Helwig et al., 2013 - Google Patents
The neuroendocrine protein 7B2 suppresses the aggregation of neurodegenerative disease-related proteinsHelwig et al., 2013
View HTML- Document ID
- 17323490804127017174
- Author
- Helwig M
- Hoshino A
- Berridge C
- Lee S
- Lorenzen N
- Otzen D
- Eriksen J
- Lindberg I
- Publication year
- Publication venue
- Journal of Biological Chemistry
External Links
Snippet
Neurodegenerative diseases such as Alzheimer (AD) and Parkinson (PD) are characterized by abnormal aggregation of misfolded β-sheet-rich proteins, including amyloid-β (Aβ)- derived peptides and tau in AD and α-synuclein in PD. Correct folding and assembly of …
- 102100019156 SCG5 0 title abstract description 187
Classifications
-
- 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
-
- 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
- G01N33/5005—Chemical analysis of biological material, e.g. blood, urine; Testing involving biospecific ligand binding methods; Immunological testing involving human or animal cells
- G01N33/5008—Chemical analysis of biological material, e.g. blood, urine; Testing involving biospecific ligand binding methods; Immunological testing involving human or animal cells for testing or evaluating the effect of chemical or biological compounds, e.g. drugs, cosmetics
- G01N33/502—Chemical analysis of biological material, e.g. blood, urine; Testing involving biospecific ligand binding methods; Immunological testing involving human or animal cells for testing or evaluating the effect of chemical or biological compounds, e.g. drugs, cosmetics for testing non-proliferative effects
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL, OR TOILET PURPOSES
- A61K31/00—Medicinal preparations containing organic active ingredients
- A61K31/33—Heterocyclic compounds
- A61K31/395—Heterocyclic compounds having nitrogen as a ring hetero atom, e.g. guanethidine, rifamycins
-
- G—PHYSICS
- G01—MEASURING; TESTING
- G01N—INVESTIGATING OR ANALYSING MATERIALS BY DETERMINING THEIR CHEMICAL OR PHYSICAL PROPERTIES
- G01N2333/00—Assays involving biological materials from specific organisms or of a specific nature
- G01N2333/435—Assays involving biological materials from specific organisms or of a specific nature from animals; from humans
- G01N2333/46—Assays involving biological materials from specific organisms or of a specific nature from animals; from humans from vertebrates
- G01N2333/47—Assays involving proteins of known structure or function as defined in the subgroups
-
- G—PHYSICS
- G01—MEASURING; TESTING
- G01N—INVESTIGATING OR ANALYSING MATERIALS BY DETERMINING THEIR CHEMICAL OR PHYSICAL PROPERTIES
- G01N2800/00—Detection or diagnosis of diseases
- G01N2800/28—Neurological disorders
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL, OR TOILET PURPOSES
- A61K9/00—Medicinal preparations characterised by special physical form
Similar Documents
Publication | Publication Date | Title |
---|---|---|
Helwig et al. | The neuroendocrine protein 7B2 suppresses the aggregation of neurodegenerative disease-related proteins | |
Song et al. | A small molecule transcription factor EB activator ameliorates beta‐amyloid precursor protein and Tau pathology in Alzheimer's disease models | |
Farmer et al. | P53 aggregation, interactions with tau, and impaired DNA damage response in Alzheimer’s disease | |
Ma et al. | Blood-brain barrier-associated pericytes internalize and clear aggregated amyloid-β42 by LRP1-dependent apolipoprotein E isoform-specific mechanism | |
Shih et al. | TDP-43 interacts with amyloid-β, inhibits fibrillization, and worsens pathology in a model of Alzheimer’s disease | |
Barini et al. | Metformin promotes tau aggregation and exacerbates abnormal behavior in a mouse model of tauopathy | |
Lu et al. | Formaldehyde induces hyperphosphorylation and polymerization of Tau protein both in vitro and in vivo | |
Thompson et al. | IKK phosphorylates Huntingtin and targets it for degradation by the proteasome and lysosome | |
Neniskyte et al. | Neuronal death induced by nanomolar amyloid β is mediated by primary phagocytosis of neurons by microglia | |
Wales et al. | Limelight on alpha-synuclein: pathological and mechanistic implications in neurodegeneration | |
Surguchov | Intracellular dynamics of synucleins:“here, there and everywhere” | |
Cho et al. | SUMO1 promotes Aβ production via the modulation of autophagy | |
Baik et al. | P in1 promotes neuronal death in stroke by stabilizing N otch intracellular domain | |
Hoshino et al. | A novel function for pro SAAS as an amyloid anti‐aggregant in Alzheimer's disease | |
Florenzano et al. | Extracellular truncated tau causes early presynaptic dysfunction associated with Alzheimer’s disease and other tauopathies | |
Yun et al. | SUMO1 modulates Aβ generation via BACE1 accumulation | |
Abisambra et al. | DnaJA1 antagonizes constitutive Hsp70-mediated stabilization of tau | |
Chaplot et al. | Secreted chaperones in neurodegeneration | |
Ekimova et al. | Exogenous protein Hsp70/Hsc70 can penetrate into brain structures and attenuate the severity of chemically‐induced seizures | |
Jarvela et al. | The neural chaperone proSAAS blocks α-synuclein fibrillation and neurotoxicity | |
Deleersnijder et al. | Comparative analysis of different peptidyl-prolyl isomerases reveals FK506-binding protein 12 as the most potent enhancer of α-synuclein aggregation | |
Pastorino et al. | Alzheimer's disease-related loss of Pin1 function influences the intracellular localization and the processing of AβPP | |
De La‐Rocque et al. | Knockin’on heaven’s door: Molecular mechanisms of neuronal tau uptake | |
Fernandez et al. | Blockade of the interaction of calcineurin with FOXO in astrocytes protects against amyloid-β-induced neuronal death | |
Sen et al. | Loss in PKC epsilon causes downregulation of MnSOD and BDNF expression in neurons of Alzheimer’s disease hippocampus |