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This Brief summarizes the current research on the novel BRICHOS domain, which is a chaperone domain found in a variety of proteins and is shown to exhibit anti-amyloidogenic chaperone-like functions. The BRICHOS domain is defined from sequence similarities, lacks established physiological function(s) and is found about 10 distantly related pro-protein families, several of which are associated with human disease. In this work, the authors review the mechanism by which BRICHOS inhibits Aβ aggregation and examine recent results from in vivo experiments where BRICHOS inhibits Aβ aggregation and toxicity in Drosophila melanogaster. BRICHOS is one of nature´s (more specific) ways to protect against fibril formation, and exploring the potential of using the BRICHOS domain in the fight against Alzeimer's Disease and other amyloid diseases seems highly relevant. This brief is useful for newcomers to this field or researchers in related fields wishing to gain a quick overview of the latest findings.

Chemistry. --- Bioorganic Chemistry. --- Protein Structure. --- Bioorganic chemistry. --- Biochemistry. --- Chimie --- Chimie bioorganique --- Biochimie --- Chemistry --- Physical Sciences & Mathematics --- Organic Chemistry --- Protein folding. --- Proteins. --- Proteids --- Folding of proteins --- Proteins --- Folding --- Biomolecules --- Polypeptides --- Proteomics --- Conformation --- Bio-organic chemistry --- Biological organic chemistry --- Biochemistry --- Chemistry, Organic --- Biological chemistry --- Chemical composition of organisms --- Organisms --- Physiological chemistry --- Biology --- Medical sciences --- Composition --- Proteins .

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This book addresses molecular mechanisms of protein misfolding and the role of lipids and related molecules in these complex processes. The focus is on the biophysical and structural studies of proteins that are involved in major human disorders such as Alzheimer’s disease, systemic amyloidoses, diabetes II, inflammation and atherosclerosis. Misfolding often results from protein mutations or modifications. Misfolding of membrane proteins can cause topological changes that target the proteins for degradation. Misfolding of soluble globular proteins and peptides converts them into β-sheet-rich aggregates and amyloid fibrils. This process can disrupt the structural integrity of the lipid membranes and thereby contribute to amyloid toxicity. In turn, lipids and lipid-associated molecules such as apolipoproteins and heparan sulfate proteoglycans, which are ubiquitous constituents of amyloid plaques, can influence protein misfolding via diverse mechanisms that are addressed in this book. The book features chapters describing the role of lipids in the misfolding of a wide range of proteins, including small peptides, globular proteins, lipid surface-binding proteins, and integral membrane proteins. The role of individual lipid molecules, lipid surfaces, and the membrane field is addressed, including specific and non-specific interactions with protein oligomers and mature fibrils. Distinct effects of various lipids on the nucleation and growth of amyloid fibrils are discussed. Modern computational approaches to the analysis of amyloid formation are addressed.  The book should be useful to experts in the field but is also accessible to novices.

Life Sciences. --- Protein Structure. --- Biomedicine general. --- Bioorganic Chemistry. --- Life sciences. --- Medicine. --- Bioorganic chemistry. --- Biochemistry. --- Sciences de la vie --- Médecine --- Chimie bioorganique --- Biochimie --- Lipids. --- Protein folding. --- Chemistry --- Physical Sciences & Mathematics --- Biochemistry --- Folding of proteins --- Proteins --- Lipides --- Lipins --- Lipoids --- Folding --- Proteins. --- Proteids --- Biomolecules --- Polypeptides --- Proteomics --- Bio-organic chemistry --- Biological organic chemistry --- Chemistry, Organic --- Biosciences --- Sciences, Life --- Science --- Steroids --- Conformation --- Clinical sciences --- Medical profession --- Human biology --- Life sciences --- Medical sciences --- Pathology --- Physicians --- Biological chemistry --- Chemical composition of organisms --- Organisms --- Physiological chemistry --- Biology --- Composition --- Health Workforce --- Proteins . --- Biomedicine, general.