The N terminus of α-synuclein dictates fibril formation.

Autor: McGlinchey RP; Laboratory of Protein Conformation and Dynamics, Biochemistry and Biophysics Center, National Heart, Lung, and Blood Institute, Bethesda, MD 20892., Ni X; Laboratory of Membrane Proteins and Structural Biology, Biochemistry and Biophysics Center, National Heart, Lung, and Blood Institute, Bethesda, MD 20892., Shadish JA; Laboratory of Protein Conformation and Dynamics, Biochemistry and Biophysics Center, National Heart, Lung, and Blood Institute, Bethesda, MD 20892., Jiang J; Laboratory of Membrane Proteins and Structural Biology, Biochemistry and Biophysics Center, National Heart, Lung, and Blood Institute, Bethesda, MD 20892., Lee JC; Laboratory of Protein Conformation and Dynamics, Biochemistry and Biophysics Center, National Heart, Lung, and Blood Institute, Bethesda, MD 20892; leej4@nhlbi.nih.gov.

Publikováno v: Proceedings of the National Academy of Sciences of the United States of America [Proc Natl Acad Sci U S A] 2021 Aug 31; Vol. 118 (35).

The Parkinson's disease risk gene cathepsin B promotes fibrillar alpha-synuclein clearance, lysosomal function and glucocerebrosidase activity in dopaminergic neurons.

Autor: Jones-Tabah, Jace^1,2 (AUTHOR), He, Kathy¹ (AUTHOR), Karpilovsky, Nathan¹ (AUTHOR), Senkevich, Konstantin^1,2 (AUTHOR), Deyab, Ghislaine¹ (AUTHOR), Pietrantonio, Isabella¹ (AUTHOR), Goiran, Thomas¹ (AUTHOR), Cousineau, Yuting² (AUTHOR), Nikanorova, Daria³ (AUTHOR), Goldsmith, Taylor⁴ (AUTHOR), del Cid Pellitero, Esther¹ (AUTHOR), Chen, Carol X.-Q.⁴ (AUTHOR), Luo, Wen⁴ (AUTHOR), You, Zhipeng⁴ (AUTHOR), Abdian, Narges⁴ (AUTHOR), Ahmad, Jamil^1,2 (AUTHOR), Ruskey, Jennifer A.^1,2 (AUTHOR), Asayesh, Farnaz^1,5 (AUTHOR), Spiegelman, Dan¹ (AUTHOR), Fahn, Stanley⁶ (AUTHOR)

Publikováno v: Molecular Neurodegeneration. 11/25/2024, Vol. 19 Issue 1, p1-21. 21p.

A characterization of Gaucher iPS-derived astrocytes: Potential implications for Parkinson's disease.

Autor: Aflaki E; Section of Molecular Neurogenetics, National Human Genome Research Institute, NIH, Bethesda, MD 20892, United States of America., Stubblefield BK; Section of Molecular Neurogenetics, National Human Genome Research Institute, NIH, Bethesda, MD 20892, United States of America., McGlinchey RP; Laboratory of Protein Conformation and Dynamics, National Heart Lung and Blood Institute, NIH, Bethesda, MD 20892, United States of America., McMahon B; Section of Molecular Neurogenetics, National Human Genome Research Institute, NIH, Bethesda, MD 20892, United States of America., Ory DS; Department of Medicine, Washington University School of Medicine, St. Louis, MO 63110, United States of America., Sidransky E; Section of Molecular Neurogenetics, National Human Genome Research Institute, NIH, Bethesda, MD 20892, United States of America. Electronic address: sidranse@mail.nih.gov.

Publikováno v: Neurobiology of disease [Neurobiol Dis] 2020 Feb; Vol. 134, pp. 104647. Date of Electronic Publication: 2019 Nov 10.

The autophagy-lysosome pathway: a potential target in the chemical and gene therapeutic strategies for Parkinson's disease.

Autor: Jiao F; School of Mental Health, Jining Medical University, Jining, Shandong Province, China.; Shandong Collaborative Innovation Center for Diagnosis, Treatment and Behavioral Interventions of Mental Disorders, Institute of Mental Health, Jining Medical University, Jining, Shandong Province, China., Meng L; School of Mental Health, Jining Medical University, Jining, Shandong Province, China., Du K; School of Mental Health, Jining Medical University, Jining, Shandong Province, China., Li X; School of Mental Health, Jining Medical University, Jining, Shandong Province, China.; Shandong Collaborative Innovation Center for Diagnosis, Treatment and Behavioral Interventions of Mental Disorders, Institute of Mental Health, Jining Medical University, Jining, Shandong Province, China.

Publikováno v: Neural regeneration research [Neural Regen Res] 2025 Jan 01; Vol. 20 (1), pp. 139-158. Date of Electronic Publication: 2024 Jan 31.

C-terminal α-synuclein truncations are linked to cysteine cathepsin activity in Parkinson's disease.

Autor: McGlinchey RP; From the Laboratory of Protein Conformation and Dynamics, Biochemistry and Biophysics Center, National Heart, Lung, and Blood Institute and., Lacy SM; From the Laboratory of Protein Conformation and Dynamics, Biochemistry and Biophysics Center, National Heart, Lung, and Blood Institute and., Huffer KE; From the Laboratory of Protein Conformation and Dynamics, Biochemistry and Biophysics Center, National Heart, Lung, and Blood Institute and., Tayebi N; Medical Genetics Branch, National Human Genome Research Institute, National Institutes of Health, Bethesda, Maryland 20892., Sidransky E; Medical Genetics Branch, National Human Genome Research Institute, National Institutes of Health, Bethesda, Maryland 20892., Lee JC; From the Laboratory of Protein Conformation and Dynamics, Biochemistry and Biophysics Center, National Heart, Lung, and Blood Institute and leej4@nhlbi.nih.gov.

Publikováno v: The Journal of biological chemistry [J Biol Chem] 2019 Jun 21; Vol. 294 (25), pp. 9973-9984. Date of Electronic Publication: 2019 May 15.