TSE
MCID: PRN023
MIFTS: 57

Prion Disease (TSE)

Categories: Genetic diseases, Mental diseases, Neuronal diseases, Rare diseases

Aliases & Classifications for Prion Disease

MalaCards integrated aliases for Prion Disease:

Name: Prion Disease 12 25 37 15 40 17
Prion Diseases 54 55 44 15 72
Transmissible Spongiform Encephalopathies 25 54 3
Transmissible Spongiform Encephalopathy 12 59
Spongiform Encephalopathy 12 75
Prion Disease Pathway 12 72
Human Transmissible Spongiform Encephalopathies, Inherited 72
Inherited Human Transmissible Spongiform Encephalopathies 25
Prion Disease, Susceptibility to 6
Prion-Associated Disorders 25
Prion-Induced Disorders 25
Transmissible Dementias 25
Prion Induced Disorder 12
Prion Protein Diseases 25
Prion Protein Disease 12
Human Prion Disease 59
Tses 25
Tse 59

Characteristics:

Orphanet epidemiological data:

59
human prion disease
Age of onset: Adult;

Classifications:

Orphanet: 59  
Rare neurological diseases


External Ids:

Disease Ontology 12 DOID:649
KEGG 37 H00061
MeSH 44 D017096
NCIt 50 C128346
SNOMED-CT 68 20484008
ICD10 33 A81.9
ICD10 via Orphanet 34 A81.0 A81.1 A81.8 more
UMLS via Orphanet 73 C0162534
Orphanet 59 ORPHA56970
UMLS 72 C0162534 C0751645 C3536911

Summaries for Prion Disease

NINDS : 54 Transmissible spongiform encephalopathies (TSEs), also known as prion diseases, are a group of rare degenerative brain disorders characterized by tiny holes that give the brain a "spongy" appearance. These holes can be seen when brain tissue is viewed under a microscope. Creutzfeldt-Jakob disease (CJD) is the most well-known of the human TSEs. It is a rare type of dementia that affects about one in every one million people each year. Other human TSEs include kuru, fatal familial insomnia (FFI), and Gerstmann-Straussler-Scheinker disease (GSS). Kuru was identified in people of an isolated tribe in Papua New Guinea and has now almost disappeared. FFI and GSS are extremely rare hereditary diseases, found in just a few families around the world. A new type of CJD, called variant CJD (vCJD), was first described in 1996 and has been found in Great Britain and several other European countries. The initial symptoms of vCJD are different from those of classic CJD and the disorder typically occurs in younger patients. Research suggests that vCJD may have resulted from human consumption of beef from cattle with a TSE disease called bovine spongiform encephalopathy (BSE), also known as "mad cow disease." Other TSEs found in animals include scrapie, which affects sheep and goats; chronic wasting disease, which affects elk and deer; and transmissible mink encephalopathy. In a few rare cases, TSEs have occurred in other mammals such as zoo animals. These cases are probably caused by contaminated feed. CJD and other TSEs also can be transmitted experimentally to mice and other animals in the laboratory. Research suggests that TSEs are caused by an abnormal version of a protein called a prion (prion is short forproteinaceous infectious particle). Prion proteins occur in both a normal form, which is a harmless protein found in the body's cells, and in an infectious form, which causes disease. The harmless and infectious forms of the prion protein are nearly identical, but the infectious form takes on a different folded shape from the normal protein. Human TSEs can occur three ways: sporadically; as hereditary diseases; or through transmission from infected individuals. Sporadic TSEs may develop because some of a person's normal prions spontaneously change into the infectious form of the protein and then alter the prions in other cells in a chain reaction. Inherited cases arise from a change, or mutation, in the prion protein gene that causes the prions to be shaped in an abnormal way. This genetic change may be transmitted to an individual's offspring. Transmission of TSEs from infected individuals is relatively rare. TSEs cannot be transmitted through the air or through touching or most other forms of casual contact. However, they may be transmitted through contact with infected tissue, body fluids, or contaminated medical instruments. Normal sterilization procedures such as boiling or irradiating materials do not prevent transmission of TSEs. Symptoms of TSEs vary, but they commonly include personality changes, psychiatric problems such as depression, lack of coordination, and/or an unsteady gait. Patients also may experience involuntary jerking movements called myoclonus, unusual sensations, insomnia, confusion, or memory problems. In the later stages of the disease, patients have severe mental impairment and lose the ability to move or speak.

