Database of articles cited by EMDB/PDB/SASBDB data

Keywords
Structure methods	All X-ray diffraction NMR electron microscopy small angle scattering neutron diffraction fiber diffraction powder diffraction infrared spectroscopy EPR fluorescence transfer theoretical model Hybrid
Author
Journal
IF	>30 >20 >10 >5 all

Title	Conformational change of α-synuclein fibrils in cerebrospinal fluid from different clinical phases of Parkinson's disease.
Journal, issue, pages	Structure, Vol. 31, Issue 1, Page 78-87.e5, Year 2023
Publish date	Jan 5, 2023
Authors	Yun Fan / Yunpeng Sun / Wenbo Yu / Youqi Tao / Wencheng Xia / Yiqi Liu / Qinyue Zhao / Yilin Tang / Yimin Sun / Fengtao Liu / Qin Cao / Jianjun Wu / Cong Liu / Jian Wang / Dan Li /
PubMed Abstract	α-Synuclein (α-syn) has been shown to form various conformational fibrils associated with different synucleinopathies. But whether the conformation of α-syn fibrils changes during disease ...α-Synuclein (α-syn) has been shown to form various conformational fibrils associated with different synucleinopathies. But whether the conformation of α-syn fibrils changes during disease progression is unclear. Here, we amplified α-syn aggregates from the cerebrospinal fluid (CSF) of patients with Parkinson's disease (PD) staged in preclinical PD (pre-PD), middle- to late-stage PD (mid-PD), and late-stage PD (late-PD). Our results show that α-syn fibrils derived from the late-PD patient are most potent in inducing endogenous α-syn aggregation in primary neurons, followed by the mid-PD and pre-PD fibrils. By using cryo-electron microscopy, we further determined the high-resolution structures of the CSF-amplified fibrils. The structures exhibit remarkable differences in a minor but significant population of conformational species in different staged samples. Our work demonstrates structural and pathological differences between α-syn fibrils derived from PD patients at a spectrum of clinical stages, which suggests potential conformational transition of α-syn fibrils during the progression of PD.
External links	Structure / PubMed:36513068
Methods	EM (helical sym.)
Resolution	2.6 - 3.4 Å
Structure data	31702 7v47 8h03 EMDB-31702, PDB-7v47: Type 1A alpha-synuclein fibril seeded by cerebrospinal fluid from a preclinical Parkinson's disease patient PDB-8h03: Major polymorph in alpha-synuclein fibril seeded by cerebrospinal fluid from a preclinical Parkinson's disease patient Method: EM (helical sym.) / Resolution: 2.8 Å 31703 7v48 8h04 EMDB-31703, PDB-7v48: Type 1D alpha-synuclein fibril seeded by cerebrospinal fluid from a postmortal Parkinson's disease patient PDB-8h04: Major polymorph in alpha-synuclein fibril seeded by cerebrospinal fluid from a postmortal Parkinson's disease patient Method: EM (helical sym.) / Resolution: 3.0 Å 31704 7v49 8h05 EMDB-31704, PDB-7v49: Type 4 alpha-synuclein fibril seeded by cerebrospinal fluid from a postmortal Parkinson's disease patient PDB-8h05: Minor polymorph in alpha-synuclein fibril seeded by cerebrospinal fluid from a postmortal Parkinson's disease patient Method: EM (helical sym.) / Resolution: 3.4 Å 33332 7xo0 EMDB-33332, PDB-7xo0: Minor polymorph inalpha-synuclein fibril seeded by cerebrospinal fluid from a mid-to-late stage (mid-PD-1) Parkinson's disease patient Method: EM (helical sym.) / Resolution: 3.0 Å 33333 7xo1 EMDB-33333, PDB-7xo1: Major polymorph in alpha-synuclein fibril seeded by cerebrospinal fluid from a mid-to-late stage (mid-PD-1) Parkinson's disease patient Method: EM (helical sym.) / Resolution: 3.0 Å 33334 7xo2 EMDB-33334, PDB-7xo2: Minor polymorph in alpha-synuclein fibril seeded by cerebrospinal fluid from a mid-to-late stage (mid-PD-4) Parkinson's disease patient Method: EM (helical sym.) / Resolution: 3.0 Å 33335 7xo3 EMDB-33335, PDB-7xo3: Type 1C alpha-synuclein fibril seeded by cerebrospinal fluid from a mid-to-late stage (mid-PD-4) Parkinson's disease patient Method: EM (helical sym.) / Resolution: 2.6 Å
Source	homo sapiens (human)
Keywords	PROTEIN FIBRIL / amyloid fibril