reviews - of /home/sholmes/web
... The protein-only hypothesis proposes that prions consist of an isoform of PrPC (generically designated PrP* and commonly assumed to be PrPSc) and that their replication comes about by a self-propagating conversion of PrPC to the pathogenic isoform (FIG. 2). According to the refolding model, PrPC unf ...
... The protein-only hypothesis proposes that prions consist of an isoform of PrPC (generically designated PrP* and commonly assumed to be PrPSc) and that their replication comes about by a self-propagating conversion of PrPC to the pathogenic isoform (FIG. 2). According to the refolding model, PrPC unf ...
Prions: Infectious Proteins with Genetic Properties
... Prion-like properties of the proteins Sup35p, Ure2p, and Het-s. In 1994 it was shown that the genetic properties of the [PSI+] and [URE3] determinants may be explained in the framework of the prion concept [26]. The role of the corresponding prions could be played by the proteins encoded by the SUP3 ...
... Prion-like properties of the proteins Sup35p, Ure2p, and Het-s. In 1994 it was shown that the genetic properties of the [PSI+] and [URE3] determinants may be explained in the framework of the prion concept [26]. The role of the corresponding prions could be played by the proteins encoded by the SUP3 ...
The Structure of Human Prions: From Biology to Structural Models
... Mutations in the PRNP gene can cause the development of prion diseases and lead to different clinical phenotypes, including CJD, GSS and FFI [28–30]. Mutations of the prion protein gene can be classified as: (1) point mutations (i.e., single nucleotide substitutions), which can cause an amino change ...
... Mutations in the PRNP gene can cause the development of prion diseases and lead to different clinical phenotypes, including CJD, GSS and FFI [28–30]. Mutations of the prion protein gene can be classified as: (1) point mutations (i.e., single nucleotide substitutions), which can cause an amino change ...
Does intracrine amplification provide a unifying principle for the
... various misfolded proteins should be sought; their interruption would be therapeutically beneficial in disease modification. These networks, usually weak and indolent, can, as is likely in some cases of CTE and AD, be more robust. They are likely mediated by misfolded proteindriven regulation of tra ...
... various misfolded proteins should be sought; their interruption would be therapeutically beneficial in disease modification. These networks, usually weak and indolent, can, as is likely in some cases of CTE and AD, be more robust. They are likely mediated by misfolded proteindriven regulation of tra ...
Scientists try to untangle the mystery behind a
... The recent research into Looney’s condition and others like it began in the 1980s with Stanley Prusiner, a neurologist at UC San Francisco. He was studying neurodegenerative diseases—ailments that attack the nervous system. He focused on scrapie, a disease that causes sheep to stagger around pasture ...
... The recent research into Looney’s condition and others like it began in the 1980s with Stanley Prusiner, a neurologist at UC San Francisco. He was studying neurodegenerative diseases—ailments that attack the nervous system. He focused on scrapie, a disease that causes sheep to stagger around pasture ...
Gene therapy - mvhs
... says. "Our work with mice will show whether these undetectable levels of prion are indeed non-infectious." Jason Shih will also test keratinase's effectiveness in decontaminating equipment that processes animal byproducts. Many scientists believe that mad cow disease is spread by healthy animals eat ...
... says. "Our work with mice will show whether these undetectable levels of prion are indeed non-infectious." Jason Shih will also test keratinase's effectiveness in decontaminating equipment that processes animal byproducts. Many scientists believe that mad cow disease is spread by healthy animals eat ...
Internal Medicine - Infectious Diseases
... The Infectious Diseases rotation is designed to provide the trainee an educational experience in the common infectious problems experienced by patients. An evidence-based approach to infectious disease problems is stressed through one on one teaching by the infectious diseases faculty, through small ...
... The Infectious Diseases rotation is designed to provide the trainee an educational experience in the common infectious problems experienced by patients. An evidence-based approach to infectious disease problems is stressed through one on one teaching by the infectious diseases faculty, through small ...
