Endoplasmic reticulum chaperones inhibit the production of amyloid-beta peptides. - Wikidata - awgldk - TriplyDB

Endoplasmic reticulum chaperones inhibit the production of amyloid-beta peptides.

Endoplasmic reticulum chaperones inhibit the production of amyloid-beta peptides.

http://www.wikidata.org/entity/Q40203503

about

Generation of amyloid-β is reduced by the interaction of calreticulin with amyloid precursor protein, presenilin and nicastrin ER chaperones in mammalian development and human diseases The collagen chaperone HSP47 is a new interactor of APP that affects the levels of extracellular beta-amyloid peptides Heat shock proteins: cellular and molecular mechanisms in the central nervous system.Activation of PERK signaling attenuates Abeta-mediated ER stress.ER stress in Alzheimer's disease: a novel neuronal trigger for inflammation and Alzheimer's pathology.Cellular stress responses: cell survival and cell death Lactic acid induces aberrant amyloid precursor protein processing by promoting its interaction with endoplasmic reticulum chaperone proteins.Parkin reverses intracellular beta-amyloid accumulation and its negative effects on proteasome function.Restoration of visual function in P23H rhodopsin transgenic rats by gene delivery of BiP/Grp78 Histone deacetylase inhibitor valproic acid inhibits cancer cell proliferation via down-regulation of the alzheimer amyloid precursor protein Suppression of melanin production by expression of HSP70 Comparative transcriptome profiling of amyloid precursor protein family members in the adult cortex Unfolded protein response-induced ERdj3 secretion links ER stress to extracellular proteostasis.Proteasomal dysfunction and endoplasmic reticulum stress enhance trafficking of prion protein aggregates through the secretory pathway and increase accumulation of pathologic prion protein Amyloid precursor protein revisited: neuron-specific expression and highly stable nature of soluble derivatives.Unfolded Protein Response and PERK Kinase as a New Therapeutic Target in the Pathogenesis of Alzheimer's Disease Preconditioning with endoplasmic reticulum stress ameliorates mesangioproliferative glomerulonephritis.Androgen receptor inclusions acquire GRP78/BiP to ameliorate androgen-induced protein misfolding stress in embryonic stem cells Do amyloid oligomers act as traps for misfolded proteins? A hypothesis p21(Cip1) protects against oxidative stress by suppressing ER-dependent activation of mitochondrial death pathways.Prostaglandin E2 stimulates the production of amyloid-beta peptides through internalization of the EP4 receptor.Chaperone signalling complexes in Alzheimer's disease.Decreased Levels of Foldase and Chaperone Proteins Are Associated with an Early-Onset Amyotrophic Lateral Sclerosis.Cross-functional E3 ligases Parkin and C-terminus Hsp70-interacting protein in neurodegenerative disorders.Protein homeostasis, aging and Alzheimer's disease.Intraneuronal β-amyloid and its interactions with proteins and subcellular organelles.Role of proteomics in understanding prion infection.DC2 and keratinocyte-associated protein 2 (KCP2), subunits of the oligosaccharyltransferase complex, are regulators of the gamma-secretase-directed processing of amyloid precursor protein (APP).Molecular Mechanism for Various Pharmacological Activities of NSAIDS Modulation of AβPP and GSK3β by Endoplasmic Reticulum Stress and Involvement in Alzheimer's Disease.Lysophosphatidic acid receptor activation affects the C13NJ microglia cell line proteome leading to alterations in glycolysis, motility, and cytoskeletal architecture.A molecular chaperone glucose-regulated protein 94 blocks apoptosis induced by virus infection.Involvement of prostaglandin E2 in production of amyloid-beta peptides both in vitro and in vivo.Conformational targeting of intracellular Aβ oligomers demonstrates their pathological oligomerization inside the endoplasmic reticulum.β-Secretase 1's Targeting Reduces Hyperphosphorilated Tau, Implying Autophagy Actors in 3xTg-AD Mice.Gene expression in primary cultured astrocytes affected by aluminum: alteration of chaperons involved in protein folding Functional rescue of P23H rhodopsin photoreceptors by gene delivery.Neurons Export Extracellular Vesicles Enriched in Cysteine String Protein and Misfolded Protein Cargo.Alzheimer disease: modeling an Aβ-centered biological network.

