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	Cryo-EM structures of four polymorphic TDP-43 amyloid cores.
Journal, issue, pages	Nat Struct Mol Biol, Vol. 26, Issue 7, Page 619-627, Year 2019
Publish date	Jun 24, 2019
Authors	Qin Cao / David R Boyer / Michael R Sawaya / Peng Ge / David S Eisenberg /
PubMed Abstract	The DNA and RNA processing protein TDP-43 undergoes both functional and pathogenic aggregation. Functional TDP-43 aggregates form reversible, transient species such as nuclear bodies, stress ...The DNA and RNA processing protein TDP-43 undergoes both functional and pathogenic aggregation. Functional TDP-43 aggregates form reversible, transient species such as nuclear bodies, stress granules, and myo-granules. Pathogenic, irreversible TDP-43 aggregates form in amyotrophic lateral sclerosis and other neurodegenerative conditions. Here we find the features of TDP-43 fibrils that confer both reversibility and irreversibility by determining structures of two segments reported to be the pathogenic cores of human TDP-43 aggregation: SegA (residues 311-360), which forms three polymorphs, all with dagger-shaped folds; and SegB A315E (residues 286-331 containing the amyotrophic lateral sclerosis hereditary mutation A315E), which forms R-shaped folds. Energetic analysis suggests that the dagger-shaped polymorphs represent irreversible fibril structures, whereas the SegB polymorph may participate in both reversible and irreversible fibrils. Our structures reveal the polymorphic nature of TDP-43 and suggest how the A315E mutation converts the R-shaped polymorph to an irreversible form that enhances pathology.
External links	Nat Struct Mol Biol / PubMed:31235914 / PubMed Central
Methods	EM (helical sym.)
Resolution	3.3 - 3.8 Å
Structure data	0334 6n3c EMDB-0334, PDB-6n3c: SegB, conformation of TDP-43 low complexity domain segment A Method: EM (helical sym.) / Resolution: 3.3 Å 9339 6n37 EMDB-9339, PDB-6n37: SegA-sym, conformation of TDP-43 low complexity domain segment A sym Method: EM (helical sym.) / Resolution: 3.8 Å 9349 6n3a EMDB-9349, PDB-6n3a: SegA-long, conformation of TDP-43 low complexity domain segment A long Method: EM (helical sym.) / Resolution: 3.3 Å 9350 6n3b EMDB-9350, PDB-6n3b: SegA-asym, conformation of TDP-43 low complexity domain segment A asym Method: EM (helical sym.) / Resolution: 3.8 Å
Source	homo sapiens (human)
Keywords	PROTEIN FIBRIL / Amyloid / TDP43 / ALS / FTLD-TDP / dna binding protein