MalaCards based summary : Prion Disease, also known as prion diseases, is related to chronic wasting disease and gerstmann-straussler disease. An important gene associated with Prion Disease is PRNP (Prion Protein), and among its related pathways/superpathways are Prion diseases and Neuroscience. The drugs Glycerol and Coal tar have been mentioned in the context of this disorder. Affiliated tissues include brain, testes and cortex, and related phenotypes are growth/size/body region and hematopoietic system

Disease Ontology : 12 A brain disease that is characterized by brain damage resulting from the abnormal folding, clumping and accumulation of cellular proteins in the brain induced by prion proteins.

Genetics Home Reference : 25 Prion disease represents a group of conditions that affect the nervous system in humans and animals. In people, these conditions impair brain function, causing changes in memory, personality, and behavior; a decline in intellectual function (dementia); and abnormal movements, particularly difficulty with coordinating movements (ataxia). The signs and symptoms of prion disease typically begin in adulthood and worsen with time, leading to death within a few months to several years.

CDC : 3 Prion diseases or transmissible spongiform encephalopathies (TSEs) are a family of rare progressive neurodegenerative disorders that affect both humans and animals. They are distinguished by long incubation periods, characteristic spongiform changes associated with neuronal loss, and a failure to induce inflammatory response. The causative agents of TSEs are believed to be prions. The term "prions" refers to abnormal, pathogenic agents that are transmissible and are able to induce abnormal folding of specific normal cellular proteins called prion proteins that are found most abundantly in the brain. The functions of these normal prion proteins are still not completely understood. The abnormal folding of the prion proteins leads to brain damage and the characteristic signs and symptoms of the disease. Prion diseases are usually rapidly progressive and always fatal.

KEGG : 37
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.

Wikipedia : 75 Transmissible spongiform encephalopathies (TSEs) are a group of progressive, invariably fatal,... more...

Related Diseases for Prion Disease

Diseases in the Prion Disease family:

Inherited Prion Disease

Diseases related to Prion Disease via text searches within MalaCards or GeneCards Suite gene sharing:

(show top 50) (show all 256)
# Related Disease Score Top Affiliating Genes
1 chronic wasting disease 33.2 SPRN PRNP CR2
2 gerstmann-straussler disease 33.1 PRNP MSMB APP
3 akinetic mutism 30.8 PRNP MAPT ENO2
4 creutzfeldt-jakob disease 30.4 SPRN SERPINA3 RPSA PRNP PRND MSMB
5 leukoencephalopathy, hereditary diffuse, with spheroids 30.4 PRNP MAPT APP
6 aphasia 30.2 PRNP MAPT APP
7 dementia, lewy body 29.8 PRNP MAPT APP
8 amyotrophic lateral sclerosis 1 29.7 SOD2 PRNP MAPT MAP2 APP
9 central nervous system disease 29.6 PRNP MAPT IL1B APP
10 scrapie 29.5 SPRN RPSA PRNP PRND MSMB MAP2
11 parkinson disease, late-onset 29.4 SOD2 MAPT CAT APP
12 nervous system disease 29.3 PRNP MAPT IL1B ENO2 APP
13 cerebral amyloid angiopathy, cst3-related 29.3 SERPINA3 PRNP MAPT APP
14 vascular dementia 29.1 SERPINA3 MAPT APP
15 alzheimer disease 28.5 SERPINA3 PRNP MAPT MAP2 IL1B CAT
16 genetic prion diseases 12.5
17 inherited prion disease 12.5
18 familial alzheimer-like prion disease 12.2
19 huntington disease-like 1 12.1
20 fatal familial insomnia 11.8
21 kuru 11.7
22 spongiform encephalopathy with neuropsychiatric features 11.7
23 variably protease-sensitive prionopathy 11.6
24 gerstmann syndrome 11.5
25 nasopharyngeal carcinoma 2 11.2
26 nasopharyngeal carcinoma 11.2
27 ciliary dyskinesia, primary, 26 11.2
28 ciliary dyskinesia, primary, 27 11.2
29 encephalopathy 11.0
30 papillary tumor of the pineal region 10.6 MAP2 ENO2
31 cerebellum cancer 10.6 MAP2 ENO2
32 ataxia and polyneuropathy, adult-onset 10.5
33 toxic optic neuropathy 10.5 IL1B CAT
34 myoclonus 10.4
35 rabies 10.4
36 neuroblastoma 1 10.4
37 dementia 10.4
38 trypanosomiasis 10.4
39 testicular cancer 10.4
40 listeriosis 10.3
41 huntington disease 10.3
42 autoimmune disease 10.3
43 cauda equina neoplasm 10.3 HSF4 ENO2
44 amyloidosis 10.3
45 cervical adenitis 10.2 IL1B HSF4
46 mutism 10.2
47 erysipelas 10.2 SOD2 CAT
48 encephalomalacia 10.2
49 encephalitis 10.2
50 dysautonomia 10.2