Cross-Roads in Research on Neurodegenerative Diseases
... by accumulation of amyloid-β and tau. Recent studies have indicated that AD may be a brain infection. Although AD has not been shown to be transmissible, the burning issue is whether the potential infectious causes are the misfolded amyloid proteins themselves, or an unidentified microorganism. The ...
... by accumulation of amyloid-β and tau. Recent studies have indicated that AD may be a brain infection. Although AD has not been shown to be transmissible, the burning issue is whether the potential infectious causes are the misfolded amyloid proteins themselves, or an unidentified microorganism. The ...
How do neurons degenerate in prion diseases or transmissible
... die via programmed cell death of which the apoptotic process is relatively well characterized. A subcellular alteration linked to apoptosis is the formation of autophagic vacuoles, which we and others demonstrated in CJD- and scrapie-affected rodent brains. Autophagy may co-exist with apoptosis or m ...
... die via programmed cell death of which the apoptotic process is relatively well characterized. A subcellular alteration linked to apoptosis is the formation of autophagic vacuoles, which we and others demonstrated in CJD- and scrapie-affected rodent brains. Autophagy may co-exist with apoptosis or m ...
Research Roundup - The Journal of Cell Biology
... potent form, Sc4, had the slowest growth. However, this slow growth was accompanied by increased amyloid fragility—the fibers fell apart more often. The potency of the Sc4 form was thus explained not by aggregate size or growth rate but instead by its propensity to break into new infectious prion pa ...
... potent form, Sc4, had the slowest growth. However, this slow growth was accompanied by increased amyloid fragility—the fibers fell apart more often. The potency of the Sc4 form was thus explained not by aggregate size or growth rate but instead by its propensity to break into new infectious prion pa ...
A brief history of prions - Oxford Academic
... just a few years earlier. Their attempts to experimentally inactivate the scrapie agent inspired their iconoclastic ideas. In 1966, Tikvah Alper attempted to use ionizing radiation to inactivate and determine the genomic size of the scrapie agent. She discovered thst the agent was not easily inactiv ...
... just a few years earlier. Their attempts to experimentally inactivate the scrapie agent inspired their iconoclastic ideas. In 1966, Tikvah Alper attempted to use ionizing radiation to inactivate and determine the genomic size of the scrapie agent. She discovered thst the agent was not easily inactiv ...
π- Stacking Interaction
... • The agent is a misfolded form (PrS) of a normal cell protein (PrP) that acts by a conversion of normal folded PrP proteins to amyloid-like aggregates. • The importance of the octapeptide repeats is the fact result from the insertion of one to nine extra octapeptide repeats in addition to the five ...
... • The agent is a misfolded form (PrS) of a normal cell protein (PrP) that acts by a conversion of normal folded PrP proteins to amyloid-like aggregates. • The importance of the octapeptide repeats is the fact result from the insertion of one to nine extra octapeptide repeats in addition to the five ...
PDF - Journal of Applied Pharmaceutical Science
... All known prion diseases affect the structure of the brain or other neural tissue and all are currently untreatable (no natural defense) and universally fatal. PrPC refers to the endogenous form of prion protein (PrP), which is found in a multitude of tissues, while PrPSc refers to the misfolded for ...
... All known prion diseases affect the structure of the brain or other neural tissue and all are currently untreatable (no natural defense) and universally fatal. PrPC refers to the endogenous form of prion protein (PrP), which is found in a multitude of tissues, while PrPSc refers to the misfolded for ...
Crystal Structures of the Odd and Even Electron One - SPring-8
... lengthened by the steric hindrance. Therefore, it is considered that the periodicity of the helical arrangement of the ligands is strongly correlated with the number of ClO4– ions. Since the molar ratio of Pt2(EtCS2)4 to ClO4– has been confirmed to be 5:2 by elemental analyses, the average oxidation ...
... lengthened by the steric hindrance. Therefore, it is considered that the periodicity of the helical arrangement of the ligands is strongly correlated with the number of ClO4– ions. Since the molar ratio of Pt2(EtCS2)4 to ClO4– has been confirmed to be 5:2 by elemental analyses, the average oxidation ...
