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	Repositioning of polyubiquitin alters the pathologic tau filament structure.
Journal, issue, pages	Nat Struct Mol Biol, Year 2026
Publish date	Aug 31, 2026
Authors	Ryohei Watanabe / Benjamin C Creekmore / Nabil F Darwich / Courtney L Smith / Hong Xu / Angelina Baltazar / Sacha Salphati / Lakshmi Changolkar / Kevt'her Hoxha / Bin Zhang / Caroline M O'Rourke / George M Burslem / Virginia M-Y Lee / Yi-Wei Chang / Edward B Lee /
PubMed Abstract	Structurally diverse tau filaments form proteinaceous aggregates in a heterogeneous group of neurodegenerative diseases called tauopathies. The factors extrinsic to the highly ordered core structure ...Structurally diverse tau filaments form proteinaceous aggregates in a heterogeneous group of neurodegenerative diseases called tauopathies. The factors extrinsic to the highly ordered core structure that influence tau filament stability are not well understood. Here, we found that polyubiquitinated tau filaments from Alzheimer disease and vacuolar tauopathy human brain tissue exhibit distinct seeding patterns in mice, in association with differences in tau filament ultrastructure determined by cryo-electron microscopy. Chemical modulation of the polarity of polyubiquitin adjacent to the tau core with the small molecule ubistatin B resulted in the repositioning of poorly structured densities toward positively charged residues on the highly structured core filament, leading to shifting of the protofilament-protofilament interface of certain vacuolar tauopathy tau filaments. These results suggest that the structure of tau filaments that are associated with different seeding activities in vivo can be influenced by post-translational modifications.
External links	Nat Struct Mol Biol / PubMed:42675211
Methods	EM (helical sym.)
Resolution	2.9 - 5.32 Å
Structure data	EMDB-73621: u-VT Ie tau filament from VT Case 3 Method: EM (helical sym.) / Resolution: 3.98 Å EMDB-73624: u-VT II tau filament from VT Case 3 Method: EM (helical sym.) / Resolution: 3.8 Å EMDB-73626: u-VT IV tau filament from VT Case 3 Method: EM (helical sym.) / Resolution: 3.69 Å 75271 10ln EMDB-75271, PDB-10ln: VT Ia tau filament from VT Case 1 Method: EM (helical sym.) / Resolution: 2.92 Å 75292 10mr EMDB-75292, PDB-10mr: VT II tau filament from VT Case 1 Method: EM (helical sym.) / Resolution: 3.14 Å 75293 10ms EMDB-75293, PDB-10ms: VT IV tau filament from VT Case 2 Method: EM (helical sym.) / Resolution: 3.24 Å 75308 10no EMDB-75308, PDB-10no: u-VT Ia tau filament from VT Case 2 Method: EM (helical sym.) / Resolution: 2.96 Å 75309 10np EMDB-75309, PDB-10np: u-VT Ib tau filament from VT Case 1 Method: EM (helical sym.) / Resolution: 3.51 Å 75310 10nq EMDB-75310, PDB-10nq: u-VT Ic tau filament from VT Case 1 Method: EM (helical sym.) / Resolution: 3.61 Å 75311 10nr EMDB-75311, PDB-10nr: u-VT II tau filament from VT Case 1 Method: EM (helical sym.) / Resolution: 3.37 Å 75313 10nt EMDB-75313, PDB-10nt: u-VT IV tau filament from VT Case 1 Method: EM (helical sym.) / Resolution: 3.05 Å EMDB-75314: AD PHF tau filament from AD Case 1 Method: EM (helical sym.) / Resolution: 3.5 Å EMDB-75315: AD SF tau filament from AD Case 1 Method: EM (helical sym.) / Resolution: 4.51 Å EMDB-75316: AD PHF tau filament from AD Case 2 Method: EM (helical sym.) / Resolution: 3.51 Å EMDB-75317: AD SF tau filament from AD Case 2 Method: EM (helical sym.) / Resolution: 4.36 Å EMDB-75318: VT III tau filament from VT Case 1 Method: EM (helical sym.) / Resolution: 3.77 Å EMDB-75319: VT IV tau filament from VT Case 1 Method: EM (helical sym.) / Resolution: 3.49 Å EMDB-75320: VT V tau filament from VT Case 1 Method: EM (helical sym.) / Resolution: 4.19 Å EMDB-75321: VT II tau filament from VT Case 2 Method: EM (helical sym.) / Resolution: 3.74 Å EMDB-75322: VT V tau filament from VT Case 2 Method: EM (helical sym.) / Resolution: 4.23 Å EMDB-75323: VT Ia tau filament from VT Case 2 Method: EM (helical sym.) / Resolution: 2.96 Å EMDB-75324: VT Ia tau filament from VT Case 3 Method: EM (helical sym.) / Resolution: 2.9 Å EMDB-75325: VT II tau filament from VT Case 3 Method: EM (helical sym.) / Resolution: 3.64 Å EMDB-75326: u-AD PHF tau filament from AD Case 1 Method: EM (helical sym.) / Resolution: 3.54 Å EMDB-75327: u-VT Id tau filament from VT Case 1 Method: EM (helical sym.) / Resolution: 3.8 Å EMDB-75328: u-AD SF tau filament from AD Case 2 Method: EM (helical sym.) / Resolution: 4.77 Å EMDB-75329: u-AD PHF tau filament from AD Case 2 Method: EM (helical sym.) / Resolution: 3.32 Å EMDB-75330: u-AD SF tau filament from AD Case 1 Method: EM (helical sym.) / Resolution: 3.7 Å EMDB-75331: VT IV tau filament from VT Case 3 Method: EM (helical sym.) / Resolution: 3.19 Å EMDB-75355: u-VT Ie tau filament from VT Case 1 Method: EM (helical sym.) / Resolution: 4.82 Å EMDB-75356: u-VT If tau filament from VT Case 1 Method: EM (helical sym.) / Resolution: 4.19 Å EMDB-75357: u-VT III tau filament from VT Case 1 Method: EM (helical sym.) / Resolution: 3.88 Å EMDB-75358: u-VT V tau filament from VT Case 1 Method: EM (helical sym.) / Resolution: 5.18 Å EMDB-75359: u-VT PHF tau filament from VT Case 1 Method: EM (helical sym.) / Resolution: 4.23 Å EMDB-75360: u-VT Ie tau filament from VT Case 2 Method: EM (helical sym.) / Resolution: 4.32 Å EMDB-75361: u-VT II tau filament from VT Case 2 Method: EM (helical sym.) / Resolution: 3.77 Å EMDB-75362: u-VT IV tau filament from VT Case 2 Method: EM (helical sym.) / Resolution: 4.82 Å EMDB-75363: u-VT V tau filament from VT Case 2 Method: EM (helical sym.) / Resolution: 5.32 Å
Source	homo sapiens (human)
Keywords	STRUCTURAL PROTEIN / Microtubule-associated protein