Prion disease tempo determined by host-dependent substrate reduction. - Wikidata - awgldk - TriplyDB

Prion disease tempo determined by host-dependent substrate reduction.

Prion disease tempo determined by host-dependent substrate reduction.

http://www.wikidata.org/entity/Q37524308

about

Prion neuropathology follows the accumulation of alternate prion protein isoforms after infective titre has peaked.Octarepeat region flexibility impacts prion function, endoproteolysis and disease manifestation Double-Edge Sword of Sustained ROCK Activation in Prion Diseases through Neuritogenesis Defects and Prion Accumulation Early Generation of New PrPSc on Blood Vessels after Brain Microinjection of Scrapie in Mice Prion Infectivity Plateaus and Conversion to Symptomatic Disease Originate from Falling Precursor Levels and Increased Levels of Oligomeric PrPSc Species.Inhibition of the FKBP family of peptidyl prolyl isomerases induces abortive translocation and degradation of the cellular prion protein.Neuroprotective properties of the PrP-like Shadoo glycoprotein assessed in the middle cerebral artery occlusion model of ischemia Rapidly progressive Alzheimer's disease features distinct structures of amyloid-β.Intra-host mathematical model of chronic wasting disease dynamics in deer (Odocoileus).The Biological Function of the Prion Protein: A Cell Surface Scaffold of Signaling Modules Physiological Functions of the Cellular Prion Protein.From Neurodegeneration to Brain Health: An Integrated Approach.Endoproteolytic processing of the mammalian prion glycoprotein family.The double life of the ribosome: When its protein folding activity supports prion propagation.The prion protein constitutively controls neuronal store-operated Ca(2+) entry through Fyn kinase.Reduced Abundance and Subverted Functions of Proteins in Prion-Like Diseases: Gained Functions Fascinate but Lost Functions Affect Aetiology.Prion Strains and Transmission Barrier Phenomena.What Is Our Current Understanding of PrPSc-Associated Neurotoxicity and Its Molecular Underpinnings?The Role of the Mammalian Prion Protein in the Control of Sleep.Protein Misfolding in Prion and Prion-Like Diseases: Reconsidering a Required Role for Protein Loss-of-Function.Prion acute synaptotoxicity is largely driven by protease-resistant PrPSc species

P2860

Q33924117-6F7A3158-D190-4D7C-B2CE-94F8A0F0D696 Q35192463-31102DAB-1E25-426D-BA61-7830483A352A Q35737668-1D538B79-38BF-41BF-B0C8-B47F79DCA95A Q36143652-DEE8DD3A-F81C-4244-9D77-DC6458FF1B89 Q36334344-9CBE2D1A-8D31-4977-AA5C-CBD22EFF6EC8 Q36716367-C290F491-1D48-4180-BB03-E68035B11A88 Q37135556-A25B22CD-B3FC-4F53-8F40-7B86090C19CF Q37238082-564E48EA-FD14-4D63-9D0D-3AF8C9EDCFF8 Q37409418-B711D405-2FA2-4FB6-A95F-9777B1A251E1 Q37710410-97D4C3D1-933D-4B88-B9C6-6CC32AE7D946 Q37739095-467889DD-21DC-4FE5-B7FE-237F2F1B2678 Q38365566-3B9F7694-02E7-4658-A6A5-82BDA744985B Q39052720-4FE0D9F4-45C4-461D-A807-2C772FEA0C89 Q39211074-BA106E31-D514-4850-934E-BC2F37689F65 Q40310258-C9C81B2E-73A0-47D9-9D56-AEB321629984 Q44607866-2CBD09FC-773C-486E-B79F-E443DEF52A40 Q47232273-245A22A6-3D21-4F5A-9576-1814FE12C23E Q47342598-3C4BC57E-46CE-43DA-8193-DCC15D67710F Q47392072-44E5D766-DCA1-4132-813B-9E5589E5A963 Q51653976-3089336F-F28E-4CD4-BEEB-A75F750286CF Q58795353-8632D3F1-0825-49F0-8C04-BEFCF8A90B9D

P2860

Prion disease tempo determined by host-dependent substrate reduction.

http://www.wikidata.org/entity/Q37524308

description

article científic

@ca

article scientifique

@fr

articolo scientifico

@it

artigo científico

@pt

bilimsel makale

@tr

scientific article published on 16 January 2014

@en

vedecký článok

@sk

vetenskaplig artikel

@sv

videnskabelig artikel

@da

vědecký článek

@cs

name

Prion disease tempo determined by host-dependent substrate reduction.

@en

Prion disease tempo determined by host-dependent substrate reduction.

@nl

type

label

Prion disease tempo determined by host-dependent substrate reduction.

