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Protein misfolding
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Ebook "Protein folding and misfolding: Neurodegenerative diseases" is to review the molecular events initiated by unfolded or misfolded proteins leading to cell death via the development of pathological inclusions, with special emphasis on the macromolecular associations of the malfolded proteins into characteristic ultrastructures found in the cases of neurological disorders, some of them are shown in this issue.
284p
ladongphongthanh1008
22-04-2024
3
2
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Ebook "Folding for the synapse" addresses the current view on how protein folding and misfolding, controlled by molecular chaperones, contribute to synapse function and dysfunction. Molecular chaperones have been studied in relation to de novo protein folding, but there is increasing awareness that chaperone function is required for the regulation of protein dynamics when functioning physiologically as an isolated moiety or part of a protein complex.
315p
tracanhphuonghoa1007
22-04-2024
3
2
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Ebook "Protein misfolding, aggregation, and conformational diseases - Part A: Protein aggregation and conformational diseases" fills the gap in protein review and protocal literature while summarizing recent achievements in the understanding of the relationships between protein misfoldings, aggregation, and development of protein deposition disorders.
450p
cotieubac1004
15-03-2024
1
0
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Ebook "Protein misfolding, aggregation, and conformational diseases - Part B: Molecular mechanisms of conformational diseases" continues to fill the gap in protein review and protocal literature while summarizing recent achievements in the understanding of the relationships between protein misfoldings, aggregation, and development of protein deposition disorders. The focus of Part B is the molecular basis of differential disorders.
557p
cotieubac1004
15-03-2024
0
0
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Systemic amyloidosis is group of disorders characterized by the accumulation of insoluble proteins in tissues. The most common form of systemic amyloidosis is light chain amyloidosis, which results from the accumulation of misfolded immunoglobulins.
9p
vidoctorstrange
06-05-2023
2
2
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Mutations in myosin chaperones Unc45b and Hsp90aa1.1 as well as in the Unc45b-binding protein Smyd1b impair formation of myofibrils in skeletal muscle and lead to the accumulation of misfolded myosin.
20p
viaristotle
29-01-2022
7
0
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Protein disulfide isomerase (PDI) and PDI-like proteins contain thioredoxin domains that catalyze protein disulfide bond, inhibit aggregation of misfolded proteins, and function in isomerization during protein folding in endoplasmic reticulum and responses during abiotic stresses.Chinese cabbage is widely recognized as an economically important, nutritious vegetable, but its yield is severely hampered by various biotic and abiotic stresses. Because of, it is prime need to identify those genes whose are responsible for biotic and abiotic stress tolerance. PDI family genes are among of them.
20p
vilarryellison
29-10-2021
7
1
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Prion diseases are zoonotic diseases with a broad infection spectrum among mammalian hosts and are caused by the misfolded prion protein (PrPSc) derived from the normal prion protein (PrPC ), which encodes the prion protein gene (PRNP). Currently, although several prion disease-resistant animals have been reported, a high dose of prion agent inoculation triggers prion disease infection in these disease-resistant animals.
7p
viansan2711
30-07-2021
10
1
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Colorectal cancer is the third most common malignancy in humans and novel therapeutic approaches are urgently needed. Autophagy is an evolutionarily highly conserved cellular process by which cells collect unnecessary organelles or misfolded proteins and subsequently degrade them in vesicular structures in order to refuel cells with energy.
11p
vimoscow2711
29-08-2020
10
1
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The endoplasmic reticulum (ER) stress response is widely known to function in eukaryotes to maintain the homeostasis of the ER when unfolded or misfolded proteins are overloaded in the ER.
12p
viminato2711
22-05-2020
14
0
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Monoclonal antibodies (mAbs) as a class of therapeutic molecules are finding an increasing demand in the biotechnology industry for the treatment of diseases like cancer and multiple sclerosis. A key challenge associated to successful commercialization of mAbs is that from the various physical and chemical instabilities that are inherent to these molecules. Out of all probable instabilities, aggregation of mAbs has been a major problem that has been associated with a change in the protein structure and is a hurdle in various upstream and downstream processes.
14p
caothientrangnguyen
09-05-2020
9
1
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Ischemia/reperfusion (I/R) is one of the main causes of acute renal failure, leading to generation of reactive oxygen species (ROS) and ensuing oxidative stress, which results in unfolded misfolded protein accumulation and its dependent response pathways, generally known as unfolded protein response (UPR), in the endoplasmic reticulum (ER).
8p
sony2711
01-02-2019
16
1
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Mitochondrial dysfunction has been previously identified in neurodegenerative diseases such as Alzheimer disease, Huntington disease, and Parkinson disease.
21p
nutifooddau
27-01-2019
22
2
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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
114
10
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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
41
2
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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
33
2
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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
29
2
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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
65
3
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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
26
3
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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
48
2
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