Graphical network of the top 20 diseases related to Prion Disease:



Diseases related to Prion Disease

Symptoms & Phenotypes for Prion Disease

MGI Mouse Phenotypes related to Prion Disease:

46
# Description MGI Source Accession Score Top Affiliating Genes
1 growth/size/body region MP:0005378 10.11 ADAM10 APP ENO2 IL1B MAP2 MAPT
2 hematopoietic system MP:0005397 10.02 ADAM10 APP CR2 FPR2 IL1B MAPT
3 mortality/aging MP:0010768 9.97 ADAM10 APP CAT CR2 FPR2 IL1B
4 immune system MP:0005387 9.96 ADAM10 APP CR2 FPR2 IL1B MAPT
5 neoplasm MP:0002006 9.43 CAT FPR2 IL1B MAPT MSMB SOD2
6 nervous system MP:0003631 9.36 ADAM10 APP ENO2 IL1B MAP2 MAPT

Drugs & Therapeutics for Prion Disease

Drugs for Prion Disease (from DrugBank, HMDB, Dgidb, PharmGKB, IUPHAR, NovoSeek, BitterDB):

(show all 31)
# Name Status Phase Clinical Trials Cas Number PubChem Id
1
Glycerol Approved, Investigational Phase 2, Phase 3 56-81-5 753
2
Coal tar Approved Phase 2 8007-45-2
3
Quinacrine Investigational Phase 2 83-89-6 237
4 Anti-Infective Agents Phase 2
5 Anthelmintics Phase 2
6 Antiparasitic Agents Phase 2
7 Antimalarials Phase 2
8 Antiprotozoal Agents Phase 2
9 insulin Phase 1, Phase 2
10 Insulin, Globin Zinc Phase 1, Phase 2
11 Liver Extracts Phase 1, Phase 2
12 Bifidobacterium Phase 2
13
Prednisolone phosphate Approved, Vet_approved Phase 1 302-25-0
14
Methylprednisolone Approved, Vet_approved Phase 1 83-43-2 6741
15
Methylprednisolone hemisuccinate Approved Phase 1 2921-57-5
16
Prednisolone Approved, Vet_approved Phase 1 50-24-8 5755
17
Prednisolone hemisuccinate Experimental Phase 1 2920-86-7
18 Prednisolone acetate Phase 1
19 Thymoglobulin Phase 1
20 Antilymphocyte Serum Phase 1
21 Methylprednisolone Acetate Phase 1
22 Anesthetics Phase 1
23 Cyclosporins Phase 1
24
Thrombin Approved, Investigational
25 Hematinics
26 Epoetin alfa 113427-24-0
27 Antibodies
28 Immunologic Factors
29 Immunoglobulins
30 Hemostatics
31 Coagulants

Interventional clinical trials:

