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Crystallin proteins and amyloid fibrils
by
Carver, John A
, Ecroyd, H
in
Alexander Disease
/ Alexander Disease - metabolism
/ alpha-Crystallin B Chain
/ alpha-Crystallin B Chain - chemistry
/ alpha-Crystallin B Chain - metabolism
/ alpha-Crystallin B Chain - physiology
/ Alzheimer disease
/ Alzheimer Disease - metabolism
/ Alzheimer's disease
/ Amyloid
/ Amyloid - metabolism
/ Amyloid - ultrastructure
/ Amyloid fibril
/ Biochemistry
/ Biomedical and Life Sciences
/ Biomedicine
/ cataract
/ Cataract - metabolism
/ Cataracts
/ Cell Biology
/ chemistry
/ Creutzfeldt-Jakob Syndrome
/ Creutzfeldt-Jakob Syndrome - metabolism
/ Crystallin
/ Fibrils
/ heat shock proteins
/ Heat-Shock Proteins, Small
/ Heat-Shock Proteins, Small - metabolism
/ Heat-Shock Proteins, Small - physiology
/ Humans
/ Lens
/ Lens, Crystalline
/ Lens, Crystalline - metabolism
/ Life Sciences
/ mechanism of action
/ metabolism
/ Molecular biology
/ molecular chaperone
/ Nanostructures
/ Parkinson disease
/ Parkinson's disease
/ physiology
/ protein aggregates
/ Protein Folding
/ Protein interaction
/ Protein Processing, Post-Translational
/ Protein Structure, Tertiary
/ Proteins
/ Review
/ small heat-shock protein
/ ultrastructure
2009
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Crystallin proteins and amyloid fibrils
by
Carver, John A
, Ecroyd, H
in
Alexander Disease
/ Alexander Disease - metabolism
/ alpha-Crystallin B Chain
/ alpha-Crystallin B Chain - chemistry
/ alpha-Crystallin B Chain - metabolism
/ alpha-Crystallin B Chain - physiology
/ Alzheimer disease
/ Alzheimer Disease - metabolism
/ Alzheimer's disease
/ Amyloid
/ Amyloid - metabolism
/ Amyloid - ultrastructure
/ Amyloid fibril
/ Biochemistry
/ Biomedical and Life Sciences
/ Biomedicine
/ cataract
/ Cataract - metabolism
/ Cataracts
/ Cell Biology
/ chemistry
/ Creutzfeldt-Jakob Syndrome
/ Creutzfeldt-Jakob Syndrome - metabolism
/ Crystallin
/ Fibrils
/ heat shock proteins
/ Heat-Shock Proteins, Small
/ Heat-Shock Proteins, Small - metabolism
/ Heat-Shock Proteins, Small - physiology
/ Humans
/ Lens
/ Lens, Crystalline
/ Lens, Crystalline - metabolism
/ Life Sciences
/ mechanism of action
/ metabolism
/ Molecular biology
/ molecular chaperone
/ Nanostructures
/ Parkinson disease
/ Parkinson's disease
/ physiology
/ protein aggregates
/ Protein Folding
/ Protein interaction
/ Protein Processing, Post-Translational
/ Protein Structure, Tertiary
/ Proteins
/ Review
/ small heat-shock protein
/ ultrastructure
2009
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Crystallin proteins and amyloid fibrils
by
Carver, John A
, Ecroyd, H
in
Alexander Disease
/ Alexander Disease - metabolism
/ alpha-Crystallin B Chain
/ alpha-Crystallin B Chain - chemistry
/ alpha-Crystallin B Chain - metabolism
/ alpha-Crystallin B Chain - physiology
/ Alzheimer disease
/ Alzheimer Disease - metabolism
/ Alzheimer's disease
/ Amyloid
/ Amyloid - metabolism
/ Amyloid - ultrastructure
/ Amyloid fibril
/ Biochemistry
/ Biomedical and Life Sciences
/ Biomedicine
/ cataract
/ Cataract - metabolism
/ Cataracts
/ Cell Biology
/ chemistry
/ Creutzfeldt-Jakob Syndrome
/ Creutzfeldt-Jakob Syndrome - metabolism
/ Crystallin
/ Fibrils
/ heat shock proteins
/ Heat-Shock Proteins, Small
/ Heat-Shock Proteins, Small - metabolism
/ Heat-Shock Proteins, Small - physiology
/ Humans
/ Lens
/ Lens, Crystalline
/ Lens, Crystalline - metabolism
/ Life Sciences
/ mechanism of action
/ metabolism
/ Molecular biology
/ molecular chaperone
/ Nanostructures
/ Parkinson disease
/ Parkinson's disease
/ physiology
/ protein aggregates
/ Protein Folding
/ Protein interaction
/ Protein Processing, Post-Translational
/ Protein Structure, Tertiary
/ Proteins
/ Review
/ small heat-shock protein
/ ultrastructure
2009
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Journal Article
Crystallin proteins and amyloid fibrils
2009
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Overview
Improper protein folding (misfolding) can lead to the formation of disordered (amorphous) or ordered (amyloid fibril) aggregates. The major lens protein, α-crystallin, is a member of the small heat-shock protein (sHsp) family of intracellular molecular chaperone proteins that prevent protein aggregation. Whilst the chaperone activity of sHsps against amorphously aggregating proteins has been well studied, its action against fibril-forming proteins has received less attention despite the presence of sHsps in deposits found in fibril-associated diseases (e.g. Alzheimer's and Parkinson's). In this review, the literature on the interaction of αB-crystallin and other sHsps with fibril-forming proteins is summarized. In particular, the ability of sHsps to prevent fibril formation, their mechanisms of action and the possible in vivo consequences of such associations are discussed. Finally, the fibril-forming propensity of the crystallin proteins and its implications for cataract formation are described along with the potential use of fibrillar crystallin proteins as bionanomaterials.
Publisher
Basel : Birkhäuser-Verlag,Birkhäuser-Verlag,Springer Nature B.V
Subject
/ Alexander Disease - metabolism
/ alpha-Crystallin B Chain - chemistry
/ alpha-Crystallin B Chain - metabolism
/ alpha-Crystallin B Chain - physiology
/ Alzheimer Disease - metabolism
/ Amyloid
/ Biomedical and Life Sciences
/ cataract
/ Creutzfeldt-Jakob Syndrome - metabolism
/ Fibrils
/ Heat-Shock Proteins, Small - metabolism
/ Heat-Shock Proteins, Small - physiology
/ Humans
/ Lens
/ Lens, Crystalline - metabolism
/ Protein Processing, Post-Translational
/ Proteins
/ Review
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