE/PubMed, a database of the U.S. National Library of Medicine."@en ?g. }
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- NP789637.RAlQOqh_KPYV3phfLe1W3V3tRPGXr12jWQdLoyvjDRWhY130_assertion description "[Although the complex formation with hDAT occurs through the NAC domain of the alpha-synuclein variants, it is the familial Parkinson's disease-linked missense mutations present in the amino-terminal lipid binding domain of the alpha-synuclein variants that dictate the extent of the regulation of hDAT function.]. Sentence from MEDLINE/PubMed, a database of the U.S. National Library of Medicine." NP789637.RAlQOqh_KPYV3phfLe1W3V3tRPGXr12jWQdLoyvjDRWhY130_provenance.
- NP302200.RAdy9J0EbI7aPgloffPt3NhUkrSkbcf8NOZChMwG3UiO4130_assertion description "[Although the complex formation with hDAT occurs through the NAC domain of the alpha-synuclein variants, it is the familial Parkinson's disease-linked missense mutations present in the amino-terminal lipid binding domain of the alpha-synuclein variants that dictate the extent of the regulation of hDAT function.]. Sentence from MEDLINE/PubMed, a database of the U.S. National Library of Medicine." NP302200.RAdy9J0EbI7aPgloffPt3NhUkrSkbcf8NOZChMwG3UiO4130_provenance.