KEGG PATHWAY: ko05020

PATHWAY: ko05020

Entry

ko05020                     Pathway

Name

Prion disease

Description

Prion diseases, also termed transmissible spongiform encephalopathies (TSEs), are a group of fatal neurodegenerative diseases that affect humans and a number of other animal species. The etiology of these diseases is thought to be associated with the conversion of a normal protein, PrPC, into an infectious, pathogenic form, PrPSc. The conversion is induced by prion infections (for example, variant Creutzfeldt-Jakob disease (vCJD), iatrogenic CJD, Kuru), mutations (familial CJD, Gerstmann-Straussler-Scheinker syndrome, fatal familial insomnia (FFI)) or unknown factors (sporadic CJD (sCJD)), and is thought to occur after PrPC has reached the plasma membrane or is re-internalized for degradation. The PrPSc form shows greater protease resistance than PrPC and accumulates in affected individuals, often in the form of extracellular plaques. Pathways that may lead to neuronal death comprise oxidative stress, regulated activation of complement, ubiquitin-proteasome and endosomal-lysosomal systems, synaptic alterations and dendritic atrophy, corticosteroid response, and endoplasmic reticulum stress. In addition, the conformational transition could lead to the lost of a beneficial activity of the natively folded protein, PrPC.

Class

Human Diseases; Neurodegenerative disease

Pathway map

ko05020

Prion disease

Disease

H00061

Prion disease

Orthology

K05634

prion protein

K06491

neural cell adhesion molecule

K05635

laminin, gamma 1

K04565

superoxide dismutase, Cu-Zn family [EC:1.15.1.1]

K09553

stress-induced-phosphoprotein 1

K04345

protein kinase A [EC:2.7.11.11]

K02159

apoptosis regulator BAX

K05703

tyrosine-protein kinase Fyn [EC:2.7.10.2]

K05208

glutamate receptor ionotropic, NMDA 1

K05209

glutamate receptor ionotropic, NMDA 2A

K05210

glutamate receptor ionotropic, NMDA 2B

K05211

glutamate receptor ionotropic, NMDA 2C

K05212

glutamate receptor ionotropic, NMDA 2D

K05213

glutamate receptor ionotropic, NMDA 3A

K05214

glutamate receptor ionotropic, NMDA 3B

K04849

voltage-dependent calcium channel N type alpha-1B

K04850

voltage-dependent calcium channel L type alpha-1C

K04851

voltage-dependent calcium channel L type alpha-1D

K04853

voltage-dependent calcium channel L type alpha-1F

K04857

voltage-dependent calcium channel L type alpha-1S

K09490

endoplasmic reticulum chaperone BiP [EC:3.6.4.10]

K08860

eukaryotic translation initiation factor 2-alpha kinase 3 [EC:2.7.11.1]

K03237

translation initiation factor 2 subunit 1

K04374

cyclic AMP-dependent transcription factor ATF-4

K04452

DNA damage-inducible transcript 3

K04961

ryanodine receptor 1

K04962

ryanodine receptor 2

K04963

ryanodine receptor 3

K04958

inositol 1,4,5-triphosphate receptor type 1

K04959

inositol 1,4,5-triphosphate receptor type 2

K04960

inositol 1,4,5-triphosphate receptor type 3

K04741

caspase 12 [EC:3.4.22.-]

K04348

serine/threonine-protein phosphatase 2B catalytic subunit [EC:3.1.3.16]

K06268

serine/threonine-protein phosphatase 2B regulatory subunit

K02158

Bcl-2-antagonist of cell death

K05862

voltage-dependent anion channel protein 1

K15040

voltage-dependent anion channel protein 2

K15041

voltage-dependent anion channel protein 3

K05863

solute carrier family 25 (mitochondrial adenine nucleotide translocator), member 4/5/6/31

K09565

peptidyl-prolyl isomerase F (cyclophilin D) [EC:5.2.1.8]

K02084

apoptotic protease-activating factor

K08738

cytochrome c

K04399

caspase 9 [EC:3.4.22.62]

K02187

caspase 3 [EC:3.4.22.56]

