Proteoglycan-mediated inhibition of A beta proteolysis. A potential cause of senile plaque accumulation. - Wikidata - awgldk - TriplyDB

Proteoglycan-mediated inhibition of A beta proteolysis. A potential cause of senile plaque accumulation.

Proteoglycan-mediated inhibition of A beta proteolysis. A potential cause of senile plaque accumulation.

http://www.wikidata.org/entity/Q53201071

about

Perlecan maintains the integrity of cartilage and some basement membranes Heparan sulfate proteoglycan induces the production of NO and TNF-alpha by murine microglia.Current Research Therapeutic Strategies for Alzheimer's Disease Treatment Proteoglycans in the central nervous system: role in development, neural repair, and Alzheimer's disease Towards understanding the roles of heparan sulfate proteoglycans in Alzheimer's disease Amyloid β precursor protein as a molecular target for amyloid β--induced neuronal degeneration in Alzheimer's disease Inflammation and Alzheimer's disease Common binding sites for beta-amyloid fibrils and fibroblast growth factor-2 in heparan sulfate from human cerebral cortex Amyloid as a depot for the formulation of long-acting drugs Agrin in Alzheimer's disease: altered solubility and abnormal distribution within microvasculature and brain parenchyma Amyloid beta-protein assembly as a therapeutic target of Alzheimer's disease.Investigation of the noncovalent interactions between anti-amyloid agents and amyloid beta peptides by ESI-MS.Life without perlecan has its problems.Heparan sulfate accumulation with Abeta deposits in Alzheimer's disease and Tg2576 mice is contributed by glial cells.Neuronal heparan sulfates promote amyloid pathology by modulating brain amyloid-β clearance and aggregation in Alzheimer's disease.Heparin oligosaccharides as potential therapeutic agents in senile dementia Role of glycosaminoglycan sulfation in the formation of immunoglobulin light chain amyloid oligomers and fibrils.Heparin nanoparticles for β amyloid binding and mitigation of β amyloid associated cytotoxicity.Selective binding of soluble Abeta1-40 and Abeta1-42 to a subset of senile plaques.Expression and distribution of amyloid precursor protein-like protein-2 in Alzheimer's disease and in normal brain Amyloid accomplices and enforcers Hippocampal administration of chondroitinase ABC increases plaque-adjacent synaptic marker and diminishes amyloid burden in aged APPswe/PS1dE9 mice.Insulin-like growth factor I protects and rescues hippocampal neurons against beta-amyloid- and human amylin-induced toxicity.Signaling pathways regulating neuron-glia interaction and their implications in Alzheimer's disease.Heat shock proteins and amateur chaperones in amyloid-Beta accumulation and clearance in Alzheimer's disease.Neuroprotective properties of glycosaminoglycans: potential treatment for neurodegenerative disorders.Heparin accelerates gelsolin amyloidogenesis.The chemical neurobiology of carbohydrates Natural products from marine organisms with neuroprotective activity in the experimental models of Alzheimer's disease, Parkinson's disease and ischemic brain stroke: their molecular targets and action mechanisms.Protective Properties of Neural Extracellular Matrix.Cellular internalization of alpha-synuclein aggregates by cell surface heparan sulfate depends on aggregate conformation and cell type Abeta(1-40) prevents heparanase-catalyzed degradation of heparan sulfate glycosaminoglycans and proteoglycans in vitro. A role for heparan sulfate proteoglycan turnover in Alzheimer's disease.Localization of perlecan (or a perlecan-related macromolecule) to isolated microglia in vitro and to microglia/macrophages following infusion of beta-amyloid protein into rodent hippocampus.Overproduction of perlecan core protein in cultured cells and transgenic mice.Nervous system-derived chondroitin sulfate proteoglycans regulate growth cone morphology and inhibit neurite outgrowth: a light, epifluorescence, and electron microscopy study.Tramiprosate, a drug of potential interest for the treatment of Alzheimer's disease, promotes an abnormal aggregation of tau.New endoscopic approach of anti-fibrotic therapy for inflammatory bowel disease.HIV-1 TAT inhibits microglial phagocytosis of Abeta peptide.Molecular Origins of the Compatibility between Glycosaminoglycans and Aβ40 Amyloid Fibrils "Amyloid is not a tombstone"--a summation. The primary role for cerebrovascular and CSF dynamics as factors in Alzheimer's disease (AD): DMSO, fluorocarbon oxygen carriers, thyroid hormonal, and other suggested therapeutic measures.

