Implications of protein structure instability: From physiological to pathological secondary structure

Biopolymers

Volumn 97, Issue 8, 2012, Pages 577-588

  Sukhanova, Alyona ^a,b   Poly, Simon ^c   Shemetov, Anton ^b   Bronstein, Igor ^d   Nabiev, Igor ^a,b  

^a TRINITY COLLEGE DUBLIN   (Ireland)

^b NATIONAL RESEARCH NUCLEAR UNIVERSITY MEPHI   (Russian Federation)

^c CIC NANOGUNE   (Spain)

^d KING'S COLLEGE LONDON   (United Kingdom)

Author keywords

amyloid; amyloidosis; proteopathy; secondary structure

Indexed keywords

ALZHEIMER'S; AMYLOID; AMYLOID DISEASE; AMYLOID PROTEINS; AMYLOIDOSIS; CREUTZFELDT-JAKOB DISEASE; DIABETES MELLITUS; ENVIRONMENTAL CHANGE; ENVIRONMENTAL CONDITIONS; MISFOLDED PROTEINS; MOLECULAR CHAPERONES; PROTEIN STRUCTURES; PROTEOPATHY; SECONDARY STRUCTURES; SOLUBLE AGGREGATES; TYPE II; UNFOLDED PROTEINS; UNFOLDING PROCESS;

AGGREGATES; BIOSYNTHESIS; DEGRADATION; DISEASES; GLYCOPROTEINS; PHYSIOLOGY;

PROTEINS;

ALPHA SYNUCLEIN; AMYLOID PROTEIN; BETA SECRETASE; GAMMA SECRETASE;

ALZHEIMER DISEASE; AMYLOIDOSIS; BETA SHEET; CREUTZFELDT JAKOB DISEASE; DEGRADATION; ENVIRONMENTAL CHANGE; FIBER; GENETIC TRAIT; HOSPITAL SERVICE; HYDROPHOBICITY; IN VITRO STUDY; METABOLISM; NON INSULIN DEPENDENT DIABETES MELLITUS; PARKINSON DISEASE; PATHOLOGY; PHYSIOLOGY; PROTEIN FOLDING; PROTEIN STRUCTURE; REVIEW;

AMYLOIDOGENIC PROTEINS; AMYLOIDOSIS; CREUTZFELDT-JAKOB SYNDROME; DIABETES MELLITUS, TYPE 2; HUMANS; MOLECULAR CHAPERONES; PROTEIN FOLDING; PROTEIN STRUCTURE, SECONDARY; PROTEIN UNFOLDING; PROTEOLYSIS;

EID: 84861315842     PISSN: 00063525     EISSN: 10970282     Source Type: Journal    
DOI: 10.1002/bip.22055     Document Type: Review

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