K20858

calcium uniporter protein, mitochondrial

K03878

NADH-ubiquinone oxidoreductase chain 1 [EC:7.1.1.2]

K03879

NADH-ubiquinone oxidoreductase chain 2 [EC:7.1.1.2]

K03880

NADH-ubiquinone oxidoreductase chain 3 [EC:7.1.1.2]

K03881

NADH-ubiquinone oxidoreductase chain 4 [EC:7.1.1.2]

K03882

NADH-ubiquinone oxidoreductase chain 4L [EC:7.1.1.2]

K03883

NADH-ubiquinone oxidoreductase chain 5 [EC:7.1.1.2]

K03884

NADH-ubiquinone oxidoreductase chain 6 [EC:7.1.1.2]

K03942

NADH dehydrogenase (ubiquinone) flavoprotein 1 [EC:7.1.1.2]

K03943

NADH dehydrogenase (ubiquinone) flavoprotein 2 [EC:7.1.1.2]

K03944

NADH dehydrogenase (ubiquinone) flavoprotein 3

K03945

NADH dehydrogenase (ubiquinone) 1 alpha subcomplex subunit 1

K03946

NADH dehydrogenase (ubiquinone) 1 alpha subcomplex subunit 2

K03947

NADH dehydrogenase (ubiquinone) 1 alpha subcomplex subunit 3

K03948

NADH dehydrogenase (ubiquinone) 1 alpha subcomplex subunit 4

K03949

NADH dehydrogenase (ubiquinone) 1 alpha subcomplex subunit 5

K03950

NADH dehydrogenase (ubiquinone) 1 alpha subcomplex subunit 6

K03951

NADH dehydrogenase (ubiquinone) 1 alpha subcomplex subunit 7

K03952

NADH dehydrogenase (ubiquinone) 1 alpha subcomplex subunit 8

K03953

NADH dehydrogenase (ubiquinone) 1 alpha subcomplex subunit 9

K03954

NADH dehydrogenase (ubiquinone) 1 alpha subcomplex subunit 10

K03955

NADH dehydrogenase (ubiquinone) 1 alpha/beta subcomplex 1, acyl-carrier protein

K03956

NADH dehydrogenase (ubiquinone) 1 alpha subcomplex subunit 11

K11352

NADH dehydrogenase (ubiquinone) 1 alpha subcomplex subunit 12

K11353

NADH dehydrogenase (ubiquinone) 1 alpha subcomplex subunit 13

K03957

NADH dehydrogenase (ubiquinone) 1 beta subcomplex subunit 1

K03958

NADH dehydrogenase (ubiquinone) 1 beta subcomplex subunit 2

K03959

NADH dehydrogenase (ubiquinone) 1 beta subcomplex subunit 3

K03960

NADH dehydrogenase (ubiquinone) 1 beta subcomplex subunit 4

K03961

NADH dehydrogenase (ubiquinone) 1 beta subcomplex subunit 5

K03962

NADH dehydrogenase (ubiquinone) 1 beta subcomplex subunit 6

K03963

NADH dehydrogenase (ubiquinone) 1 beta subcomplex subunit 7

K03964

NADH dehydrogenase (ubiquinone) 1 beta subcomplex subunit 8

K03965

NADH dehydrogenase (ubiquinone) 1 beta subcomplex subunit 9

K03966

NADH dehydrogenase (ubiquinone) 1 beta subcomplex subunit 10

K11351

NADH dehydrogenase (ubiquinone) 1 beta subcomplex subunit 11

K03934

NADH dehydrogenase (ubiquinone) Fe-S protein 1 [EC:7.1.1.2]

K03935

NADH dehydrogenase (ubiquinone) Fe-S protein 2 [EC:7.1.1.2]

K03936

NADH dehydrogenase (ubiquinone) Fe-S protein 3 [EC:7.1.1.2]

K03937

NADH dehydrogenase (ubiquinone) Fe-S protein 4

K03938

NADH dehydrogenase (ubiquinone) Fe-S protein 5

K03939

NADH dehydrogenase (ubiquinone) Fe-S protein 6

K03940

NADH dehydrogenase (ubiquinone) Fe-S protein 7 [EC:7.1.1.2]

