Search Results - "amyloid"

Amyloidosis disease caused by amyloid /

Table of Contents: “…Contents: What is, and what is not amyloidosis -- Amyloid deposits -- Clinical amyloidosis -- Amyloid fibrillogenesis -- Tissue damage by amyloid -- Imaging amyloid in vivo -- Treatment of amyloidosis.…”
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Amyloidosis disease caused by amyloid /

Table of Contents: “…Contents: What is, and what is not amyloidosis -- Amyloid deposits -- Clinical amyloidosis -- Amyloid fibrillogenesis -- Tissue damage by amyloid -- Imaging amyloid in vivo -- Treatment of amyloidosis.…”
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Amyloidosis disease caused by amyloid /

Table of Contents: “…Contents: What is, and what is not amyloidosis -- Amyloid deposits -- Clinical amyloidosis -- Amyloid fibrillogenesis -- Tissue damage by amyloid -- Imaging amyloid in vivo -- Treatment of amyloidosis.…”
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The sequence determinants of amyloid fibril formation

Table of Contents: “…Contents: Amyloid fibril formation is a shared property of proteins -- The effect of mutations on the aggregation of unstructured polypeptide chains -- The importance of hydrophobicity, propensity to form beta-sheet structure and charge in amyloid formation of unstructured proteins -- The regions of the sequence forming the beta-core of amyloid fibrils -- The sequence and structural determinants of aggregation for partially folded states of proteins -- Amino acid sequences have evolved to avoid formation of amyloid-like aggregates.…”
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The sequence determinants of amyloid fibril formation

Table of Contents: “…Contents: Amyloid fibril formation is a shared property of proteins -- The effect of mutations on the aggregation of unstructured polypeptide chains -- The importance of hydrophobicity, propensity to form beta-sheet structure and charge in amyloid formation of unstructured proteins -- The regions of the sequence forming the beta-core of amyloid fibrils -- The sequence and structural determinants of aggregation for partially folded states of proteins -- Amino acid sequences have evolved to avoid formation of amyloid-like aggregates.…”
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The sequence determinants of amyloid fibril formation

Table of Contents: “…Contents: Amyloid fibril formation is a shared property of proteins -- The effect of mutations on the aggregation of unstructured polypeptide chains -- The importance of hydrophobicity, propensity to form beta-sheet structure and charge in amyloid formation of unstructured proteins -- The regions of the sequence forming the beta-core of amyloid fibrils -- The sequence and structural determinants of aggregation for partially folded states of proteins -- Amino acid sequences have evolved to avoid formation of amyloid-like aggregates.…”
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Adapting proteostasis to ameliorate aggregation-associated amyloid diseases

Table of Contents: “…Contents: Protein folding, misfolding, aggregation -- The proteostasis network and its regulation -- Gain and loss of function diseases -- The transthyretin (TTR) amyloidosis -- Kinetic stabilizers & clinical trial results -- Tafamidis & Diflunisal: evidence for the amyloid hypothesis -- Improving protein misfolding/aggregation diseases -- The unfolded protein response (UPR) and its arm-selective activators -- ATF6 activation & reduction of TTR mutant -- Clinical trials in amyloidosis with cardiac involvement.…”
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Adapting proteostasis to ameliorate aggregation-associated amyloid diseases

Table of Contents: “…Contents: Protein folding, misfolding, aggregation -- The proteostasis network and its regulation -- Gain and loss of function diseases -- The transthyretin (TTR) amyloidosis -- Kinetic stabilizers & clinical trial results -- Tafamidis & Diflunisal: evidence for the amyloid hypothesis -- Improving protein misfolding/aggregation diseases -- The unfolded protein response (UPR) and its arm-selective activators -- ATF6 activation & reduction of TTR mutant -- Clinical trials in amyloidosis with cardiac involvement.…”
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Adapting proteostasis to ameliorate aggregation-associated amyloid diseases

Table of Contents: “…Contents: Protein folding, misfolding, aggregation -- The proteostasis network and its regulation -- Gain and loss of function diseases -- The transthyretin (TTR) amyloidosis -- Kinetic stabilizers & clinical trial results -- Tafamidis & Diflunisal: evidence for the amyloid hypothesis -- Improving protein misfolding/aggregation diseases -- The unfolded protein response (UPR) and its arm-selective activators -- ATF6 activation & reduction of TTR mutant -- Clinical trials in amyloidosis with cardiac involvement.…”
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Protein folding and misfolding from theory to therapy /

Table of Contents: “…Contents: Protein nature, folding and complexity -- Folding in a cellular environment -- The underlying principles of folding -- Native and transition states -- Exploring the energy surface -- The folding of lysozyme -- The consequences of protein misfolding -- The relationship between folding and disease -- Protein deposition diseases -- Protein aggregates in amyloid diseases -- Amyloidogenic mutations of lysozyme -- Mechanism of amyloid formation -- Structure of the amyloidogenic intermediate -- Amyloid formation by lysozyme in vivo -- SH3 domain of PI3 kinase -- Model of an amyloid fibril -- The underlying origins of amyloid disease -- Generic toxicity of amyloid aggregates -- Cellular defences against aggregation -- Evolutionary design of proteins -- "Post-evolutionary" diseases.…”
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Protein folding and misfolding from theory to therapy /

