248 related articles for article (PubMed ID: 24138030)
1. Over-expression of an inactive mutant cathepsin D increases endogenous alpha-synuclein and cathepsin B activity in SH-SY5Y cells.
Crabtree D; Dodson M; Ouyang X; Boyer-Guittaut M; Liang Q; Ballestas ME; Fineberg N; Zhang J
J Neurochem; 2014 Mar; 128(6):950-61. PubMed ID: 24138030
[TBL] [Abstract][Full Text] [Related]
2. Recombinant pro-CTSD (cathepsin D) enhances SNCA/α-Synuclein degradation in α-Synucleinopathy models.
Prieto Huarcaya S; Drobny A; Marques ARA; Di Spiezio A; Dobert JP; Balta D; Werner C; Rizo T; Gallwitz L; Bub S; Stojkovska I; Belur NR; Fogh J; Mazzulli JR; Xiang W; Fulzele A; Dejung M; Sauer M; Winner B; Rose-John S; Arnold P; Saftig P; Zunke F
Autophagy; 2022 May; 18(5):1127-1151. PubMed ID: 35287553
[TBL] [Abstract][Full Text] [Related]
3. Cysteine cathepsins are essential in lysosomal degradation of α-synuclein.
McGlinchey RP; Lee JC
Proc Natl Acad Sci U S A; 2015 Jul; 112(30):9322-7. PubMed ID: 26170293
[TBL] [Abstract][Full Text] [Related]
4. Lysosomal enzyme cathepsin D protects against alpha-synuclein aggregation and toxicity.
Qiao L; Hamamichi S; Caldwell KA; Caldwell GA; Yacoubian TA; Wilson S; Xie ZL; Speake LD; Parks R; Crabtree D; Liang Q; Crimmins S; Schneider L; Uchiyama Y; Iwatsubo T; Zhou Y; Peng L; Lu Y; Standaert DG; Walls KC; Shacka JJ; Roth KA; Zhang J
Mol Brain; 2008 Nov; 1():17. PubMed ID: 19021916
[TBL] [Abstract][Full Text] [Related]
5. Cathepsin D is the main lysosomal enzyme involved in the degradation of alpha-synuclein and generation of its carboxy-terminally truncated species.
Sevlever D; Jiang P; Yen SH
Biochemistry; 2008 Sep; 47(36):9678-87. PubMed ID: 18702517
[TBL] [Abstract][Full Text] [Related]
6. Lysosomal enzyme cathepsin B enhances the aggregate forming activity of exogenous α-synuclein fibrils.
Tsujimura A; Taguchi K; Watanabe Y; Tatebe H; Tokuda T; Mizuno T; Tanaka M
Neurobiol Dis; 2015 Jan; 73():244-53. PubMed ID: 25466281
[TBL] [Abstract][Full Text] [Related]
7. Mannose 6-Phosphate Receptor Is Reduced in -Synuclein Overexpressing Models of Parkinsons Disease.
Matrone C; Dzamko N; Madsen P; Nyegaard M; Pohlmann R; Søndergaard RV; Lassen LB; Andresen TL; Halliday GM; Jensen PH; Nielsen MS
PLoS One; 2016; 11(8):e0160501. PubMed ID: 27509067
[TBL] [Abstract][Full Text] [Related]
8. Lysosomal response in relation to α-synuclein pathology differs between Parkinson's disease and multiple system atrophy.
Puska G; Lutz MI; Molnar K; Regelsberger G; Ricken G; Pirker W; Laszlo L; Kovacs GG
Neurobiol Dis; 2018 Jun; 114():140-152. PubMed ID: 29505813
[TBL] [Abstract][Full Text] [Related]
9. Activation of β-Glucocerebrosidase Reduces Pathological α-Synuclein and Restores Lysosomal Function in Parkinson's Patient Midbrain Neurons.