K03941

NADH dehydrogenase (ubiquinone) Fe-S protein 8 [EC:7.1.1.2]

K03967

NADH dehydrogenase (ubiquinone) 1 subunit C1

K03968

NADH dehydrogenase (ubiquinone) 1 subunit C2

K00234

succinate dehydrogenase (ubiquinone) flavoprotein subunit [EC:1.3.5.1]

K00235

succinate dehydrogenase (ubiquinone) iron-sulfur subunit [EC:1.3.5.1]

K00236

succinate dehydrogenase (ubiquinone) cytochrome b560 subunit

K00237

succinate dehydrogenase (ubiquinone) membrane anchor subunit

K00411

ubiquinol-cytochrome c reductase iron-sulfur subunit [EC:7.1.1.8]

K00412

ubiquinol-cytochrome c reductase cytochrome b subunit

K00413

ubiquinol-cytochrome c reductase cytochrome c1 subunit

K00414

ubiquinol-cytochrome c reductase core subunit 1

K00415

ubiquinol-cytochrome c reductase core subunit 2

K00416

ubiquinol-cytochrome c reductase subunit 6

K00417

ubiquinol-cytochrome c reductase subunit 7

K00418

ubiquinol-cytochrome c reductase subunit 8

K00419

ubiquinol-cytochrome c reductase subunit 9

K00420

ubiquinol-cytochrome c reductase subunit 10

K02262

cytochrome c oxidase subunit 3

K02256

cytochrome c oxidase subunit 1 [EC:7.1.1.9]

K02261

cytochrome c oxidase subunit 2

K02263

cytochrome c oxidase subunit 4

K02264

cytochrome c oxidase subunit 5a

K02265

cytochrome c oxidase subunit 5b

K02266

cytochrome c oxidase subunit 6a

K02267

cytochrome c oxidase subunit 6b

K02268

cytochrome c oxidase subunit 6c

K02270

cytochrome c oxidase subunit 7a

K02271

cytochrome c oxidase subunit 7b

K02272

cytochrome c oxidase subunit 7c

K02273

cytochrome c oxidase subunit 8

K02132

F-type H+-transporting ATPase subunit alpha

K02133

F-type H+-transporting ATPase subunit beta [EC:7.1.2.2]

K02136

F-type H+-transporting ATPase subunit gamma

K02134

F-type H+-transporting ATPase subunit delta

K02135

F-type H+-transporting ATPase subunit epsilon

K02126

F-type H+-transporting ATPase subunit a

K02127

F-type H+-transporting ATPase subunit b

K02128

F-type H+-transporting ATPase subunit c

K02138

F-type H+-transporting ATPase subunit d

K02137

F-type H+-transporting ATPase subunit O

K02131

F-type H+-transporting ATPase subunit 6

K02125

F-type H+-transporting ATPase subunit 8

K02730

20S proteasome subunit alpha 1 [EC:3.4.25.1]

K02726

20S proteasome subunit alpha 2 [EC:3.4.25.1]

K02728

20S proteasome subunit alpha 3 [EC:3.4.25.1]

K02731

20S proteasome subunit alpha 4 [EC:3.4.25.1]

K02729

20S proteasome subunit alpha 5 [EC:3.4.25.1]

K02725

20S proteasome subunit alpha 6 [EC:3.4.25.1]

K02727

20S proteasome subunit alpha 7 [EC:3.4.25.1]

K02738

20S proteasome subunit beta 1 [EC:3.4.25.1]

K02739

20S proteasome subunit beta 2 [EC:3.4.25.1]

K02735

20S proteasome subunit beta 3 [EC:3.4.25.1]

K02734

20S proteasome subunit beta 4 [EC:3.4.25.1]

K02737

20S proteasome subunit beta 5 [EC:3.4.25.1]

K02732

20S proteasome subunit beta 6 [EC:3.4.25.1]

K02736

20S proteasome subunit beta 7 [EC:3.4.25.1]

