Prion-like domain disease-causing mutations and misregulation of alternative splicing relevance in limb-girdle muscular dystrophy (LGMD) 1G  

作　　者：Cristina Batlle Salvador Ventura 

机构地区：[1]Departament de Bioquímica i Biologia Molecular and Institut de Biotecnologia i Biomedicina,Universitat Autònoma de Barcelona,Bellaterra,Spain

出　　处：《Neural Regeneration Research》2020年第12期2239-2240,共2页中国神经再生研究（英文版）

摘　　要：Human prion-like proteins often correspond to nucleic acid binding proteins,displaying both globular domains and long intrinsically disordered regions(IDRs)(Harrison and Shorter,2017).Their IDRs are of low complexity and resemble in amino acid composition to the disordered yeast prion domains,being usually enriched in Gln and Asn residues and depleted in hydrophobic and charged residues.Accordingly,these sequence stretches are named prion-like domains(PrLDs).Prion-like proteins can aggregate into amyloid fibrils,which can accommodate incoming protein monomers,propagating thus the polymeric fold,both processes being。

关 键 词：DYSTROPHY MUSCULAR amyloid 

分 类 号：R746.2[医药卫生—神经病学与精神病学]