Table of Contents: “…Contents: Protein nature, folding and complexity -- Folding in a cellular environment -- The underlying principles of folding -- Native and transition states -- Exploring the energy surface -- The folding of lysozyme -- The consequences of protein misfolding -- The relationship between folding and disease -- Protein deposition diseases -- Protein aggregates in amyloid diseases -- Amyloidogenic mutations of lysozyme -- Mechanism of amyloid formation -- Structure of the amyloidogenic intermediate -- Amyloid formation by lysozyme in vivo -- SH3 domain of PI3 kinase -- Model of an amyloid fibril -- The underlying origins of amyloid disease -- Generic toxicity of amyloid aggregates -- Cellular defences against aggregation -- Evolutionary design of proteins -- "Post-evolutionary" diseases.…”
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Protein folding and misfolding from theory to therapy /

Table of Contents: “…Contents: Protein nature, folding and complexity -- Folding in a cellular environment -- The underlying principles of folding -- Native and transition states -- Exploring the energy surface -- The folding of lysozyme -- The consequences of protein misfolding -- The relationship between folding and disease -- Protein deposition diseases -- Protein aggregates in amyloid diseases -- Amyloidogenic mutations of lysozyme -- Mechanism of amyloid formation -- Structure of the amyloidogenic intermediate -- Amyloid formation by lysozyme in vivo -- SH3 domain of PI3 kinase -- Model of an amyloid fibril -- The underlying origins of amyloid disease -- Generic toxicity of amyloid aggregates -- Cellular defences against aggregation -- Evolutionary design of proteins -- "Post-evolutionary" diseases.…”
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Molecules nucleation, aggregation and crystallization : beyond medical and other implications /

Table of Contents: “…Gordeliy and Ekaterina S. Moiseeva -- Amyloid, the amyloid [beta]-peptide, and Alzheimer's disease : structural considerations / Lars O. …”
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Novel proteins from designed combinatorial libraries

Table of Contents: “…Contents: Novel proteins can be devised using either rational/computational approaches or random/combinatorial methods -- Description of a hybrid approach that combines rational and combinatorial methods: libraries of novel proteins -- Combinatorial diversity -- Random vs. focused libraries -- Amphiphilic alpha-helices and beta-strands -- Binary patterning of polar and non-polar amino acids -- Genetic encoding of combinatorial mixtures of polar and non-polar amino acids -- Design of libraries of novel 4-helix bundles -- Library construction and expression in vivo -- Dynamic vs. wellordered protein structures -- Second generation libraries -- Biophysical characterization -- Solution structure of native-like 4-helix bundle proteins from designed libraries -- Functionally active proteins including cofactor binding proteins, peroxidases and esterases -- Designed libraries of beta sheet proteins: amyloid-like fibrils, monomeric beta-sheet proteins and novel biomaterials.…”
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Novel proteins from designed combinatorial libraries

Table of Contents: “…Contents: Novel proteins can be devised using either rational/computational approaches or random/combinatorial methods -- Description of a hybrid approach that combines rational and combinatorial methods: libraries of novel proteins -- Combinatorial diversity -- Random vs. focused libraries -- Amphiphilic alpha-helices and beta-strands -- Binary patterning of polar and non-polar amino acids -- Genetic encoding of combinatorial mixtures of polar and non-polar amino acids -- Design of libraries of novel 4-helix bundles -- Library construction and expression in vivo -- Dynamic vs. wellordered protein structures -- Second generation libraries -- Biophysical characterization -- Solution structure of native-like 4-helix bundle proteins from designed libraries -- Functionally active proteins including cofactor binding proteins, peroxidases and esterases -- Designed libraries of beta sheet proteins: amyloid-like fibrils, monomeric beta-sheet proteins and novel biomaterials.…”
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Novel proteins from designed combinatorial libraries

Table of Contents: “…Contents: Novel proteins can be devised using either rational/computational approaches or random/combinatorial methods -- Description of a hybrid approach that combines rational and combinatorial methods: libraries of novel proteins -- Combinatorial diversity -- Random vs. focused libraries -- Amphiphilic alpha-helices and beta-strands -- Binary patterning of polar and non-polar amino acids -- Genetic encoding of combinatorial mixtures of polar and non-polar amino acids -- Design of libraries of novel 4-helix bundles -- Library construction and expression in vivo -- Dynamic vs. wellordered protein structures -- Second generation libraries -- Biophysical characterization -- Solution structure of native-like 4-helix bundle proteins from designed libraries -- Functionally active proteins including cofactor binding proteins, peroxidases and esterases -- Designed libraries of beta sheet proteins: amyloid-like fibrils, monomeric beta-sheet proteins and novel biomaterials.…”
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