K03061

26S proteasome regulatory subunit T1

K03062

26S proteasome regulatory subunit T2

K03063

26S proteasome regulatory subunit T3

K03064

26S proteasome regulatory subunit T4

K03065

26S proteasome regulatory subunit T5

K03066

26S proteasome regulatory subunit T6

K03028

26S proteasome regulatory subunit N1

K03032

26S proteasome regulatory subunit N2

K03033

26S proteasome regulatory subunit N3

K06693

26S proteasome regulatory subunit N4

K03035

26S proteasome regulatory subunit N5

K03036

26S proteasome regulatory subunit N6

K03037

26S proteasome regulatory subunit N7

K03038

26S proteasome regulatory subunit N8

K03039

26S proteasome regulatory subunit N9

K03029

26S proteasome regulatory subunit N10

K03030

26S proteasome regulatory subunit N11

K03031

26S proteasome regulatory subunit N12

K06691

26S proteasome regulatory subunit N13

K10881

26 proteasome complex subunit DSS1

K03994

complement component 5

K03995

complement component 6

K03996

complement component 7

K03997

complement component 8 subunit alpha

K03998

complement component 8 subunit beta

K03999

complement component 8 subunit gamma

K04000

complement component 9

K03986

complement C1q subcomponent subunit A

K03987

complement C1q subcomponent subunit B

K03988

complement C1q subcomponent subunit C

K03283

heat shock 70kDa protein 1/6/8

K02599

Notch 1

K06278

caveolin 1

K12958

caveolin 2

K12959

caveolin 3

K00922

phosphatidylinositol-4,5-bisphosphate 3-kinase catalytic subunit alpha/beta/delta [EC:2.7.1.153]

K02649

phosphoinositide-3-kinase regulatory subunit alpha/beta/delta

K06068

novel protein kinase C delta type [EC:2.7.11.13]

K21421

NADPH oxidase 2 [EC:1.-.-.-]

K08009

cytochrome b-245, alpha polypeptide

K08012

neutrophil cytosolic factor 4

K08011

neutrophil cytosolic factor 1

K08010

neutrophil cytosolic factor 2

K04392

Ras-related C3 botulinum toxin substrate 1

K07860

Ras-related C3 botulinum toxin substrate 2

K04441

p38 MAP kinase [EC:2.7.11.24]

K04440

mitogen-activated protein kinase 8/9/10 (c-Jun N-terminal kinase) [EC:2.7.11.24]

K04371

mitogen-activated protein kinase 1/3 [EC:2.7.11.24]

K05870

cyclic AMP-responsive element-binding protein 1

K04450

cyclic AMP-dependent transcription factor ATF-2

K09048

cyclic AMP-responsive element-binding protein 3

K09047

cyclic AMP-responsive element-binding protein 5

K09049

cyclic AMP-dependent transcription factor ATF-6 beta

K09203

early growth response protein 1

K12499

C-C motif chemokine 5

K04383

interleukin 1 alpha

K04519

interleukin 1 beta

K05405

interleukin 6

K03156

tumor necrosis factor superfamily, member 2

K03083

glycogen synthase kinase 3 beta [EC:2.7.11.26]

K03097

casein kinase II subunit alpha [EC:2.7.11.1]

K03115

casein kinase II subunit beta

K10396

kinesin family member 5

K10407

kinesin light chain

K07374

tubulin alpha

K07375

tubulin beta

Compound

C00027

Hydrogen peroxide

C00076

Calcium cation

C00575

3',5'-Cyclic AMP

C00704

Superoxide

C02140

Corticosterone

Reference

PMID:27055367

Authors

Saa P, Harris DA, Cervenakova L

Title

Mechanisms of prion-induced neurodegeneration.

Journal

Expert Rev Mol Med 18:e5 (2016)
DOI:10.1017/erm.2016.8

Reference

PMID:25584786

Authors

Goold R, McKinnon C, Tabrizi SJ

Title

Prion degradation pathways: Potential for therapeutic intervention.

