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International Journal of Molecular Sciences, ISSN 1661-6596, 05/2017, Volume 18, Issue 5, p. 901
Scaffolds for tissue engineering application may be made from a collagenous extracellular matrix (ECM) of connective tissues because the ECM can mimic the... 
Decellularised tissue | Fibril-fibril interactions | Mutable collagenous tissues | Fibril taper | Fracture | Collagen fibril | Elastic stress transfer | Fibril diameter | Plastic stress transfer | decellularised tissue | FIBRIL DIAMETER DISTRIBUTION | CATCH CONNECTIVE-TISSUE | collagen fibril | BIOCHEMISTRY & MOLECULAR BIOLOGY | fibril-fibril interactions | plastic stress transfer | MECHANICAL-PROPERTIES | CHEMISTRY, MULTIDISCIPLINARY | fracture | fibril diameter | FIBER SHAPE | IN-VITRO | INTERFIBRILLAR SHEAR-STRESS | mutable collagenous tissues | SPINE JOINT | fibril taper | elastic stress transfer | CRITICAL LENGTH | TENDON MORPHOGENESIS | FINITE-ELEMENT-ANALYSIS | Biocompatible Materials - metabolism | Collagen - metabolism | Shear Strength | Animals | Biocompatible Materials - chemistry | Sea Urchins - metabolism | Extracellular Matrix - metabolism | Elastic Modulus | Tissue Engineering | Surgical implants | Aquatic life | Separation | Fracture mechanics | Control systems | Risk | Biochemistry | Biology | Mechanical analysis | Fibers | Connective tissues | Biomedical materials | BSE | Encephalopathy | Extracellular matrix | Stiffness | Spongiform encephalopathy | Stresses | Architecture | Tissue engineering | Analogue | Fibrils | Macromolecules | Mechanical properties | Fiber composites | Transmissible spongiform encephalopathy | Mammals | Bovine spongiform encephalopathy | Collagen | Marine organisms | Skin | Livestock | Ligaments | Fracturing | Strength | Structure-function relationships
Journal Article
2006, Methods in enzymology, ISBN 9780121828189, Volume 413., xxxvi, 375
The ability of polypeptides to form alternatively folded, polymeric structures such as amyloids and related aggregates is being increasingly recognized as a... 
Amyloid | Prions | Amyloid beta-protein | Amyloid beta-Peptides
Book
Process Biochemistry, ISSN 1359-5113, 09/2016, Volume 51, Issue 9, pp. 1183 - 1192
Journal Article
1999, Methods in enzymology, ISBN 0121822109, Volume 309, xxxix, 820
This volume includes a core of methodologies to attack the unique experimental problems presented by protein misassembly. Emphasis is on human biology... 
Prions | Amyloid | Amyloid beta-protein | Proteins
Book
Journal of Biological Chemistry, ISSN 0021-9258, 01/2015, Volume 290, Issue 4, pp. 2395 - 2404
Journal Article
Journal of Dairy Science, ISSN 0022-0302, 10/2013, Volume 96, Issue 10, pp. 6127 - 6146
A typical casein micelle contains thousands of casein molecules, most of which form thermodynamically stable complexes with nanoclusters of amorphous calcium... 
molecular chaperone | unfolded protein | amyloid fibril | calcium phosphate sequestration | Calcium phosphate sequestration | Amyloid fibril | Molecular chaperone | Unfolded protein
Journal Article
FEBS Letters, ISSN 0014-5793, 04/2013, Volume 587, Issue 8, pp. 1128 - 1138
Alpha synuclein (αsyn) fibrils are found in the Lewy Bodies of patients with Parkinson’s disease (PD). The aggregation of the αsyn monomer to soluble oligomers... 
Aggregation | α-Synuclein | Fibril-resistance | Ensemble | Acetylation | Intrinsically disordered protein | Oligomer | Parkinson’s disease | Fibril | Nat | red blood cells | ThT | Parkinson's disease | NatB | PTM | circular dichroism | CN-PAGE | N-acetyltransferase | electrospray ionization–ion mobility spectrometry-mass spectrometry | SE-AUC | RBC | IDP | αsyn | sedimentation equilibrium-analytical ultracentrifugation | BOG | post-translational modifications | SLS | clear native PAGE | N-acetyltransferase B | α-synuclein | intrinsically disordered protein | size exclusion chromatography | GST | ESI-MS | Ac-αsyn | thioflavin T | non-amyloid component region | nuclear magnetic resonance | beta-octyl glucopyranoside | SEC | NAC | NMR | acetylated α-synuclein | glutathione S-transferase | enzyme-linked immunosorbent assay | static light scattering | electrospray ionization-mass spectrometry | ESI–IMS-MS | ELISA | Keywords α-Synuclein Acetylation Aggregation Ensemble Fibril Fibril-resistance Intrinsically disordered protein Oligomer Parkinson's disease | ALZHEIMERS-DISEASE | BIOCHEMISTRY & MOLECULAR BIOLOGY | METAL-CATALYZED OXIDATION | CELL BIOLOGY | BIOPHYSICS | METHIONINE OXIDATION | POINT MUTATIONS A30P | SECONDARY STRUCTURE | DISEASE-ASSOCIATED MUTANTS | AMYLOID FIBRIL FORMATION | alpha-Synuclein | LONG-RANGE ORDER | LEWY BODIES | PARKINSONS-DISEASE | Parkinson Disease - pathology | Protein Structure, Secondary | Humans | Protein Multimerization | Protein Conformation | Parkinson Disease - metabolism | Lewy Bodies - metabolism | alpha-Synuclein - metabolism | alpha-Synuclein - chemistry | Intrinsically Disordered Proteins | Monomer
Journal Article