P2860

Q24338484-5D3AE3F8-E4E0-4728-9D4F-0FED82635879 Q28300625-BDE3261C-4520-462B-AF87-90260384D930 Q28476363-235727CB-5282-465A-B297-50AB41CEE7DD Q30392284-C85E3F0E-4C1E-490B-BB07-58256F04AB53 Q33576967-7CF62CC6-5D1F-4CF3-B718-6AEAF0981031 Q33589732-20E26E4B-346F-4C55-AB61-8CD74BBEB33E Q33674213-C147669B-8B51-4DDA-9546-BC9F8D3E6AC4 Q33745135-AB0B3A7C-4BA9-43D6-BCEA-00BB4099E9A1 Q33749114-E7CB074C-E550-4D13-9D12-2BBA8E686D7B Q33778232-1424AE67-F265-4C62-A96A-D827FA1F2A73 Q33796184-6FC76297-C58A-45ED-A2A9-EE348F7CF8A8 Q33800204-0A34ECA2-4EDD-4B47-A2BB-C12014EEC8DD Q33854917-1C8BB6E8-A0C8-4EE4-83CD-71DD4638EAA7 Q34923990-8EE3BF72-0C8E-4589-9F18-969FF1FEEAC1 Q35311053-3601FF81-1A66-40D9-97C2-7E645F69A364 Q35709838-DD3C9414-91B1-4A0E-BF01-9D717C59F747 Q35748263-601B3D8F-A897-4439-9A47-39A8E96C1D42 Q36662140-ADE1C815-C0B5-4466-A39D-ECEE14CF0AAF Q36809544-D8739CA3-9BA2-4DD6-9323-F29644D39B08 Q36955453-CC50F558-665E-43C1-AA32-F14D390BBC96 Q37074474-A9C19295-F52C-4818-8538-6F1132673520 Q37258545-9139482E-67EC-4D01-A5E1-4A4C93C9F7AB Q37486421-A9A48F0F-A0FA-479A-A633-DA487983DA48 Q37739259-EC1AF5E9-00B3-47E9-8C59-CD9781B50385 Q37958101-D6A0126C-2EE2-48D0-BC82-92BA6EC24120 Q37987808-539BFF53-F664-4E8F-A628-686877ACE1BD Q38060656-D294F836-4247-4F99-8D4E-C465332605B8 Q38068928-90A14117-AAA7-4A9F-8872-C654045B252C Q38419073-BAF1F18E-B9A6-40DD-A8E9-EC5A2EA7C928 Q38974315-14EE9FA0-91A8-4B92-9581-0AE3F4AE1997 Q39198755-F2033ED0-793F-4EDB-9BE5-CE91A59E86CC Q39777367-E9BECD0A-BD9F-4EF8-A84D-987331AC73D0 Q40013272-EF1D027D-74F9-400D-ABA3-069DC17FC8AA Q40085988-52903905-FF4A-44B2-B512-3AB46FAE144A Q40470312-811DB563-D526-4EB6-ABBE-789ECF944A8D Q40969425-0BCFE01E-C711-4A38-B39C-0CB18D92714C Q41114641-A8E5A8D5-F946-4BD7-865E-4D954341EE38 Q41867422-D78A87F7-05A6-4D61-B454-BFF465FA6686 Q42269174-CFD75078-3211-4F9E-A267-C9E2D8CC46DE Q47878052-C9C85759-A8A1-4545-8B23-544A7C5874F9

P2860

Endoplasmic reticulum chaperones inhibit the production of amyloid-beta peptides.

http://www.wikidata.org/entity/Q40203503

description

2007 nî lūn-bûn

@nan

2007年の論文

@ja

2007年論文

@yue

2007年論文

@zh-hant

2007年論文

@zh-hk

2007年論文

@zh-mo

2007年論文

@zh-tw

2007年论文

@wuu

2007年论文

@zh

2007年论文

@zh-cn

name

Endoplasmic reticulum chaperones inhibit the production of amyloid-beta peptides.

@en

type

label

Endoplasmic reticulum chaperones inhibit the production of amyloid-beta peptides.

@en

prefLabel

Endoplasmic reticulum chaperones inhibit the production of amyloid-beta peptides.

