Protein misfolded

Microvesicles (đôi khi được gọi là exosomes) là những mảnh của màng tế bào khác nhau, sinh ra từ hầu như tất cả các loại tế bào. Microvesicles đóng một vai trò trong việc truyền thông tin nội bào và có thể vận chuyển mRNA và protein giữa các tế bào.

16p kecodon360 30-08-2013 117 11   Download

Misfolded proteins, aggregates, and inclusion bodies are hall-marks of the cytopathology of neurodegenerative disorders including Huntington’s disease, Amyotropic lateral sclerosis, Parkinson’s disease, Prion diseases, and Alzheimer’s disease. The appearance of proteins with altered folded states is regula-ted by the protein folding quality control machinery and age-dependent. We have identified an unexpected molecular link between metabolic state, accumulation of damaged proteins, the heat-shock response and chaperones, and longevity....

61p fptmusic 11-04-2013 46 5   Download

Protein misfolding and deposition underlie an increasing number of debili-tating human disorders. Alzheimer’s disease is pathologically characterized by the presence of numerous insoluble amyloid plaques in the brain, com-posed primarily of the 42 amino acid humanb-amyloid peptide (Ab42). Disease-linked mutations in Ab42 occur in or near a central hydrophobic cluster comprising residues 17–21.

11p dell39 27-03-2013 37 5   Download

The study of protein aggregation saw a renaissance in the last decade, when it was discovered that aggregation is the cause of several human dis-eases, making this field of research one of the most exciting frontiers in science today. Building on knowledge about protein folding energy land-scapes, determined using an array of biophysical methods, theory and simulation, new light is now being shed on some of the key questions in protein-misfolding diseases.

9p dell39 27-03-2013 33 3   Download

A large number of neurodegenerative diseases in humans result from pro-tein misfolding and aggregation. Protein misfolding is believed to be the primary cause of Alzheimer’s disease, Parkinson’s disease, Huntington’s disease, Creutzfeldt–Jakob disease, cystic fibrosis, Gaucher’s disease and many other degenerative and neurodegenerative disorders.

19p inspiron33 26-03-2013 69 5   Download

Secretory and transmembrane proteins are synthesized in the endoplasmic reticulum (ER) in eukaryotic cells. Nascent polypeptide chains, which are translated on the rough ER, are translocated to the ER lumen and folded into their native conformation. When protein folding is inhibited because of mutations or unbalanced ratios of subunits of hetero-oligomeric pro-teins, unfolded or misfolded proteins accumulate in the ER in an event called ER stress.

20p galaxyss3 21-03-2013 28 5   Download

1The epidemic of bovine spongiform encephalopathy (BSE), or ‘mad cow disease’, and the subsequent emer-gence of a new variant of Creutzfeldt–Jakob disease (vCJD) in humans, has directed great political and sci-entific attention to a family of related neurodegenera-tive protein-misfolding diseases, collectively known as transmissible spongiform encephalopathies (TSEs) or prion diseases.

1p galaxyss3 21-03-2013 51 3   Download

After the successful cloning of the first gene for a polyglutamine disease in 1991, the expanded polyglutamine tract in the nine polyglutamine disease proteins became an obvious therapeutic target. Early hypotheses were that misfolded, precipitated protein could be a universal pathogenic mechanism. However, new data are accumulating on Huntington’s disease and other polyglutamine diseases that appear to contradict the toxic aggregate hypothesis.

11p galaxyss3 07-03-2013 55 5   Download

Surfactant protein C (SP-C) constitutes the transmembrane part of prosurf-actant protein C (proSP-C) and isa-helical in its native state. The C-termi-nal part of proSP-C (CTC) is localized in the endoplasmic reticulum lumen and binds to misfolded (b-strand) SP-C, thereby preventing its aggregation and amyloid fibril formation.

12p media19 05-03-2013 28 4   Download

Protein misfolding is recognized as an important pathophysiological cause of protein deficiency in many genetic disorders. Inherited mutations can disrupt native protein folding, thereby producing proteins with misfolded conformations.

10p media19 04-03-2013 24 2   Download

Rare, inherited mutations causing familial forms of Parkinson’s disease have provided insight into the molecular mechanisms that underlie the genetic and sporadic forms of this disease. Loss of protein function result-ing from autosomal-recessive mutations in PTEN-induced putative kinase 1 (PINK1), Parkin and DJ-1 has been linked to mitochondrial dysfunction, accumulation of abnormal and misfolded proteins, impaired protein clear-ance and oxidative stress.

9p vinaphone15 28-02-2013 39 3   Download

Transmissible spongiform encephalopathies (TSEs), or prion diseases, are fatal neurodegenerative disorders caused by an infectious agent termed a prion, which can convert normal cellular prion protein (PrP C ) into a patho-logically misfolded isoform (PrP Sc ). Taking advantage of protein misfolding cyclic amplification (PMCA), a series of experiments was conducted to investigate the possible influences of pyridine nucleotides on the propaga-

10p vinaphone15 27-02-2013 40 2   Download

Endoplasmic reticulum (ER)-associated degradation (ERAD) is a cell-autonomous process that eliminates large quantities of misfolded, newly synthesized protein, and is thus essential for the survival of any basic eukaryotic cell.

13p vinaphone15 27-02-2013 24 2   Download

Abnormal forms of prion protein (PrP Sc ) accumulate via structural conver-sion of normal PrP (PrP C ) in the progression of transmissible spongiform encephalopathy. Under cell-free conditions, the process can be efficiently replicated usingin vitro PrP Sc amplification methods, including protein mis-folding cyclic amplification.

8p viettel02 22-02-2013 21 2   Download

Arylsulfatase A is an oligomeric lysosomal enzyme. In the present study, we use this enzyme as a model protein to examine how heteromerization of wild-type and misfolded endoplasmic reticulum-degraded arylsulfatase A polypeptides affects the quality control of wild-type arylsulfatase A subun-its.

11p viettel02 19-02-2013 36 4   Download

It is assumed that protein fibrils manifested in amyloidosis result from an aggregation reaction involving small misfolded protein sequences being in an ‘oligomeric’ or ‘prefibrillar’ state. This review covers recent optical spectroscopic studies of amyloid protein misfolding, oligomerization and amyloid fibril growth.

9p mobifone23 18-01-2013 49 3   Download

The accumulation of misfolded proteins in the cytosol and nucleus of neuronal cells leads to neurodegenerative disorders. Polyglutamine diseases are caused by polyglutamine-expanded proteins, whereas mutations in superoxide dismutase 1 lead to amyotrophic lateral sclerosis.

11p mobifone23 18-01-2013 41 3   Download

Several protein misfolding diseases are associated with the conversion of native proteins into ordered protein aggregates known as amyloid. Studies of amyloid assemblies have indicated that non-native proteins are responsi-ble for initiating aggregationin vitro andin vivo.

16p cosis54 04-01-2013 36 3   Download

REVIEW ARTICLE Hanna Willander1,2, EriThe BRICHOS domain was initially defined from sequence alignments of the Bri protein associated with familial dementia, chondromodulin associ-ated with chondrosarcoma and surfactant protein C precursor (proSP-C) associated with respiratory distress syndrome and interstitial lung disease (ILD). Today BRICHOS has been found in 12 protein families.

12p cosis54 09-12-2012 46 3   Download