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The hydrophobic residue Leu73 is crucial for the high stability and low aggregation properties of murine transthyretin
Author(s) -
Mei Nakagawa,
Takayuki Obita,
Mineyuki Mizuguchi
Publication year - 2022
Publication title -
biochemical journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.706
H-Index - 265
eISSN - 1470-8728
pISSN - 0264-6021
DOI - 10.1042/bcj20220203
Subject(s) - transthyretin , tetramer , thioflavin , chemistry , amyloidosis , mutant , amyloid (mycology) , protein aggregation , biophysics , biochemistry , mutation , fibril , protein folding , biology , enzyme , medicine , gene , endocrinology , inorganic chemistry , disease , alzheimer's disease

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