@en

P1433

Q40203503-23423FA0-FCE7-47E9-8CFC-DB632FCCACC6

P1476

Q40203503-F8D2F3EC-2FC0-484F-B188-58D13F3CA9BD

P2093

Q40203503-100E8AA6-D0FA-4471-BAD8-809E074D28BC

Q40203503-90F33E3E-04DE-477F-85A7-1B31BF3AFBE3

Q40203503-ACCD06D6-8C2A-481C-A66C-6013887E5088

Q40203503-D79D04AE-96D5-402C-AFBD-4E817EC7E585

Q40203503-E14F00ED-C3EB-4379-BFCA-4533D6684D5E

P2860

Q40203503-0AED3CAD-F798-46F3-9989-6BE883586EBE

Q40203503-16EFD511-49B0-4E11-9542-76CA1126E4AB

Q40203503-1999D8A9-F82B-4179-9FFD-801B3F866364

Q40203503-2120EFE6-4384-439D-BAAF-B25FE7D28F4B

Q40203503-35F6FD12-D0E2-4931-8F81-D30B423B3AF4

Q40203503-3A0ADF6D-8207-427A-83E9-F387F887D9F7

Q40203503-40A5E130-EED0-4934-92C4-C597269DDB9B

Q40203503-4797FCF6-B7A3-4D0D-9831-43E7C867DC5F

Q40203503-47EE4FA9-8A28-420C-8955-1C150472CF81

Q40203503-4E69CBD4-DF12-4000-B0B5-97E5DE3D85DF

P304

Q40203503-06A7AC92-677B-45CB-935D-CCACD4A22887

P31

Q40203503-121A6C5E-0005-4D00-BCD0-6BBE7EE835CC

P356

Q40203503-18280828-D6A2-499D-8BF0-AFBB8C1F0720

P407

Q40203503-A1ADD39B-4F38-4F60-8433-17B66E6D4F37

P433

Q40203503-125EDB96-347C-4695-A178-C89912E405E8

P478

Q40203503-A04F18F2-082B-425D-9FFF-08863FDA2886

P50

Q40203503-8E9BC7EA-D16F-4B02-A66B-C81D9BBF6380

P577

Q40203503-98FC7306-67AD-4467-BA35-502F13C88162

P5875

Q40203503-AC3EC84D-1A9B-42A9-8DA1-EC25528B67F9

P698

Q40203503-4134B012-8F2E-45BC-BBE3-90A3648D2A8B

P921

Q40203503-C7782042-D8DF-4819-8590-24F5D9BED714

Q40203503-C9B4D7AB-FEC4-4ACD-BD15-9C2EB7ECC0FA

P932

Q40203503-162BF73A-D683-489F-9810-8028CF45B53B

P356

P1433

Biochemical Journal

P1476

Endoplasmic reticulum chaperones inhibit the production of amyloid-beta peptides

@en

P2093

Keitarou Suzuki

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

Tadashi Nakaya

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

Tatsuya Hoshino

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

Tohru Mizushima

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

Toshiharu Suzuki

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

P2860

Alzheimer-type neuropathology in transgenic mice overexpressing V717F β-amyloid precursor protein

Induction of Grp78/BiP by translational block: activation of the Grp78 promoter by ATF4 through and upstream ATF/CRE site independent of the endoplasmic reticulum stress elements

An intracellular protein that binds amyloid-beta peptide and mediates neurotoxicity in Alzheimer's disease

Pathways towards and away from Alzheimer's disease

The amyloid hypothesis of Alzheimer's disease: progress and problems on the road to therapeutics

Deranged expression of molecular chaperones in brains of patients with Alzheimer's disease

ORP150 protects against hypoxia/ischemia-induced neuronal death

A transcriptionally [correction of transcriptively] active complex of APP with Fe65 and histone acetyltransferase Tip60

EDEM as an acceptor of terminally misfolded glycoproteins released from calnexin

Regulated translation initiation controls stress-induced gene expression in mammalian cells

P304

581-589

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

P31

scholarly article

P356

10.1042/BJ20061318

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

P407

P433

3

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

P478

402

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

P50

P577

2007-03-01T00:00:00Z

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

P5875

6666745

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

P698

17132139

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

P921

molecular chaperones

endoplasmic reticulum

P932

1863563

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