Journal

Mol Cell Neurosci 66:12-20 (2015)
DOI:10.1016/j.mcn.2014.12.009

Reference

PMID:20889378

Authors

Soto C, Satani N

Title

The intricate mechanisms of neurodegeneration in prion diseases.

Journal

Trends Mol Med 17:14-24 (2011)
DOI:10.1016/j.molmed.2010.09.001

Reference

PMID:27060771

Authors

Mays CE, Soto C

Title

The stress of prion disease.

Journal

Brain Res 1648:553-560 (2016)
DOI:10.1016/j.brainres.2016.04.009

Reference

PMID:32565065

Authors

Jones E, Mead S

Title

Genetic risk factors for Creutzfeldt-Jakob disease.

Journal

Neurobiol Dis 142:104973 (2020)
DOI:10.1016/j.nbd.2020.104973

Reference

PMID:18245809

Authors

Kovacs GG, Budka H

Title

Prion diseases: from protein to cell pathology.

Journal

Am J Pathol 172:555-65 (2008)
DOI:10.2353/ajpath.2008.070442

Reference

PMID:15695097

Authors

Campana V, Sarnataro D, Zurzolo C

Title

The highways and byways of prion protein trafficking.

Journal

Trends Cell Biol 15:102-11 (2005)
DOI:10.1016/j.tcb.2004.12.002

Reference

PMID:17051207

Authors

Caughey B, Baron GS

Title

Prions and their partners in crime.

Journal

Nature 443:803-10 (2006)
DOI:10.1038/nature05294

Reference

PMID:11592845

Authors

Chiesa R, Harris DA

Title

Prion diseases: what is the neurotoxic molecule?

Journal

Neurobiol Dis 8:743-63 (2001)
DOI:10.1006/nbdi.2001.0433

Reference

PMID:17085779

Authors

Fasano C, Campana V, Zurzolo C

Title

Prions: protein only or something more? Overview of potential prion cofactors.

Journal

J Mol Neurosci 29:195-214 (2006)
DOI:10.1385/JMN:29:3:195

Reference

PMID:14705136

Authors

Roucou X, Gains M, LeBlanc AC

Title

Neuroprotective functions of prion protein.

Journal

J Neurosci Res 75:153-61 (2004)
DOI:10.1002/jnr.10864

Reference

PMID:10398674

Authors

Harris DA

Title

Cellular biology of prion diseases.

Journal

Clin Microbiol Rev 12:429-44 (1999)

Reference

PMID:15890824

Authors

Novakofski J, Brewer MS, Mateus-Pinilla N, Killefer J, McCusker RH

Title

Prion biology relevant to bovine spongiform encephalopathy.

Journal

J Anim Sci 83:1455-76 (2005)
DOI:10.2527/2005.8361455x

Reference

PMID:27581199

Authors

Peggion C, Bertoli A, Sorgato MC

Title

Almost a century of prion protein(s): From pathology to physiology, and back to pathology.

Journal

Biochem Biophys Res Commun 483:1148-1155 (2017)
DOI:10.1016/j.bbrc.2016.07.118

Reference

PMID:31618844

Authors

Ryskalin L, Busceti CL, Biagioni F, Limanaqi F, Familiari P, Frati A, Fornai F

Title

Prion Protein in Glioblastoma Multiforme.

Journal

Int J Mol Sci 20:E5107 (2019)
DOI:10.3390/ijms20205107

Reference

PMID:31795242

Authors

Ureshino RP, Erustes AG, Bassani TB, Wachilewski P, Guarache GC, Nascimento AC, Costa AJ, Smaili SS, Pereira GJDS

Title

The Interplay between Ca(2+) Signaling Pathways and Neurodegeneration.

Journal

Int J Mol Sci 20:E6004 (2019)
DOI:10.3390/ijms20236004

Reference

PMID:30710214

Authors

Meneghetti E, Gasperini L, Virgilio T, Moda F, Tagliavini F, Benetti F, Legname G

Title

Prions Strongly Reduce NMDA Receptor S-Nitrosylation Levels at Pre-symptomatic and Terminal Stages of Prion Diseases.

