The mechanism of toxicity in HET-S/HET-s prion incompatibility. - Wikidata - awgldk - TriplyDB

The mechanism of toxicity in HET-S/HET-s prion incompatibility.

The mechanism of toxicity in HET-S/HET-s prion incompatibility.

http://www.wikidata.org/entity/Q34539592

about

As a toxin dies a prion comes to life: A tentative natural history of the [Het-s] prion Prion-like polymerization as a signaling mechanism Asparagine repeats in Plasmodium falciparum proteins: good for nothing?Inter-species cross-seeding: stability and assembly of rat-human amylin aggregates Contribution of specific residues of the β-solenoid fold to HET-s prion function, amyloid structure and stability.Prion-promoted phosphorylation of heterologous amyloid is coupled with ubiquitin-proteasome system inhibition and toxicity.Heterogeneous seeding of HET-s(218-289) and the mutability of prion structures.Prion-like polymerization underlies signal transduction in antiviral immune defense and inflammasome activation.Functional amyloidogenesis and cytotoxicity-insights into biology and pathology.Signal transduction by a fungal NOD-like receptor based on propagation of a prion amyloid fold Pernicious pathogens or expedient elements of inheritance: the significance of yeast prions.Identification of a novel cell death-inducing domain reveals that fungal amyloid-controlled programmed cell death is related to necroptosis.Virus-mediated suppression of host non-self recognition facilitates horizontal transmission of heterologous viruses.Nonpathogenic prions.Overlapping Podospora anserina Transcriptional Responses to Bacterial and Fungal Non Self Indicate a Multilayered Innate Immune Response.The transcriptional response to nonself in the fungus Podospora anserina A Meiotic Drive Element in the Maize Pathogen Fusarium verticillioides Is Located Within a 102 kb Region of Chromosome V.Diversity and variability of NOD-like receptors in fungi.Prion-Like Polymerization in Immunity and Inflammation.Key Points Concerning Amyloid Infectivity and Prion-Like Neuronal Invasion The HET-S/s Prion Motif in the Control of Programmed Cell Death.The Three-Dimensional Structures of Amyloids.The activities of amyloids from a structural perspective.Protein aggregation, misfolding and consequential human neurodegenerative diseases.Diversity of Amyloid Motifs in NLR Signaling in Fungi.Intrinsically Disordered Proteins Drive Emergence and Inheritance of Biological Traits.Two genomes are better than one: history, genetics, and biotechnological applications of fungal heterokaryons.On the evolutionary trajectories of signal-transducing amyloids in fungi and beyond.Theme and variations: evolutionary diversification of the HET-s functional amyloid motif.Regulated Forms of Cell Death in Fungi When amyloids become prions The conformation of the prion domain of Sup35p in isolation and in the full-length protein.Wild type and mutants of the HET-s(218-289) prion show different flexibility at fibrillar ends: a simulation study.Structure insight of GSDMD reveals the basis of GSDMD autoinhibition in cell pyroptosis.Functional amyloids: interrelationship with other amyloids and therapeutic assessment to treat neurodegenerative diseases.Veni, vidi, vici: the success of wtf meiotic drivers in fission yeast.PAIN with and without PAR: variants for third-spin assisted heteronuclear polarization transfer.Genetic Villains: Killer Meiotic Drivers.Protein Co-Aggregation Related to Amyloids: Methods of Investigation, Diversity, and Classification

P2860

Q26825702-7F9B5D8A-6013-4605-9BB2-66476512B614 Q26995776-B5E44EC1-0236-4C03-972D-49690C4D50AC Q27011896-63086F84-C0B7-41FA-8341-1171CEEB5607 Q28538620-18948D41-6CA5-4ADB-8C1D-40FAEB180242 Q33749018-5A7601DF-9547-4BDF-A304-2AFA3BDDC590 Q34115717-1A820783-D9C7-476D-8588-5BF22D9AA817 Q34307230-723EC056-38BE-4641-8CA6-8AC95C743603 Q34410101-C1A7D2EC-51C0-4A40-BF48-B1BCCBF5EB1B Q34539609-D28D1716-46CA-4CCC-8968-78CD1FAD9866 Q35130900-D4E6C3E0-D6C7-4665-9200-79BE633E2E08 Q35145581-0342EE7E-6139-4736-969F-C95C790FBC96 Q35931840-E1161E9F-1D25-4B2D-B719-3F127073864C Q36320147-3FE1E5F8-AC55-4FF0-995E-ADD13D2F817E Q36799032-56E8DE72-4A84-44E9-8F6E-D7D6D6DF3DFD Q36809324-D576673E-C5AE-4ACE-B91B-220625BE97E7 Q36947234-AD0953B1-2C7C-4DFB-8FED-4BD8D831BE0B Q37163040-E6C323FF-E4FF-47C8-937E-38EB8055F044 Q37178778-C480F328-6058-4CBA-A1AF-21666C47D5E9 Q38791444-3E9F1832-AE7B-4F34-A76C-EDA32AB326D6 Q38826332-8954C75C-C370-4819-A1EA-3E99441A2274 Q38879717-0C3C162B-0B3C-450A-BD17-EA44150306A2 Q38994211-B6BDD642-7FF4-4EA0-B171-D9316B3A8738 Q39004351-AA471592-F41C-428C-8874-3C40B8AB2816 Q39097864-FA6DA4F4-6FF7-4577-87C3-3800DD67C11C Q39240147-E847D1A2-DBB5-4946-B096-AEA950CDAF75 Q39331960-A921B4A3-E6CF-426A-8768-457A3576F88D Q41684974-AF077D15-2AF2-4A50-AADF-731DC0016452 Q41717134-63DF87BE-B372-4760-9F15-405EC53AC4BB Q41921152-CD7A83C3-CFD0-44C1-85A9-779B013550AB Q42065808-A8C7750A-075D-4DD5-9FF3-305B698D36B8 Q42215147-A514AFE2-4715-466E-AEBD-E9E5FB0D93A5 Q43975044-8C3DD573-D4F6-4CF9-A276-2E7FE88FF7ED Q46112510-A26D3ED7-B87A-4E14-9A87-A5CF4FC8A7A1 Q46304262-DD99EAA4-48DF-45E1-9FBA-FCF7C3837370 Q47404503-BD921A94-7E94-4001-94EF-93C6637B67FD Q48043658-0BEFC6C9-962F-43BE-9A11-DEE99DB59C63 Q50872227-D6AD52A8-A906-4126-9E91-642B8E23CDAA Q52729221-69E16860-F884-4981-AFAB-B63B0AF023E9 Q58800414-184208C6-8773-44F1-B167-B7BD5B5BC847

