Native state hydrogen exchange study of suppressor and pathogenic variants of transthyretin

Journal of Molecular Biology

Volumn 320, Issue 4, 2002, Pages 821-832

  Liu, Kai ^a   Kelly, Jeffery W ^a   Wemmer, David E ^b,c  

^a SCRIPPS RESEARCH INSTITUTE   (United States)

^b UNIVERSITY OF CALIFORNIA   (United States)

^c LAWRENCE BERKELEY NATIONAL LABORATORY   (United States)

Author keywords

Amyloid; Hydrogen exchange; NMR spectroscopy; Protection factor; Transthyretin

Indexed keywords

PREALBUMIN;

AMYLOID NEUROPATHY; ARTICLE; DISEASE CARRIER; FAMILIAL DISEASE; HUMAN; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PATHOGENESIS; PRIORITY JOURNAL; PROTEIN STABILITY; PROTEIN VARIANT; PROTON TRANSPORT;

EID: 0036306257     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0022-2836(02)00471-0     Document Type: Article

References (24)

1. Structure of complex of two plasma proteins - Transthyretin and retinol-binding protein
2. The acid-mediated denaturation pathway of transthyretin yields a conformational intermediate that can self-assemble into amyloid
3. A glimpse of a possible amyloidogenic intermediate of transthyretin
4. Transthyretin slowly exchanges subunits under physiological conditions: A convenient chromatographic method to study subunit exchange in oligomeric proteins
5. The amyloidogenic potential of transthyretin variants correlates with their tendency to aggregate in solution
6. Deuterium-proton exchange on the native wild-type transthyretin tetramer identifies the stable core of the individual subunits and indicates mobility at the subunit interface
7. Structure of Val122ile variant transthyretin - A cardiomyopathic mutant
8. The X-ray crystal structure refinements of normal human transthyretin and the amyloidogenic Val-30.fwdarw. Met variant to 1.7 Angstorm resolution
9. A comparative analysis of 23 structures of the amyloidogenic protein transthyretin
10. Transthyretin stability as a key factor in amyloidogenesis: X-ray analysis at atomic resolution
11. The crystal structure of amyloidogenic Leu(55) → Pro transthyretin variant reveals a possible pathway for transthyretin polymerization into amyloid fibrils
12. Structure of Met30 variant of transthyretin and its amyloidogenic implications
13. Instability, unfolding and aggregation of human lysozyme variants underlying amyloid fibrillogenesis
14. Alternative conformations of amyloidogenic proteins govern their behavior
15. Amyloid fibrils - Mutations make enzyme polymerize
16. From the globular to the fibrous state: Protein structure and structural conversion in amyloid formation
17. A suite of triple resonance NMR experiments for the backbone assignment of N-15, C-13, H-2 labeled proteins with high sensitivity
18. Primary structure effects on peptide group hydrogen exchange
19. Isotope effects in peptide group hydrogen exchange
20. Structural and genetic analysis of the folding and function of T4 lysozyme
21. Thyroxine binding to transthyretin (TTR) variants - Two variants (TTR Pro55 and TTR Met111) with a particularly low binding affinity
22. Comparative calorimetric study of non-amyloidogenic and amyloidogenic variants of the homotetrameric protein transthyretin
23. Intermolecular disulfide linkages are not required for transthyretin amyloid fibril formation in vitro