(show all 15)
# Name Status NCT ID Phase Drugs
1 A Randomized Controlled Trial of the Safety and Efficacy of Fecal Microbiota Transplantation in a Population With Bipolar Disorder Recruiting NCT03279224 Phase 2, Phase 3
2 Novel Therapeutics For Prion Diseases: A Randomized, Double-blinded, Placebo-controlled Study of the Efficacy of Quinacrine in the Treatment of Sporadic Creutzfeldt-Jakob Disease Completed NCT00183092 Phase 2 Quinacrine;Placebo
3 Bovine Colostrum for Patients With Non Alcoholic Fatty Liver Disease Completed NCT01016418 Phase 1, Phase 2
4 FDDNP-PET Imaging in Persons at Risk for Chronic Traumatic Encephalopathy Active, not recruiting NCT02003183 Phase 2
5 The Safety and Effectiveness of Probiotic Supplementation on Bipolar Depression: a Proof of Concept Randomized Controlled Trial Terminated NCT02155972 Phase 2
6 Phase I Serum-Free Cultured Thymus Transplantation in DiGeorge Anomaly, IND9836 Terminated NCT00849888 Phase 1
7 PRION-1: Quinacrine for Human Prion Disease. A Partially Randomized Patient Preference Trial to Evaluate the Activity and Safety of Quinacrine in Human Prion Disease Completed NCT00104663 Quinacrine
8 CardioCel Tri-leaflet Repair Study; a Prospective, Non-randomised, Single Arm, Multi-centre Clinical Investigation Completed NCT02629328
9 A Prospective, Immunogenicity Surveillance Registry (PRIMS) to Estimate the Incidence of Erythropoietin Antibody-Mediated Pure Red Cell Aplasia Among Subjects With Chronic Renal Failure and Subcutaneous Exposure to Recombinant Erythropoietin Products Completed NCT00391287
10 Vascular Post Market Review Completed NCT02681341
11 The Clinical Utility of the Congo-Red Dot Test for Diagnosis and Early Prediction of Preeclampsia During Pregnancy Completed NCT02455544
12 Enhanced CJD Surveillance in the Older Population Recruiting NCT02629640
13 The Canadian Depression Research and Intervention Network (CDRIN) Maritimes Registry: Reliable Assessment to Enable Research and Improve Clinical Care Recruiting NCT02443636
14 Therapeutic Antibodies Against Prion Diseases From PRNP Mutation Carriers Active, not recruiting NCT02837705
15 The Role of the Coagulation Pathway at the Synapse in Prion Diseases Not yet recruiting NCT02480725

Search NIH Clinical Center for Prion Disease

Cochrane evidence based reviews: prion diseases

Genetic Tests for Prion Disease

Anatomical Context for Prion Disease

MalaCards organs/tissues related to Prion Disease:

41
Brain, Testes, Cortex, Spleen, Liver, Bone, T Cells

Publications for Prion Disease

Articles related to Prion Disease:

