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A Single Mutation at the Sheet Switch Region Results in Conformational Changes Favoring lambda 6 Light-Chain Fibrillogenesis
(ACADEMIC PRESS LTD- ELSEVIER SCIENCE LTD, 2010)
Systemic amyloid light-chain (LC) amyloidosis is a disease process characterized by the pathological deposition of monoclonal LCs in tissue. All LC subtypes are capable of fibril formation although lambda chains, particularly ...
Ultrastructural aspects of connective tissue in hereditary gingival fibromatosis
(Mosby, IncSt LouisEUA, 2001)
Aβ-Amyloid fibrils are self-triggered by the interfacial lipid environment and low peptide content
(American Chemical Society, 2020-07-21)
We studied the surface properties of Aβ(1-40) amyloid peptides mixed with 1-palmitoyl-2-oleoyl-phosphatidylcholine (POPC) (liquid state) or 1,2-disteraoyl-phosphatidylcholine (DSPC) (solid state) phospholipids by using ...
Establishment of Constraints on Amyloid Formation Imposed by Steric Exclusion of Globular Domains
(Academic Press Ltd - Elsevier Science Ltd, 2018-10)
In many disease-related and functional amyloids, the amyloid-forming regions of proteins are flanked by globular domains. When located in close vicinity of the amyloid regions along the chain, the globular domains can ...
The effect of age and spontaneous exercise on the biomechanical and biochemical properties of chicken superficial digital flexor tendon
(Taylor & Francis LtdAbingdonInglaterra, 2010)
Changes of Large Molecular Weight Hyaluronan and Versican in the Mouse Pubic Symphysis Through Pregnancy
(Soc Study ReproductionMadison, 2012)
Biochemical and biomechanical analysis of tendons of caged and penned chickens
(Taylor & Francis LtdAbingdonInglaterra, 2004)
Fine structure study of A beta(1-42) fibrillogenesis with atomic force microscopy
(FEDERATION AMER SOC EXP BIOL., 2005-05)
One of the hallmarks of Alzheimer's disease is the self-aggregation of the amyloid beta peptide (A beta) in extracellular amyloid fibrils. Among the different forms of A beta, the 42-residue fragment (A beta(1-42)) readily ...