About: Prion

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An Entity of Type : wikibase:Item, within Data Space : wikidata.demo.openlinksw.com associated with source document(s)

journal

Attributes	Values
rdf:type	Item
description	journal (en) revista científica (es) ساینَسی رِسالہٕ (ks) revue scientifique (fr) rivista scientifica (it) науковий журнал (uk) wissenschaftliche Fachzeitschrift (de) wetenschappelijk tijdschrift van Landes Bioscience (nl)
language of work or name	wds:Q26842757-920F72F8-8B47-4AAA-B09C-C74FC1299CEE
language of work or name	English
OpenCitations bibliographic resource ID	wds:Q26842757-58271D66-A08E-432D-9FC1-9822CE6F3C53
Scilit journal ID	wds:Q26842757-DAE92487-782F-4E07-9403-5D9101F98814
Crossref journal ID	wds:Q26842757-1325B781-87B7-41A6-ACBF-EBC45287A178
OpenCitations bibliographic resource ID	https://w3id.org/oc/corpus/br/82950
OpenCitations bibliographic resource ID	82950
Scilit journal ID	1289307
Crossref journal ID	85917
rdfs:label	Prion (en) Prion (nl) Prion (es) Prion (it) Prion (ast)
skos:prefLabel	Prion (en) Prion (nl) Prion (es) Prion (it) Prion (ast)
name	Prion (en) Prion (nl) Prion (es) Prion (it) Prion (ast)
title	wds:Q26842757-6b0ecaa1-4f8e-c875-19b8-1a0159957327
title	Prion (en)
ERA Journal ID	wds:Q26842757-4C24F0BC-3383-4A02-AEBA-84F624D5992A
Directory of Open Access Journals ID	wds:Q26842757-232DA7DE-36AD-4712-BCE6-C8BDC845726B wds:Q26842757-67154A9E-8094-4D0B-B4D2-E4F513AE5697
ERA Journal ID	201399
Directory of Open Access Journals ID	1933-6896 1933-690X
NLM Unique ID	wds:Q26842757-263D4BF9-FFFA-419F-A63C-B3F66FAC30A4
HAL journal ID	wds:Q26842757-6142E953-A046-4120-923F-F3D403C575EF
NLM Unique ID	101472305
HAL journal ID	41371
instance of	wds:Q26842757-4CEC4093-AA0E-46C5-89C0-6C77C42CBA85 wds:Q26842757-8C873619-ADE5-4E6B-8B94-A08CBABEAFF8 wds:Q26842757-A54EB921-5CFD-4679-9D0F-1BC423EAF88F wds:Q26842757-ec8f1a0c-44e7-28f5-ae0f-0d1e679ea88c
instance of	scientific journal scientific journal hybrid open access journal open-access journal
publisher	wds:Q26842757-37671F50-2953-4315-9FBB-72388506D9AC
publisher	Landes Bioscience
OpenAlex ID	wds:Q26842757-4BAD66AB-586C-4A11-A721-D9EDFDECCEFF
country of origin	wds:Q26842757-1468EE81-0A65-4B97-8661-0785B8837127
official website	wds:Q26842757-176e05b5-4885-618e-fb43-12a000323634 wds:Q26842757-A3BFD355-90E6-436D-89BE-825031D41272 wds:Q26842757-AA44F429-6329-4B52-BE34-713452899D1B
OpenAlex ID	V4594078
country of origin	United States of America
official website	http://www.tandfonline.com/toc/kprn20/current http://landesbioscience.com/journals/prion https://www.tandfonline.com/toc/kprn20/current
Scopus source ID	wds:Q26842757-60D6FC98-E201-46D3-983C-E28756003454
ISSN	wds:Q26842757-3B1955AC-1C6C-4614-83B6-DF8B912834F9 wds:Q26842757-E89F10EE-3374-47C0-AE6D-2A7D0CBE04BA
ISSN-L	wds:Q26842757-2DFEF652-2413-4073-854D-B1271ECE8F26
indexed in bibliographic review	wds:Q26842757-5102CD07-74B4-4FEA-A530-A2170462E1E4 wds:Q26842757-DE6377B6-D846-4B90-9F55-D0958E7195BB
ISSN	urn:ISSN:1933-6896 urn:ISSN:1933-690X
ISSN-L	http://issn.org/resource/ISSN/1933-6896
Scopus source ID	17100154713
ISSN	1933-6896 1933-690X
ISSN-L	1933-6896
indexed in bibliographic review	Scopus Science Citation Index Expanded
is about of	https://www.wikidata.org/wiki/Special:EntityData/Q26842757
is published in of	Prion transmission: prion excretion and occurrence in the environment Not on the menu: autophagy-independent clearance of prions Heligmosomoides polygyrus antigens inhibit the intrinsic pathway of apoptosis by overexpression of survivin and Bcl-2 protein in CD4 T cells Life cycle of cytosolic prions Prions on the run: How extracellular vesicles serve as delivery vehicles for self-templating protein aggregates Exploring the zoonotic potential of animal prion diseases: in vivo and in vitro approaches. Generation of antisera to purified prions in lipid rafts Slow spontaneous α-to-β structural conversion in a non-denaturing neutral condition reveals the intrinsically disordered property of the disulfide-reduced recombinant mouse prion protein Amyloid-β induced signaling by cellular prion protein and Fyn kinase in Alzheimer disease Dynamic properties of pH-dependent structural organization of the amyloidogenic beta-protein (1-40). Interdependence of amyloid formation in yeast: implications for polyglutamine disorders and biological functions Protein aggregation and polyasparagine-mediated cellular toxicity in Saccharomyces cerevisiae Prion-dependent lethality of sup45 mutants in Saccharomyces cerevisiae Prion formation by a yeast GLFG nucleoporin. A structural overview of the vertebrate prion proteins Yeast prions: evolution of the prion concept Prion proteostasis: Hsp104 meets its supporting cast S-nitrosylation of Cdk5: potential implications in amyloid-β-related neurotoxicity in Alzheimer disease Is tau ready for admission to the prion club?

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