Kourie, 2001 - Google Patents
Mechanisms of prion-induced modifications in membrane transport properties: implications for signal transduction and neurotoxicityKourie, 2001
- Document ID
- 4074154287182365327
- Author
- Kourie J
- Publication year
- Publication venue
- Chemico-Biological Interactions
External Links
Snippet
Prion-related encephalopathies are associated with the conversion of a normal cellular isoform of prion protein (PrPc) to an abnormal pathologic scrapie isoform (PrPSc). The conversion of this single polypeptide chain involves a reduction in the α-helices and an …
- 239000012528 membrane 0 title abstract description 64
Classifications
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL, OR TOILET PURPOSES
- A61K38/00—Medicinal preparations containing peptides
- A61K38/16—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- A61K38/17—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans
- A61K38/1703—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans from vertebrates
- A61K38/1709—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans from vertebrates from mammals
-
- G—PHYSICS
- G01—MEASURING; TESTING
- G01N—INVESTIGATING OR ANALYSING MATERIALS BY DETERMINING THEIR CHEMICAL OR PHYSICAL PROPERTIES
- G01N33/00—Investigating or analysing materials by specific methods not covered by the preceding groups
- G01N33/48—Investigating or analysing materials by specific methods not covered by the preceding groups biological material, e.g. blood, urine; Haemocytometers
- G01N33/50—Chemical analysis of biological material, e.g. blood, urine; Testing involving biospecific ligand binding methods; Immunological testing
- G01N33/68—Chemical analysis of biological material, e.g. blood, urine; Testing involving biospecific ligand binding methods; Immunological testing involving proteins, peptides or amino acids
- G01N33/6893—Chemical analysis of biological material, e.g. blood, urine; Testing involving biospecific ligand binding methods; Immunological testing involving proteins, peptides or amino acids related to diseases not provided for elsewhere
- G01N33/6896—Neurological disorders, e.g. Alzheimer's disease
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- C07K14/435—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans
- C07K14/46—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans from vertebrates
- C07K14/47—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans from vertebrates from mammals
- C07K14/4701—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans from vertebrates from mammals not used
- C07K14/4711—Alzheimer's disease; Amyloid plaque core protein
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL, OR TOILET PURPOSES
- A61K38/00—Medicinal preparations containing peptides
- A61K38/04—Peptides having up to 20 amino acids in a fully defined sequence; Derivatives thereof
- A61K38/07—Tetrapeptides
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL, OR TOILET PURPOSES
- A61K38/00—Medicinal preparations containing peptides
- A61K38/04—Peptides having up to 20 amino acids in a fully defined sequence; Derivatives thereof
- A61K38/06—Tripeptides
Similar Documents
Publication | Publication Date | Title |
---|---|---|
Kourie | Mechanisms of prion-induced modifications in membrane transport properties: implications for signal transduction and neurotoxicity | |
Fields et al. | Targeting alpha-synuclein as a therapy for Parkinson’s disease | |
Burré et al. | Cell biology and pathophysiology of α-synuclein | |
Vasili et al. | Spreading of α-synuclein and tau: A systematic comparison of the mechanisms involved | |
Tagliavini et al. | Tetracycline affects abnormal properties of synthetic PrP peptides and PrPSc in vitro | |
Fan et al. | Golgi apparatus and neurodegenerative diseases | |
Ferreiro et al. | The release of calcium from the endoplasmic reticulum induced by amyloid-beta and prion peptides activates the mitochondrial apoptotic pathway | |
Lee et al. | Internalization of mammalian fluorescent cellular prion protein and N‐terminal deletion mutants in living cells | |
Brown | Role of the prion protein in copper turnover in astrocytes | |
Behensky et al. | Afobazole activation of σ-1 receptors modulates neuronal responses to amyloid-β25–35 | |
Haigh et al. | Copper binding is the governing determinant of prion protein turnover | |
Thellung et al. | Intracellular mechanisms mediating the neuronal death and astrogliosis induced by the prion protein fragment 106–126 | |
Salmona et al. | A neurotoxic and gliotrophic fragment of the prion protein increases plasma membrane microviscosity | |
Aksenov et al. | Glutamine synthetase‐induced enhancement of β‐amyloid peptide Aβ (1–40) neurotoxicity accompanied by abrogation of fibril formation and Aβ fragmentation | |
DeMarco et al. | Local environmental effects on the structure of the prion protein | |
Ricchelli et al. | Aggregation/fibrillogenesis of recombinant human prion protein and Gerstmann− Sträussler− Scheinker disease peptides in the presence of metal ions | |
Longhena et al. | Targeting of disordered proteins by small molecules in neurodegenerative diseases | |
Ren et al. | Flotillin-1 Mediates PrP C Endocytosis in the Cultured Cells During Cu 2+ Stimulation Through Molecular Interaction | |
Rana et al. | Prion metal interaction: is prion pathogenesis a cause or a consequence of metal imbalance? | |
Mizuno et al. | Involvement of trace elements in the pathogenesis of prion diseases | |
Pass et al. | Prion infection in cells is abolished by a mutated manganese transporter but shows no relation to zinc | |
Osiecka et al. | Prion protein region 23–32 interacts with tubulin and inhibits microtubule assembly | |
Guo et al. | α‐Synuclein decoy peptide protects mice against α‐synuclein‐induced memory loss | |
Ruttenberg et al. | β-Hairpin Alignment Alters Oligomer Formation in Aβ-Derived Peptides | |
Vieira et al. | PrP meets alpha‐synuclein: Molecular mechanisms and implications for disease |