(show top 50) (show all 5868)
# Title Authors PMID Year
1
A novel protective prion protein variant that colocalizes with kuru exposure. 9 38 71
19923577 2009
2
Prion disease genetics. 9 38 71
16391566 2006
3
Complete sequence data support lack of balancing selection on PRNP in a natural Chinese population. 38 71
16565881 2006
4
Association of sporadic Creutzfeldt-Jakob disease with homozygous genotypes at PRNP codons 129 and 219 in the Korean population. 38 71
16217673 2005
5
Human prion protein with valine 129 prevents expression of variant CJD phenotype. 38 71
15539564 2004
6
Fatal familial insomnia and the widening spectrum of prion diseases. 38 71
8137139 1993
7
Presymptomatic detection or exclusion of prion protein gene defects in families with inherited prion diseases. 38 71
1684089 1991
8
Homozygous prion protein genotype predisposes to sporadic Creutzfeldt-Jakob disease. 38 71
1677164 1991
9
Upregulation of miRNA hsa-miR-342-3p in experimental and idiopathic prion disease. 38 88
19712440 2009
10
The prion gene is associated with human long-term memory. 71
15987701 2005
11
Polymorphisms in the prion protein gene and in the doppel gene increase susceptibility for Creutzfeldt-Jakob disease. 71
14970845 2004
12
Distribution of codon 129 genotype in human growth hormone-treated CJD patients in France and the UK. 71
12867116 2003
13
PRNP Val129 homozygosity increases risk for early-onset Alzheimer's disease. 71
12601712 2003
14
Distribution of the M129V polymorphism of the prion protein gene in a Turkish population suggests a high risk for Creutzfeldt-Jakob disease. 71
11840201 2001
15
Biochemical and structural studies of the prion protein polymorphism. 71
11749972 2001
16
Increased incidence of sporadic Creutzfeldt-Jakob disease on the island of Crete associated with a high rate of PRNP 129-methionine homozygosity in the local population. 71
11506406 2001
17
Sporadic Creutzfeldt-Jakob disease in a young Dutch valine homozygote: atypical molecular phenotype. 71
11506411 2001
18
The genetics of prions--a contradiction in terms? 71
10437852 1999
19
Phenotype-genotype studies in kuru: implications for new variant Creutzfeldt-Jakob disease. 71
9789072 1998
20
Prion protein NMR structure and familial human spongiform encephalopathies. 71
9751723 1998
21
Genotype at codon 129 and susceptibility to Creutzfeldt-Jakob disease. 71
9643750 1998
22
Fatal familial insomnia and familial Creutzfeldt-Jakob disease: different prion proteins determined by a DNA polymorphism. 71
7908444 1994
23
Creutzfeldt-Jakob disease cosegregates with the codon 178Asn PRNP mutation in families of European origin. 71
1353341 1992
24
CJD discrepancy. 71
1682813 1991
25
Codon 129 changes in the prion protein gene in Caucasians. 71
2378641 1990
26
A codon 129 polymorphism in the PRIP gene. 71
1971924 1990
27
Pro----leu change at position 102 of prion protein is the most common but not the sole mutation related to Gerstmann-Sträussler syndrome. 71
2783132 1989
28
Mutant prion protein expression is associated with an alteration of the Rab GDP dissociation inhibitor alpha (GDI)/Rab11 pathway. 9 38
19996123 2010
29
Changes of tau profiles in brains of the hamsters infected with scrapie strains 263 K or 139 A possibly associated with the alteration of phosphate kinases. 9 38
20356412 2010
30
Structure of the prion protein and its gene: an analysis using bioinformatics and computer simulation. 9 38
20158453 2010
31
Involvement of Dab1 in APP processing and beta-amyloid deposition in sporadic Creutzfeldt-Jakob patients. 9 38
19853035 2010
32
Genetic analysis of the SPRN gene in ruminants reveals polymorphisms in the alanine-rich segment of shadoo protein. 9 38
19515828 2009
33
Prions: protein aggregation and infectious diseases. 9 38
19789378 2009
34
Prion protein oligomers in Creutzfeldt-Jakob disease detected by gel-filtration centrifuge columns. 9 38
19389076 2009
35
Loss of anti-Bax function in Gerstmann-Sträussler-Scheinker syndrome-associated prion protein mutants. 9 38
19680558 2009
36
Spontaneous generation of prion infectivity in fatal familial insomnia knockin mice. 9 38
19709627 2009
37
Prion protein (PrP) knock-out mice show altered iron metabolism: a functional role for PrP in iron uptake and transport. 9 38
19568430 2009
38
[Stable inhibition of human prion protein through a retrovirus-based RNAi system]. 9 38
19835143 2009
39
[Alternations of tau protein and its phosphorylated profiles in the experimental hamsters infected by scrapie agents 263K and 139A]. 9 38
19634763 2009
40
An antibody to the aggregated synthetic prion protein peptide (PrP106-126) selectively recognizes disease-associated prion protein (PrP) from human brain specimens. 9 38
18507665 2009
41
Early onset prion disease from octarepeat expansion correlates with copper binding properties. 9 38
19381258 2009
42
Duplex high-throughput flow cytometry screen identifies two novel formylpeptide receptor family probes. 9 38
18785269 2009
43
Production and characterization of a panel of monoclonal antibodies against native human cellular prion protein. 9 38
19132894 2009
44
Phenotypic heterogeneity and genetic modifiers in prion disease caused by a Pro102Leu mutation in the PRNP gene. 9 38
19092795 2009
45
Generating antibodies against the native form of the human prion protein (hPrP) in wild-type animals: a comparison between DNA and protein immunizations. 9 38
19027745 2009
46
Genetic risk factors for variant Creutzfeldt-Jakob disease: a genome-wide association study. 9 38
19081515 2009
47
Detection and characterization of proteinase K-sensitive disease-related prion protein with thermolysin. 9 38
18684106 2008
48
PRNP mutations in a series of apparently sporadic neurodegenerative dementias in China. 9 38
18425766 2008
49
Lack of TAR-DNA binding protein-43 (TDP-43) pathology in human prion diseases. 9 38
18657254 2008
50
Inter-oligomer interactions of the human prion protein are modulated by the polymorphism at codon 129. 9 38
18597782 2008