Mazzulli JR; Zunke F; Tsunemi T; Toker NJ; Jeon S; Burbulla LF; Patnaik S; Sidransky E; Marugan JJ; Sue CM; Krainc D
J Neurosci; 2016 Jul; 36(29):7693-706. PubMed ID: 27445146
[TBL] [Abstract][Full Text] [Related]
10. Tctex1 plays a key role in the α-synuclein autophagy lysosomal degradation pathway.
Dong S; Zhang Y; Ming J; Zhang X; Li X; Xu J; Sun Z; Cai Z; Li X
Neurosci Lett; 2017 Nov; 661():90-95. PubMed ID: 28970129
[TBL] [Abstract][Full Text] [Related]
11. Rotenone impairs autophagic flux and lysosomal functions in Parkinson's disease.
Wu F; Xu HD; Guan JJ; Hou YS; Gu JH; Zhen XC; Qin ZH
Neuroscience; 2015 Jan; 284():900-911. PubMed ID: 25446361
[TBL] [Abstract][Full Text] [Related]
12. Triptolide Promotes the Clearance of α-Synuclein by Enhancing Autophagy in Neuronal Cells.
Hu G; Gong X; Wang L; Liu M; Liu Y; Fu X; Wang W; Zhang T; Wang X
Mol Neurobiol; 2017 Apr; 54(3):2361-2372. PubMed ID: 26957304
[TBL] [Abstract][Full Text] [Related]
13. Expression of A53T mutant but not wild-type alpha-synuclein in PC12 cells induces alterations of the ubiquitin-dependent degradation system, loss of dopamine release, and autophagic cell death.
Stefanis L; Larsen KE; Rideout HJ; Sulzer D; Greene LA
J Neurosci; 2001 Dec; 21(24):9549-60. PubMed ID: 11739566
[TBL] [Abstract][Full Text] [Related]
14. C-terminal α-synuclein truncations are linked to cysteine cathepsin activity in Parkinson's disease.
McGlinchey RP; Lacy SM; Huffer KE; Tayebi N; Sidransky E; Lee JC
J Biol Chem; 2019 Jun; 294(25):9973-9984. PubMed ID: 31092553
[TBL] [Abstract][Full Text] [Related]
15. Extracellular α-synuclein impairs sphingosine 1-phosphate receptor type 3 (S1PR3)-regulated lysosomal delivery of cathepsin D in HeLa cells.
Nishida S; Matovelo SA; Kajimoto T; Nakamura SI; Okada T
Genes Cells; 2024 Mar; 29(3):207-216. PubMed ID: 38163647
[TBL] [Abstract][Full Text] [Related]
16. Upregulation of the p53-p21 pathway by G2019S LRRK2 contributes to the cellular senescence and accumulation of α-synuclein.
Ho DH; Seol W; Son I
Cell Cycle; 2019 Feb; 18(4):467-475. PubMed ID: 30712480
[TBL] [Abstract][Full Text] [Related]
17. α-Synuclein Overexpression Induces Lysosomal Dysfunction and Autophagy Impairment in Human Neuroblastoma SH-SY5Y.
Nascimento AC; Erustes AG; Reckziegel P; Bincoletto C; Ureshino RP; Pereira GJS; Smaili SS
Neurochem Res; 2020 Nov; 45(11):2749-2761. PubMed ID: 32915398
[TBL] [Abstract][Full Text] [Related]
18. Alterations in lysosomal and proteasomal markers in Parkinson's disease: relationship to alpha-synuclein inclusions.
Chu Y; Dodiya H; Aebischer P; Olanow CW; Kordower JH
Neurobiol Dis; 2009 Sep; 35(3):385-98. PubMed ID: 19505575
[TBL] [Abstract][Full Text] [Related]
19. Familial knockin mutation of LRRK2 causes lysosomal dysfunction and accumulation of endogenous insoluble α-synuclein in neurons.
Schapansky J; Khasnavis S; DeAndrade MP; Nardozzi JD; Falkson SR; Boyd JD; Sanderson JB; Bartels T; Melrose HL; LaVoie MJ
Neurobiol Dis; 2018 Mar; 111():26-35. PubMed ID: 29246723
[TBL] [Abstract][Full Text] [Related]
20. Glucocerebrosidase activity, cathepsin D and monomeric α-synuclein interactions in a stem cell derived neuronal model of a PD associated GBA1 mutation.
Yang SY; Gegg M; Chau D; Schapira A
Neurobiol Dis; 2020 Feb; 134():104620. PubMed ID: 31634558
[TBL] [Abstract][Full Text] [Related]
[Next] [New Search]