Journal

Mol Neurobiol 56:6035-6045 (2019)
DOI:10.1007/s12035-019-1505-6

Reference

PMID:23439666

Authors

Song Z, Zhao D, Yang L

Title

Molecular mechanisms of neurodegeneration mediated by dysfunctional subcellular organelles in transmissible spongiform encephalopathies.

Journal

Acta Biochim Biophys Sin (Shanghai) 45:452-64 (2013)
DOI:10.1093/abbs/gmt014

Reference

PMID:28643372

Authors

Halliday M, Hughes D, Mallucci GR

Title

Fine-tuning PERK signaling for neuroprotection.

Journal

J Neurochem 142:812-826 (2017)
DOI:10.1111/jnc.14112

Reference

PMID:29194372

Authors

Hughes D, Halliday M

Title

What Is Our Current Understanding of PrP(Sc)-Associated Neurotoxicity and Its Molecular Underpinnings?

Journal

Pathogens 6:E63 (2017)
DOI:10.3390/pathogens6040063

Reference

PMID:24619348

Authors

Hetz C, Mollereau B

Title

Disturbance of endoplasmic reticulum proteostasis in neurodegenerative diseases.

Journal

Nat Rev Neurosci 15:233-49 (2014)
DOI:10.1038/nrn3689

Reference

PMID:29476642

Authors

Hughes D, Mallucci GR

Title

The unfolded protein response in neurodegenerative disorders - therapeutic modulation of the PERK pathway.

Journal

FEBS J 286:342-355 (2019)
DOI:10.1111/febs.14422

Reference

PMID:21722302

Authors

Doyle KM, Kennedy D, Gorman AM, Gupta S, Healy SJ, Samali A

Title

Unfolded proteins and endoplasmic reticulum stress in neurodegenerative disorders.

Journal

J Cell Mol Med 15:2025-39 (2011)
DOI:10.1111/j.1582-4934.2011.01374.x

Reference

PMID:18420416

Authors

Ferreiro E, Oliveira CR, Pereira CM

Title

The release of calcium from the endoplasmic reticulum induced by amyloid-beta and prion peptides activates the mitochondrial apoptotic pathway.

Journal

Neurobiol Dis 30:331-42 (2008)
DOI:10.1016/j.nbd.2008.02.003

Reference

PMID:16844381

Authors

Ferreiro E, Resende R, Costa R, Oliveira CR, Pereira CM

Title

An endoplasmic-reticulum-specific apoptotic pathway is involved in prion and amyloid-beta peptides neurotoxicity.

Journal

Neurobiol Dis 23:669-78 (2006)
DOI:10.1016/j.nbd.2006.05.011

Reference

PMID:21980554

Authors

Torres M, Encina G, Soto C, Hetz C

Title

Abnormal calcium homeostasis and protein folding stress at the ER: A common factor in familial and infectious prion disorders.

Journal

Commun Integr Biol 4:258-61 (2011)
DOI:10.4161/cib.4.3.15019

Reference

PMID:25766616

Authors

Ciechanover A, Kwon YT

Title

Degradation of misfolded proteins in neurodegenerative diseases: therapeutic targets and strategies.

Journal

Exp Mol Med 47:e147 (2015)
DOI:10.1038/emm.2014.117

Reference

PMID:17466621

Authors

Kristiansen M, Deriziotis P, Dimcheff DE, Jackson GS, Ovaa H, Naumann H, Clarke AR, van Leeuwen FW, Menendez-Benito V, Dantuma NP, Portis JL, Collinge J, Tabrizi SJ

Title

Disease-associated prion protein oligomers inhibit the 26S proteasome.

Journal

Mol Cell 26:175-88 (2007)
DOI:10.1016/j.molcel.2007.04.001

Reference

PMID:10195903

Authors

Wang HG, Pathan N, Ethell IM, Krajewski S, Yamaguchi Y, Shibasaki F, McKeon F, Bobo T, Franke TF, Reed JC.

Title

Ca2+-induced apoptosis through calcineurin dephosphorylation of BAD.