Variations for Prion Disease

ClinVar genetic disease variations for Prion Disease:

6 (show top 50) (show all 61)
# Gene Variation Type Significance SNP ID GRCh37 Pos GRCh38 Pos
1 PRNP NM_000311.4(PRNP) NT expansion Pathogenic rs193922906 20:4680026-4680049 20:4699380-4699403
2 PRNP NM_000311.5(PRNP): c.305C> T (p.Pro102Leu) single nucleotide variant Pathogenic rs74315401 20:4680171-4680171 20:4699525-4699525
3 PRNP NM_000311.5(PRNP): c.350C> T (p.Ala117Val) single nucleotide variant Pathogenic rs74315402 20:4680216-4680216 20:4699570-4699570
4 PRNP NM_000311.5(PRNP): c.598G> A (p.Glu200Lys) single nucleotide variant Pathogenic rs28933385 20:4680464-4680464 20:4699818-4699818
5 PRNP NM_000311.5(PRNP): c.532G> A (p.Asp178Asn) single nucleotide variant Pathogenic rs74315403 20:4680398-4680398 20:4699752-4699752
6 PRNP NM_000311.4(PRNP): c.593T> C (p.Phe198Ser) single nucleotide variant Pathogenic rs74315405 20:4680459-4680459 20:4699813-4699813
7 PRNP NM_000311.5(PRNP): c.650A> G (p.Gln217Arg) single nucleotide variant Pathogenic rs74315406 20:4680516-4680516 20:4699870-4699870
8 PRNP NM_000311.5(PRNP): c.628G> A (p.Val210Ile) single nucleotide variant Pathogenic rs74315407 20:4680494-4680494 20:4699848-4699848
9 PRNP NM_000311.5(PRNP): c.314C> T (p.Pro105Leu) single nucleotide variant Pathogenic rs11538758 20:4680180-4680180 20:4699534-4699534
10 PRNP NM_000311.5(PRNP): c.547A> G (p.Thr183Ala) single nucleotide variant Pathogenic rs74315411 20:4680413-4680413 20:4699767-4699767
11 PRNP NM_000311.5(PRNP): c.560A> G (p.His187Arg) single nucleotide variant Pathogenic rs74315413 20:4680426-4680426 20:4699780-4699780
12 PRNP NM_000311.5(PRNP): c.313C> A (p.Pro105Thr) single nucleotide variant Pathogenic rs74315414 20:4680179-4680179 20:4699533-4699533
13 PRNP NM_000311.5(PRNP): c.313C> T (p.Pro105Ser) single nucleotide variant Pathogenic rs74315414 20:4680179-4680179 20:4699533-4699533
14 PRNP NM_000311.5(PRNP): c.435T> G (p.Tyr145Ter) single nucleotide variant Pathogenic rs80356710 20:4680301-4680301 20:4699655-4699655
15 PRNP NM_000311.5(PRNP): c.478C> T (p.Gln160Ter) single nucleotide variant Pathogenic rs80356711 20:4680344-4680344 20:4699698-4699698
16 PRNP NM_000311.5(PRNP): c.538G> A (p.Val180Ile) single nucleotide variant Pathogenic/Likely pathogenic rs74315408 20:4680404-4680404 20:4699758-4699758
17 PRNP NM_000311.5(PRNP): c.695T> G (p.Met232Arg) single nucleotide variant Conflicting interpretations of pathogenicity rs74315409 20:4680561-4680561 20:4699915-4699915
18 PRNP NM_000311.5(PRNP): c.623G> A (p.Arg208His) single nucleotide variant Conflicting interpretations of pathogenicity rs74315412 20:4680489-4680489 20:4699843-4699843
19 PRNP NM_000311.5(PRNP): c.*994C> T single nucleotide variant Uncertain significance rs886056746 20:4681622-4681622 20:4700976-4700976
20 PRNP NM_000311.5(PRNP): c.*1588C> T single nucleotide variant Uncertain significance rs886056750 20:4682216-4682216 20:4701570-4701570
21 PRNP NM_000311.5(PRNP): c.-22C> G single nucleotide variant Uncertain significance rs886056741 20:4667147-4667147 20:4686501-4686501
22 PRNP NM_000311.5(PRNP): c.*1035T> G single nucleotide variant Uncertain significance rs886056747 20:4681663-4681663 20:4701017-4701017
23 PRNP NM_000311.5(PRNP): c.*216G> A single nucleotide variant Uncertain significance rs748532463 20:4680844-4680844 20:4700198-4700198
24 PRNP NM_000311.5(PRNP): c.*407T> G single nucleotide variant Uncertain significance rs886056745 20:4681035-4681035 20:4700389-4700389