@en

Prion disease tempo determined by host-dependent substrate reduction.

@nl

prefLabel

Prion disease tempo determined by host-dependent substrate reduction.

@en

Prion disease tempo determined by host-dependent substrate reduction.

@nl

P1433

Q37524308-E1789505-B283-45E4-95F2-4D063C50336F

P1476

Q37524308-11FF1E2D-0767-44BA-9951-1BD37849C1A3

P2093

Q37524308-235E2A10-30CA-49F1-9358-592AC2F761DD

Q37524308-36E0A828-C10F-45A8-877C-23ADC10DBAE6

Q37524308-43DBAA95-8401-4E25-B7F2-817CDBD6075E

Q37524308-5EB1AFAE-6608-4BDC-B601-D1E0827B03DC

Q37524308-649083D8-4FAF-4920-AED3-2519035999A6

Q37524308-67175FDC-1C79-45AC-892A-1AA36970A15F

Q37524308-818CD81A-89E9-49FD-A994-7DD1E328615A

Q37524308-A0FE6ED9-F6C2-4377-999B-7804A292F2E6

Q37524308-C089BC7D-4A05-4CC0-853D-F4F580C16535

Q37524308-CB239D3D-7060-4623-9EB4-4503F6F3B74D

P2860

Q37524308-00AEE654-FC6D-4F35-883E-425CBC3D3C85

Q37524308-09179B35-8D9A-4BF6-AE16-7463F3749C6B

Q37524308-0A77A9BF-370D-4272-BFD2-1A5593957707

Q37524308-0ABE7838-E1BE-4B22-927C-0EBED4D11E35

Q37524308-0F75646E-FCF7-4F6D-B153-389AAA6613FE

Q37524308-1255CC77-A31F-4E6D-A5E2-AC54B3AE0270

Q37524308-1613A0BF-4FCB-491A-A7E4-483BA9911A11

Q37524308-1AEA4EC9-0887-4B5C-A3F0-7C49EBF1B9AA

Q37524308-1D024065-C0AC-48C2-84BB-BCA7896A76F6

Q37524308-1E5F8E85-032A-4DB4-B1A3-74DCCB575F33

P304

Q37524308-9749F57C-EF53-4802-AB5C-48E1746C044C

P31

Q37524308-E36543EC-3DF8-48A6-9860-00CABDA4C703

P356

Q37524308-5B0D548E-44C0-4488-82CB-1FFF636EB3A8

P407

Q37524308-4479D624-B3BC-4E76-8EB4-3B2CD57BA682

P433

Q37524308-7E9D3123-EA0C-4ED0-B865-1CC730BC2BED

P478

Q37524308-137542AC-4036-4486-B12B-707CA75C6E01

P50

Q37524308-0B8656B9-1327-46AB-8290-BCFEF0C50B74

Q37524308-A5B5C3DB-44C8-4487-ABEA-9C8B2B254578

P577

Q37524308-CEE25B0C-4317-48C8-8637-D48970CF6BB0

P698

Q37524308-F05D2E7B-60A1-4721-8FE1-CF04F459AEA1

P921

Q37524308-D94F2A25-1637-43DC-A566-FDCBFC321B74

P932

Q37524308-BD6D032A-1F59-4E0F-B4D4-F538E045057A

P356

P1433

Journal of Clinical Investigation

P1476

Prion disease tempo determined by host-dependent substrate reduction.

@en

P2093

Agnes Lau

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

Chae Kim

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

Charles E Mays

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

David Westaway

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

Glenn C Telling

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

Jacques van der Merwe

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

Jan Langeveld

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

Jennifer Grams

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

Jing Yang

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

Jiri G Safar

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

P2860

NIH Image to ImageJ: 25 years of image analysis

Sustained translational repression by eIF2α-P mediates prion neurodegeneration

Isolation of phosphatidylethanolamine as a solitary cofactor for prion formation in the absence of nucleic acids

Generating a prion with bacterially expressed recombinant prion protein.

Cofactor molecules maintain infectious conformation and restrict strain properties in purified prions

A clinical study of kuru patients with long incubation periods at the end of the epidemic in Papua New Guinea

Mice devoid of PrP are resistant to scrapie

A general model of prion strains and their pathogenicity

Prion propagation and toxicity in vivo occur in two distinct mechanistic phases

Interactome analyses identify ties of PrP and its mammalian paralogs to oligomannosidic N-glycans and endoplasmic reticulum-derived chaperones

P304

847-858

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

P31

scholarly article

P356

10.1172/JCI72241

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

P407

P433

2

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

P478

124

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

P50

Debbie McKenzie

P577

2014-01-16T00:00:00Z

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

P698

24430187

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

P921

Prion protein family

P932

3904628

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