P2860

Q24680954-C0DEDABC-FA61-480F-A006-29B494DBCA63 Q24813947-60EAA3FD-BD63-4424-8112-5DF4D8AE078A Q26765530-36EF977A-731B-4C4C-B98D-762DDD268DAC Q26865932-4094ED40-B563-44AE-8AD7-AA26641CE562 Q26992202-84F290B3-3657-4AD3-80BE-2A94A03AE83E Q27012950-72BBD9B0-714B-4975-B4A4-ECE7566C54B5 Q28138617-72566021-3A68-4702-9B11-4334430441B7 Q28374326-CC81D159-DDF2-4C7E-AD5B-D570935AD945 Q28472154-10D894AB-4E0F-4122-B19E-76F358099DE1 Q28645584-BD7FBB27-1EE0-4E69-8C4F-C22E8B5B5674 Q33392254-B82FAD85-D0D4-43E5-A6E4-88951F36D43A Q33617203-91CC798E-FC0E-4A20-BAA3-36943BF58491 Q33783384-C3AB81F8-1EC6-4C09-94A4-876FBB1736A2 Q33795144-D4B1CF5E-E5CB-4889-AF64-7FC262CFA93E Q33908201-6775604B-3934-484D-84DC-92278C4564AF Q33965772-2469E08E-DC2E-4AA4-81F7-592C8393F4A1 Q34333759-67765E90-0A3A-470D-90AB-072177CAFD91 Q35040469-64FE9DCC-B022-4D5C-8264-50D72184BD76 Q35774013-D5D8F060-2E44-496C-8D52-421729044502 Q35782137-562EEC31-6DC4-4662-8633-9176E029262A Q35970547-89FA59A2-6F30-4DD3-ACBE-16AFA074E6F8 Q36027554-CAD86F39-364C-457C-B12F-0A93225C6E0C Q36146984-CB2E1006-1C66-430F-862A-00AA5AA7DA75 Q36483870-951E9830-3380-4457-B1B1-163F3CD8386D Q36961152-3E6A7332-A0B9-4EA3-882C-6F3C0C53A0E5 Q37103046-DD55F554-AF79-4B8C-B388-3595C5A7CA83 Q37132636-1755AF51-48EA-4420-AA6F-B35DD0FE9E02 Q37152815-D8877685-6ACB-4C81-A2B8-855C22AF6039 Q38263124-B5D93EB2-64A6-4720-A00D-0E2DF0645E39 Q38268912-984E4C8D-2D7B-44D9-B95E-D6F7DA14F799 Q38694463-A9A831ED-E4C6-4594-B2EF-EE55C90451A2 Q39115074-90D94E42-BA3C-4234-9037-C2563909F019 Q39115335-363941DE-7ABC-4A16-BF88-7D305B67D0A4 Q39121464-C2C7C3CE-E758-4336-9EC4-FE5D1975C3B3 Q39121881-1B091C4F-9222-47C9-90F1-A3842EB13851 Q39250861-C314C69B-0706-479C-9DA8-DBFAF013238D Q39374847-63092096-B67E-4386-B1FB-D904370B9B7A Q40048514-8BE013F0-FE0B-4DF2-AF6E-3B7A4598D58C Q41301732-09E439F3-3DFF-4BBB-869D-BBEB72FD8CF9 Q41611139-AEA98472-DE07-4DAD-9800-A07FC043891A

P2860

Proteoglycan-mediated inhibition of A beta proteolysis. A potential cause of senile plaque accumulation.

http://www.wikidata.org/entity/Q53201071

description

1995 nî lūn-bûn

@nan

1995年の論文

@ja

1995年学术文章

@wuu

1995年学术文章

@zh

1995年学术文章

@zh-cn

1995年学术文章

@zh-hans

1995年学术文章

@zh-my

1995年学术文章

@zh-sg

1995年學術文章

@yue

1995年學術文章

@zh-hant

name

Proteoglycan-mediated inhibiti ...... of senile plaque accumulation.

@en

Proteoglycan-mediated inhibiti ...... of senile plaque accumulation.

@nl

type

label

Proteoglycan-mediated inhibiti ...... of senile plaque accumulation.