25 PRNP NM_000311.4(PRNP): c.-211G> A single nucleotide variant Uncertain significance rs886056739 20:4666958-4666958 20:4686312-4686312
26 PRNP NM_000311.5(PRNP): c.-21G> T single nucleotide variant Uncertain significance rs886056742 20:4667148-4667148 20:4686502-4686502
27 PRNP NM_000311.5(PRNP): c.*358C> A single nucleotide variant Uncertain significance rs886056744 20:4680986-4680986 20:4700340-4700340
28 PRNP NM_000311.5(PRNP): c.159C> T (p.Gly53=) single nucleotide variant Uncertain significance rs776188950 20:4680025-4680025 20:4699379-4699379
29 PRNP NM_000311.4(PRNP): c.-310T> A single nucleotide variant Uncertain significance rs765471807 20:4666859-4666859 20:4686213-4686213
30 PRNP NM_000311.5(PRNP): c.*874C> T single nucleotide variant Uncertain significance rs760516358 20:4681502-4681502 20:4700856-4700856
31 PRNP NM_000311.5(PRNP): c.*1193G> A single nucleotide variant Uncertain significance rs886056748 20:4681821-4681821 20:4701175-4701175
32 PRNP NM_000311.4(PRNP): c.-206C> G single nucleotide variant Uncertain significance rs886056740 20:4666963-4666963 20:4686317-4686317
33 PRNP NM_000311.5(PRNP): c.*1466G> C single nucleotide variant Uncertain significance rs886056749 20:4682094-4682094 20:4701448-4701448
34 PRNP NM_000311.5(PRNP): c.204T> C (p.Pro68=) single nucleotide variant Likely benign rs532493114 20:4680070-4680070 20:4699424-4699424
35 PRNP NM_000311.5(PRNP): c.424G> A (p.Gly142Ser) single nucleotide variant Likely benign rs150351644 20:4680290-4680290 20:4699644-4699644
36 PRNP NM_000311.5(PRNP): c.*70G> A single nucleotide variant Likely benign rs116970629 20:4680698-4680698 20:4700052-4700052
37 PRNP NM_000311.5(PRNP): c.*98_*100TCT[1] short repeat Likely benign rs570683075 20:4680729-4680731 20:4700083-4700085
38 PRNP NM_000311.5(PRNP): c.*115G> A single nucleotide variant Likely benign rs746943389 20:4680743-4680743 20:4700097-4700097
39 PRNP NM_000311.5(PRNP): c.*206A> G single nucleotide variant Likely benign rs41279420 20:4680834-4680834 20:4700188-4700188
40 PRNP NM_000311.5(PRNP): c.*4A> T single nucleotide variant Likely benign rs11087654 20:4680632-4680632 20:4699986-4699986
41 PRNP NM_000311.5(PRNP): c.*592T> C single nucleotide variant Likely benign rs138751953 20:4681220-4681220 20:4700574-4700574
42 PRNP NM_000311.5(PRNP): c.*800C> T single nucleotide variant Likely benign rs111321071 20:4681428-4681428 20:4700782-4700782
43 PRNP NM_000311.5(PRNP): c.160G> A (p.Gly54Ser) single nucleotide variant Likely benign rs763524380 20:4680026-4680026 20:4699380-4699380
44 PRNP NM_000311.5(PRNP): c.*672C> G single nucleotide variant Likely benign rs183570240 20:4681300-4681300 20:4700654-4700654
45 PRNP NM_000311.5(PRNP): c.*1281A> G single nucleotide variant Likely benign rs540167431 20:4681909-4681909 20:4701263-4701263
46 PRNP NM_000311.5(PRNP): c.*1412T> A single nucleotide variant Likely benign rs150850205 20:4682040-4682040 20:4701394-4701394
47 PRNP NM_000311.3(PRNP): c.204_227del24 (p.Pro84_Gln91del) short repeat Likely benign rs193922906 20:4680070-4680093 20:4699424-4699447
48 PRNP NM_000311.5(PRNP): c.*936C> T single nucleotide variant Likely benign rs76116805 20:4681564-4681564 20:4700918-4700918
49 PRNP NM_000311.5(PRNP): c.-18C> T single nucleotide variant Likely benign rs537449340 20:4667151-4667151 20:4686505-4686505
50 PRNP NM_000311.5(PRNP): c.*1063G> A single nucleotide variant Likely benign rs58499385 20:4681691-4681691 20:4701045-4701045

