6371 - 6380 of 6568 Results
Title
Year
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OPENTitle: Impact of 100 LRRK2 variants linked to Parkinson's disease on kinase activity and microtubule bindingJournal Name: Biochemical JournalPublisher: Portland Press Ltd.Vol: 479Issue #: 17Start Page: 1759End Page: 1783Publication Date:Open Access(OA) Status: OPENLicense: cc-byDOI - Digital Object Identifier: 10.1042/bcj20220161Best OA location URL: https://portlandpress.com/biochemj/article-pdf/479/17/1759/936843/bcj-2022-0161.pdfCitation Count: 141
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OPENTitle: Endogenous Rab29 does not impact basal or stimulated LRRK2 pathway activityJournal Name: Biochemical JournalPublisher: Portland Press Ltd.Vol: 477Issue #: 22Start Page: 4397End Page: 4423Publication Date:Open Access(OA) Status: OPENLicense: cc-byDOI - Digital Object Identifier: 10.1042/bcj20200458Best OA location URL: https://portlandpress.com/biochemj/article-pdf/477/22/4397/898287/bcj-2020-0458.pdfCitation Count: 75
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OPENTitle: Deciphering the LRRK code: LRRK1 and LRRK2 phosphorylate distinct Rab proteins and are regulated by diverse mechanismsJournal Name: Biochemical JournalPublisher: Portland Press Ltd.Vol: 478Issue #: 3Start Page: 553End Page: 578Publication Date:Open Access(OA) Status: OPENLicense: cc-byDOI - Digital Object Identifier: 10.1042/bcj20200937Best OA location URL: https://portlandpress.com/biochemj/article-pdf/478/3/553/904049/bcj-2020-0937.pdfCitation Count: 54
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OPENTitle: PINK1-dependent phosphorylation of Serine111 within the SF3 motif of Rab GTPases impairs effector interactions and LRRK2-mediated phosphorylation at Threonine72Journal Name: Biochemical JournalPublisher: Portland Press Ltd.Vol: 477Issue #: 9Start Page: 1651End Page: 1668Publication Date:Open Access(OA) Status: OPENLicense: cc-by, cc-byDOI - Digital Object Identifier: 10.1042/bcj20190664Best OA location URL: https://portlandpress.com/biochemj/article-pdf/477/9/1651/878955/bcj-2019-0664.pdfCitation Count: 41
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OPENTitle: MHCII reduction is insufficient to protect mice from alpha-synuclein-induced degeneration and the Parkinson’s HLA locus exhibits epigenetic regulationJournal Name: Scientific ReportsPublisher: Springer Science and Business Media LLCVol: 15Issue #: 1Start Page: 13705End Page: 13705Publication Date:Open Access(OA) Status: OPENLicense: cc-byDOI - Digital Object Identifier: 10.1038/s41598-025-95679-3Best OA location URL: https://www.nature.com/articles/s41598-025-95679-3.pdfCitation Count: 1
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OPENTitle: Soluble and Insoluble Lysates from the Human A53T Mutant α-Synuclein Transgenic Mouse Model Induces α-Synucleinopathy Independent of Injection SiteJournal Name: International Journal of Molecular SciencesPublisher: MDPI AGVol: 26Issue #: 13Start Page: 6254End Page: 6254Publication Date:Open Access(OA) Status: OPENLicense: cc-byDOI - Digital Object Identifier: 10.3390/ijms26136254Best OA location URL: https://www.mdpi.com/1422-0067/26/13/6254/pdf?version=1751101536Citation Count: 4
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OPENTitle: Biochemical Fractionation of Human α-Synuclein in a Drosophila Model of SynucleinopathiesJournal Name: International Journal of Molecular SciencesPublisher: MDPI AGVol: 25Issue #: 7Start Page: 3643End Page: 3643Publication Date:Open Access(OA) Status: OPENLicense: cc-byDOI - Digital Object Identifier: 10.3390/ijms25073643Best OA location URL: https://www.mdpi.com/1422-0067/25/7/3643/pdf?version=1711354407Citation Count: 0
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OPENTitle: Structure-based design and characterization of Parkin-activating mutationsJournal Name: Life Science AlliancePublisher: Life Science Alliance, LLCVol: 6Issue #: 6Start Page: e202201419End Page: e202201419Publication Date:Open Access(OA) Status: OPENLicense: cc-by, cc-byDOI - Digital Object Identifier: 10.26508/lsa.202201419Best OA location URL: https://www.life-science-alliance.org/content/lsa/6/6/e202201419.full.pdfCitation Count: 31
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OPENTitle: USP30 sets a trigger threshold for PINK1–PARKIN amplification of mitochondrial ubiquitylationJournal Name: Life Science AlliancePublisher: Life Science Alliance, LLCVol: 3Issue #: 8Start Page: e202000768End Page: e202000768Publication Date:Open Access(OA) Status: OPENLicense: cc-by, cc-byDOI - Digital Object Identifier: 10.26508/lsa.202000768Best OA location URL: https://www.life-science-alliance.org/content/lsa/3/8/e202000768.full.pdfCitation Count: 131
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OPENTitle: A proteome-wide quantitative platform for nanoscale spatially resolved extraction of membrane proteins into native nanodiscsJournal Name: Nature MethodsPublisher: Springer Science and Business Media LLCVol: 22Issue #: 2Start Page: 412End Page: 421Publication Date:Open Access(OA) Status: OPENLicense: cc-byDOI - Digital Object Identifier: 10.1038/s41592-024-02517-xBest OA location URL: https://www.nature.com/articles/s41592-024-02517-x.pdfCitation Count: 12