@en

Proteoglycan-mediated inhibiti ...... of senile plaque accumulation.

@nl

prefLabel

Proteoglycan-mediated inhibiti ...... of senile plaque accumulation.

@en

Proteoglycan-mediated inhibiti ...... of senile plaque accumulation.

@nl

P1433

Q53201071-B3BAC7B5-DEE3-4B2A-8BB3-17CA86D83EE2

P1476

Q53201071-FD179B0D-00E8-4240-9727-C76C31B0E13C

P2093

Q53201071-18018C44-1582-495A-A8B8-15AAF011C711

Q53201071-34F3D2A6-FC07-4096-8318-38AB521E6907

Q53201071-E5299AEB-5BF9-44F3-B67C-CF732225139C

P2860

Q53201071-0EB0C6A6-7C77-46BA-BC80-59EE3E865567

Q53201071-130F44FE-DD8F-4393-B755-77B04FCEE1F7

Q53201071-13FD34D4-CEED-4FDE-A489-5A521DB5FCCA

Q53201071-1DDB8B0E-409A-4488-9407-5AB1D3D11503

Q53201071-20C002DC-AD18-47D6-91A1-29228B70C9A1

Q53201071-2878FEAE-8148-4446-B455-65174800DA25

Q53201071-3D39A224-19F6-4708-B73C-19A8AE4BBE5E

Q53201071-40E2C9AB-B660-412C-99CD-5BD0DE66DDC1

Q53201071-50A2F15B-D266-4C6E-B96D-53A5FC7F86E9

Q53201071-52D368B2-A781-476B-9142-062B39C6B29D

P304

Q53201071-5B217CFF-D196-49E1-8EE6-2EFACA69B0E9

P31

Q53201071-86C11708-5055-4CCE-BAAC-54F2B5BA1151

P356

Q53201071-51F148AB-7349-47F9-BFC7-D8294FEE032C

P407

Q53201071-F83EBA33-0362-408B-BF90-2EC0100B8F41

P433

Q53201071-25694B99-E9A6-49FC-9527-84C837175FE8

P478

Q53201071-741DD02F-E323-4D7A-ADC5-DA45D1794C38

P577

Q53201071-EED10181-CAED-4F11-9297-E6602A9932E7

P698

Q53201071-D50FCD6D-3C73-42CB-AA68-36ACF3811FB9

P921

Q53201071-FFF3979A-FA3A-405B-B0B8-D37746BB5170

P356

JBC.270.31.18666

P1433

Journal of Biological Chemistry

P1476

Proteoglycan-mediated inhibiti ...... of senile plaque accumulation.

@en

P2093

Brunden KR

http://www.w3.org/2001/XMLSchema#string

Frederickson RC

http://www.w3.org/2001/XMLSchema#string

Gupta-Bansal R

http://www.w3.org/2001/XMLSchema#string

P2860

Cleavage of structural proteins during the assembly of the head of bacteriophage T4

Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa

A pathogenic mutation for probable Alzheimer's disease in the APP gene at the N-terminus of beta-amyloid

Early-onset Alzheimer's disease caused by mutations at codon 717 of the beta-amyloid precursor protein gene

Alzheimer's disease: initial report of the purification and characterization of a novel cerebrovascular amyloid protein

The precursor of Alzheimer's disease amyloid A4 protein resembles a cell-surface receptor

Enzymatically active lysosomal proteases are associated with amyloid deposits in Alzheimer brain

Mutation of the beta-amyloid precursor protein in familial Alzheimer's disease increases beta-protein production.

Chondroitin sulfate proteoglycans are associated with the lesions of Alzheimer's disease.

Molecular cloning and characterization of a cDNA encoding the cerebrovascular and the neuritic plaque amyloid peptides.

P304

18666-18671

http://www.w3.org/2001/XMLSchema#string

P31

scholarly article

P356

10.1074/JBC.270.31.18666

http://www.w3.org/2001/XMLSchema#string

P407

P433

31

http://www.w3.org/2001/XMLSchema#string

P478

270

http://www.w3.org/2001/XMLSchema#string

P577

1995-08-01T00:00:00Z

http://www.w3.org/2001/XMLSchema#dateTime

P698

7629198

http://www.w3.org/2001/XMLSchema#string

P921