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	Structures of dye-bound transthyretin amyloid fibrils from abdominal fat biopsies.
Journal, issue, pages	Nat Commun, Vol. 17, Issue 1, Year 2026
Publish date	Apr 24, 2026
Authors	Boyuan Ma / Yuxuan Yao / Qingping Wang / Qinyue Zhao / Kaien Liu / Feiyang Chen / Hui Cheng / Ruxu Zhang / Cong Liu / Dan Li /
PubMed Abstract	Transthyretin (TTR) amyloidosis is a protein misfolding disease characterized by amyloid fibril deposition in vital organs, leading to cardiomyopathy (ATTR-CM). Early diagnosis of ATTR-CM remains ...Transthyretin (TTR) amyloidosis is a protein misfolding disease characterized by amyloid fibril deposition in vital organs, leading to cardiomyopathy (ATTR-CM). Early diagnosis of ATTR-CM remains challenging due to lack of sensitive, rapid screening methods. Here, we report cryo-EM structures of TTR amyloid fibrils extracted from minimally invasive abdominal fat-pad biopsies of three living Ala97Ser ATTR-CM patients. The adipose-derived fibril structures closely mirror those from diseased post-mortem cardiac tissues, validating the use of fat-pad biopsies to investigate the atomic structure of TTR fibrils in living patients. Furthermore, we determined cryo-EM structures of TTR fibrils in complex with two amyloid-binding dyes, Congo Red (CR) and Thioflavin S (ThS), which are widely used in the clinical diagnosis of ATTR-CM. Both CR and ThS predominantly bind to a specific surface arginine site on the TTR fibril via electrostatic interactions. These findings provide structural insights into how small-molecule dyes bind TTR fibrils, offering a molecular foundation for the rational design of TTR-specific tracers to enable early and accurate diagnosis of TTR amyloidosis.
External links	Nat Commun / PubMed:42026093 / PubMed Central
Methods	EM (helical sym.)
Resolution	3.0 - 3.3 Å
Structure data	65344 9vtw EMDB-65344, PDB-9vtw: Cryo-EM structure of ATTRA97S amyloid fibrils extracted from patient-derived abdominal adipose biopsy tissue. Method: EM (helical sym.) / Resolution: 3.0 Å 65345 9vtx EMDB-65345, PDB-9vtx: Cryo-EM structure of Congo Red-bound ATTRA97S amyloid fibrils extracted from patient-derived abdominal adipose biopsy tissu Method: EM (helical sym.) / Resolution: 3.0 Å 65346 9vty EMDB-65346, PDB-9vty: Cryo-EM structure of ThS-bound ATTRA97S amyloid fibrils extracted from patient-derived abdominal adipose biopsy tissue. Method: EM (helical sym.) / Resolution: 3.3 Å 67024 9xmg EMDB-67024, PDB-9xmg: Cryo-EM structure of ATTRA97S amyloid fibrils extracted from patient-derived abdominal adipose biopsy tissue (patient 2). Method: EM (helical sym.) / Resolution: 3.3 Å 67025 9xmi EMDB-67025, PDB-9xmi: Cryo-EM structure of ATTRA97S amyloid fibrils extracted from patient-derived abdominal adipose biopsy tissue (patient 3). Method: EM (helical sym.) / Resolution: 3.2 Å
Chemicals	ChemComp-CGO: sodium 3,3'-(1E,1'E)-biphenyl-4,4'-diylbis(diazene-2,1-diyl)bis(4-aminonaphthalene-1-sulfonate) PDB-1etv: THE CRYSTAL STRUCTURE OF E. COLI FIS MUTANT G72A
Source	homo sapiens (human)
Keywords	PROTEIN FIBRIL / amyloid / protein fibril.