Expression for Prion Disease

Search GEO for disease gene expression data for Prion Disease.

Pathways for Prion Disease

Pathways related to Prion Disease according to KEGG:

37
# Name Kegg Source Accession
1 Prion diseases hsa05020

GO Terms for Prion Disease

Cellular components related to Prion Disease according to GeneCards Suite gene sharing:

# Name GO ID Score Top Affiliating Genes
1 extracellular exosome GO:0070062 9.65 SOD2 SERPINA3 RPSA PRNP IL1B ENO2
2 neuronal cell body GO:0043025 9.46 MAPT MAP2 ENO2 ADAM10
3 nuclear periphery GO:0034399 9.4 MAPT MAP2
4 anchored component of external side of plasma membrane GO:0031362 9.37 PRNP PRND
5 intracellular GO:0005622 9.02 RPSA
6 main axon GO:0044304 8.8 MAPT MAP2 APP
7 plasma membrane GO:0005886 10.03 SPRN SCN2A RPSA PRNP PRND MAPT

Biological processes related to Prion Disease according to GeneCards Suite gene sharing:

(show all 18)
# Name GO ID Score Top Affiliating Genes
1 neuron projection development GO:0031175 9.75 MAPT MAP2 APP
2 response to oxidative stress GO:0006979 9.74 PRNP CAT APP
3 microglial cell activation GO:0001774 9.56 MAPT FPR2
4 regulation of peptidyl-tyrosine phosphorylation GO:0050730 9.55 PRNP APP
5 positive regulation of superoxide anion generation GO:0032930 9.54 MAPT FPR2
6 central nervous system neuron development GO:0021954 9.52 MAPT MAP2
7 complement receptor mediated signaling pathway GO:0002430 9.51 FPR2 CR2
8 regulation of microtubule polymerization GO:0031113 9.49 MAPT MAP2
9 neuron projection maintenance GO:1990535 9.48 PRNP APP
10 negative regulation of long-term synaptic potentiation GO:1900272 9.46 PRNP APP
11 amyloid fibril formation GO:1990000 9.43 MAPT APP
12 cellular response to amyloid-beta GO:1904646 9.43 PRNP FPR2 APP
13 modulation of age-related behavioral decline GO:0090647 9.4 PRNP APP
14 response to lead ion GO:0010288 9.33 MAPT CAT APP
15 cellular copper ion homeostasis GO:0006878 9.13 PRNP PRND APP
16 response to ozone GO:0010193 9.07 CAT
17 response to L-ascorbic acid GO:0033591 9.02 CAT
18 astrocyte activation GO:0048143 8.8 MAPT FPR2 APP

Molecular functions related to Prion Disease according to GeneCards Suite gene sharing:

# Name GO ID Score Top Affiliating Genes
1 tubulin binding GO:0015631 8.8 PRNP MAPT MAP2

Sources for Prion Disease

3 CDC
7 CNVD
9 Cosmic
10 dbSNP
11 DGIdb
17 EFO
18 ExPASy
19 FMA
28 GO
29 GTR
30 HGMD
31 HMDB
32 HPO
33 ICD10
34 ICD10 via Orphanet
35 ICD9CM
36 IUPHAR
37 KEGG
38 LifeMap
40 LOVD
42 MedGen
44 MeSH
45 MESH via Orphanet
46 MGI
49 NCI
50 NCIt
51 NDF-RT
54 NINDS
55 Novoseek
57 OMIM
58 OMIM via Orphanet
62 PubMed
64 QIAGEN
69 SNOMED-CT via HPO
70 TGDB
71 Tocris
72 UMLS
73 UMLS via Orphanet
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