Lecture 13-Effects of glycosylation on protein structure and function
... Differential glycosylation of prion proteins may be linked to the conformational changes leading to CJD and related diseases! Glycobiology of disease ...
... Differential glycosylation of prion proteins may be linked to the conformational changes leading to CJD and related diseases! Glycobiology of disease ...
18.1 Studying Viruses and Prokaryotes
... – non-living pathogen – can infect many organisms – 50 – 200 nm • Viroid: Infectious particle that is made only of single-stranded RNA. – causes disease in plants – passed through seeds or pollen ...
... – non-living pathogen – can infect many organisms – 50 – 200 nm • Viroid: Infectious particle that is made only of single-stranded RNA. – causes disease in plants – passed through seeds or pollen ...
A General Model of Prion Strains and Their Pathogenicity
... population exposure, suggest the need for caution (8). Prion infection is associated with prolonged, clinically silent incubation periods, which in humans can exceed 50 years (9), and secondary transmission of vCJD by blood transfusion appears to be efficient (10). Prions have also assumed much wide ...
... population exposure, suggest the need for caution (8). Prion infection is associated with prolonged, clinically silent incubation periods, which in humans can exceed 50 years (9), and secondary transmission of vCJD by blood transfusion appears to be efficient (10). Prions have also assumed much wide ...
About chronic wasting disease
... abnormality in the protein throughout the brain, causing increasing damage and, ultimately, death. Other prion diseases include mad cow disease in cattle, Creutzfeldt-Jakob (pronounced CROYTZ-felt YAH-cawb) disease in humans, and scrapie (pronounced SCRAY-pee) in sheep and goats. The abnormally fold ...
... abnormality in the protein throughout the brain, causing increasing damage and, ultimately, death. Other prion diseases include mad cow disease in cattle, Creutzfeldt-Jakob (pronounced CROYTZ-felt YAH-cawb) disease in humans, and scrapie (pronounced SCRAY-pee) in sheep and goats. The abnormally fold ...
Classical Creutzfeldt–Jakob Disease (CJD) Human Prion Diseases (Other Than vCJD)
... Current evidence supports the theory that the infectious agent is a prion. However, the existence of accessory factors has not been excluded. Prions are considered members of the transmissible spongiform encephalopathy (TSE) group of agents that include kuru, Creutzfeldt–Jakob Disease (CJD) and vari ...
... Current evidence supports the theory that the infectious agent is a prion. However, the existence of accessory factors has not been excluded. Prions are considered members of the transmissible spongiform encephalopathy (TSE) group of agents that include kuru, Creutzfeldt–Jakob Disease (CJD) and vari ...
ORGANIC CHEMISTRY SEMINAR Professor Jeff Kelly Biological and Chemical Approaches to Adapt
... proteome function by controlling ribosomal protein synthesis, chaperone and enzyme mediated protein folding, protein trafficking, proteindegradation and the like. Stress responsive signaling pathways match proteostasis network capacity with demand in each subcellular compartment to maintain cellular ...
... proteome function by controlling ribosomal protein synthesis, chaperone and enzyme mediated protein folding, protein trafficking, proteindegradation and the like. Stress responsive signaling pathways match proteostasis network capacity with demand in each subcellular compartment to maintain cellular ...
Protein folding is essential to life
... Why do proteins fold? Like all proteins, villin is formed by a unique sequences of aminoacids. However, only knowing the sequence tells us little about what the protein villin does and how it does it. In order to carry out their function (for instance as enzymes or antibodies), proteins must take o ...
... Why do proteins fold? Like all proteins, villin is formed by a unique sequences of aminoacids. However, only knowing the sequence tells us little about what the protein villin does and how it does it. In order to carry out their function (for instance as enzymes or antibodies), proteins must take o ...
Molecular Machines (1MB429) Exam 2011-12-21
... the similarity and dissimilarity of prion diseases with other neurodegenerative diseases of mammals. (4p) Answer: Prions are infectious protein particles that can cause neurodegenerative diseases in higher eukaryotes. Usually prion proteins form amyloid fiber in the brain of the infected animals, wh ...