Journal

Science 284:339-43 (1999)
DOI:10.1126/science.284.5412.339

Reference

PMID:14532116

Authors

Hetz C, Russelakis-Carneiro M, Maundrell K, Castilla J, Soto C

Title

Caspase-12 and endoplasmic reticulum stress mediate neurotoxicity of pathological prion protein.

Journal

EMBO J 22:5435-45 (2003)
DOI:10.1093/emboj/cdg537

Reference

PMID:31417367

Authors

Zamponi E, Pigino GF

Title

Protein Misfolding, Signaling Abnormalities and Altered Fast Axonal Transport: Implications for Alzheimer and Prion Diseases.

Journal

Front Cell Neurosci 13:350 (2019)
DOI:10.3389/fncel.2019.00350

Reference

PMID:29261664

Authors

Zamponi E, Buratti F, Cataldi G, Caicedo HH, Song Y, Jungbauer LM, LaDu MJ, Bisbal M, Lorenzo A, Ma J, Helguera PR, Morfini GA, Brady ST, Pigino GF

Title

Prion protein inhibits fast axonal transport through a mechanism involving casein kinase 2.

Journal

PLoS One 12:e0188340 (2017)
DOI:10.1371/journal.pone.0188340

Reference

PMID:21196165

Authors

Schneider B, Pietri M, Pradines E, Loubet D, Launay JM, Kellermann O, Mouillet-Richard S

Title

Understanding the neurospecificity of Prion protein signaling.

Journal

Front Biosci (Landmark Ed) 16:169-86 (2011)
DOI:10.2741/3682

Reference

PMID:23479001

Authors

Didonna A

Title

Prion protein and its role in signal transduction.

Journal

Cell Mol Biol Lett 18:209-30 (2013)
DOI:10.2478/s11658-013-0085-0

Reference

PMID:28507517

Authors

Shah SZA, Zhao D, Hussain T, Yang L

Title

The Role of Unfolded Protein Response and Mitogen-Activated Protein Kinase Signaling in Neurodegenerative Diseases with Special Focus on Prion Diseases.

Journal

Front Aging Neurosci 9:120 (2017)
DOI:10.3389/fnagi.2017.00120

Reference

PMID:15528202

Authors

Marella M, Gaggioli C, Batoz M, Deckert M, Tartare-Deckert S, Chabry J

Title

Pathological prion protein exposure switches on neuronal mitogen-activated protein kinase pathway resulting in microglia recruitment.

Journal

J Biol Chem 280:1529-34 (2005)
DOI:10.1074/jbc.M410966200

Reference

PMID:15640354

Authors

Ishikura N, Clever JL, Bouzamondo-Bernstein E, Samayoa E, Prusiner SB, Huang EJ, DeArmond SJ

Title

Notch-1 activation and dendritic atrophy in prion disease.

Journal

Proc Natl Acad Sci U S A 102:886-91 (2005)
DOI:10.1073/pnas.0408612101

Reference

PMID:20205843

Authors

Dearmond SJ, Bajsarowicz K

Title

PrPSc accumulation in neuronal plasma membranes links Notch-1 activation to dendritic degeneration in prion diseases.

Journal

Mol Neurodegener 5:6 (2010)
DOI:10.1186/1750-1326-5-6

Reference

PMID:29998397

Authors

Hirsch TZ, Martin-Lanneree S, Reine F, Hernandez-Rapp J, Herzog L, Dron M, Privat N, Passet B, Halliez S, Villa-Diaz A, Lacroux C, Klein V, Haik S, Andreoletti O, Torres JM, Vilotte JL, Beringue V, Mouillet-Richard S

Title

Epigenetic Control of the Notch and Eph Signaling Pathways by the Prion Protein: Implications for Prion Diseases.

Journal

Mol Neurobiol 56:2159-2173 (2019)
DOI:10.1007/s12035-018-1193-7

Reference

PMID:28714865

Authors

Aguzzi A, Zhu C

Title

Microglia in prion diseases.

Journal

J Clin Invest 127:3230-3239 (2017)
DOI:10.1172/JCI90605