... the similarity and dissimilarity of prion diseases with other neurodegenerative diseases of mammals. (4p) Answer: Prions are infectious protein particles that can cause neurodegenerative diseases in higher eukaryotes. Usually prion proteins form amyloid fiber in the brain of the infected animals, wh ...
BOOK REVIEWS Prions Prions Prions Practical Food Microbiology
... inherited and sporadic forms of the transmissible encephalopathies, as seen from the perspective of the prion hypothesis. In view of the topicality of bovine spongieform encephalopathy (BSE), this book will appeal potentially to a wide audience. Microbiologists may be disappointed that the volume is ...
... inherited and sporadic forms of the transmissible encephalopathies, as seen from the perspective of the prion hypothesis. In view of the topicality of bovine spongieform encephalopathy (BSE), this book will appeal potentially to a wide audience. Microbiologists may be disappointed that the volume is ...
“Mad Cow” Disease: Bovine Spongiform Encephalopathy
... into the brain stem via the vagus nerve (American Scientist, Jul/Aug 2004). The abnormal proteins then transform the normal proteins in the brain into the pathogenic form and this process continues to the next protein, and so on, until there is a large build-up of the pathogen in the cells of these ...
... into the brain stem via the vagus nerve (American Scientist, Jul/Aug 2004). The abnormal proteins then transform the normal proteins in the brain into the pathogenic form and this process continues to the next protein, and so on, until there is a large build-up of the pathogen in the cells of these ...
Prion
A prion (/ˈpriːɒn/) is a protein that can fold in multiple, structurally distinct ways, at least one of which is transmissible to other prion proteins. It is this form of replication that leads to disease that is similar to viral infection. The word prion, coined in 1982 by Stanley B. Prusiner, is short for “proteinaceous infectious particle” derived from the words protein and infection, in reference to a prion's ability to self-propagate and transmit its conformation to other prions. While several yeast proteins have been identified as having prionogenic properties, the first prion protein was discovered in mammals and is referred to as the major prion protein (PrP). This infectious agent causes mammalian transmissible spongiform encephalopathies, including bovine spongiform encephalopathy (BSE, also known as ""mad cow disease"") and scrapie in sheep. In humans, PrP causes Creutzfeldt-Jakob Disease (CJD), variant Creutzfeldt-Jakob Disease (vCJD), Gerstmann–Sträussler–Scheinker syndrome, Fatal Familial Insomnia and kuru.A protein as an infectious agent stands in contrast to all other known infectious agents, like viruses, bacteria, fungi, or parasites—all of which must contain nucleic acids (either DNA, RNA, or both). All known prion diseases in mammals affect the structure of the brain or other neural tissue and all are currently untreatable and universally fatal.Prions are not considered living organisms because they are misfolded protein molecules which may propagate by transmitting a misfolded protein state. If a prion enters a healthy organism, it induces existing, properly folded proteins to convert into the misfolded prion form. In this way, the prion acts as a template to guide the misfolding of more proteins into prion form. In yeast, this refolding is assisted by chaperone proteins such as Hsp104p. These refolded prions can then go on to convert more proteins themselves, leading to a chain reaction resulting in large amounts of the prion form. All known prions induce the formation of an amyloid fold, in which the protein polymerises into an aggregate consisting of tightly packed beta sheets. Amyloid aggregates are fibrils, growing at their ends, and replicate when breakage causes two growing ends to become four growing ends. The incubation period of prion diseases is determined by the exponential growth rate associated with prion replication, which is a balance between the linear growth and the breakage of aggregates. (Note that the propagation of the prion depends on the presence of normally folded protein in which the prion can induce misfolding; animals that do not express the normal form of the prion protein can neither develop nor transmit the disease.)Prion aggregates are extremely stable and accumulate in infected tissue, causing tissue damage and cell death. This structural stability means that prions are resistant to denaturation by chemical and physical agents, making disposal and containment of these particles difficult. Prion structure varies slightly between species, but nonetheless prion replication is subject to occasional epimutation and natural selection just like other forms of replication.