P2860

The mechanism of toxicity in HET-S/HET-s prion incompatibility.

http://www.wikidata.org/entity/Q34539592

description

2012 nî lūn-bûn

@nan

2012 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած

@hyw

2012 թվականի դեկտեմբերին հրատարակված գիտական հոդված

@hy

2012年の論文

@ja

2012年論文

@yue

2012年論文

@zh-hant

2012年論文

@zh-hk

2012年論文

@zh-mo

2012年論文

@zh-tw

2012年论文

@wuu

name

The mechanism of toxicity in HET-S/HET-s prion incompatibility.

@ast

The mechanism of toxicity in HET-S/HET-s prion incompatibility.

@en

The mechanism of toxicity in HET-S/HET-s prion incompatibility.

@nl

type

label

The mechanism of toxicity in HET-S/HET-s prion incompatibility.

@ast

The mechanism of toxicity in HET-S/HET-s prion incompatibility.

@en

The mechanism of toxicity in HET-S/HET-s prion incompatibility.

@nl

prefLabel

The mechanism of toxicity in HET-S/HET-s prion incompatibility.

@ast

The mechanism of toxicity in HET-S/HET-s prion incompatibility.

@en

The mechanism of toxicity in HET-S/HET-s prion incompatibility.

@nl

P1433

Q34539592-4F99732A-5E25-4802-BDDB-500C9A1D6D23

P1476

Q34539592-2CE74905-ED8B-4FDC-9CAD-DD43E3536A10

P2093

Q34539592-BC1DD2BE-1B0E-49A3-8FF3-BD4CF1D705B4

Q34539592-DB68C526-B366-4ED1-97DA-59F64D935813

Q34539592-E5E80C3E-3D52-4F43-A353-36CDF682234B

P2860

Q34539592-0028980F-1B75-4DE7-B809-E513A2431B1B

Q34539592-01DFA7B0-49C9-4855-B9F9-746847B2E556

Q34539592-026E816F-BACE-40E1-A787-63A15183B192

Q34539592-065702C7-92E1-4E08-80E6-585DDE71D586

Q34539592-0B44E835-FA2B-4CF2-8772-53237365CF4D

Q34539592-0EA72714-3838-4EE4-8648-5FFBCB9124A2

Q34539592-16E5711B-3154-4583-B633-F7D3BFEA10B2

Q34539592-19710098-8F1F-4AB1-B1C2-16DCC9E79A10

Q34539592-2CBAB3E4-9F2C-444D-BDAB-0026EF0A0B8F

Q34539592-2DF81C82-171C-40AF-B10D-1F3DF682E7CB

P304

Q34539592-C8D1AE86-9DB5-4818-91D5-F40063502464

P31

Q34539592-5552AE8C-3BC2-4E61-9A83-C7F36DB9B437

P356

Q34539592-41604BDD-2FB3-4FC4-9E41-2996625AFF02

P407

Q34539592-B579119F-A2F1-4010-A07B-89BEBF157025

P433

Q34539592-8A7AAAB6-43C7-464C-8BB5-55DDDEB02CB0

P478

Q34539592-00107D18-5B3B-4EB9-9441-D7894437361F

P50

Q34539592-349AE806-1979-4E75-91ED-3CF6E055A4BF

Q34539592-7814E2D8-F070-49EB-9926-6916592D6D8C

Q34539592-C997B7E8-002F-481D-A526-28EC1F89D9B5

Q34539592-E6330525-31EF-4A4A-B869-BB849BFADCFD

P577

Q34539592-51BB7EC9-3A02-476F-B851-C551F534288C

P5875

Q34539592-285663D1-0D67-4ED7-A789-63A5F36651C0

P698

Q34539592-3FD693CE-3351-4BA9-A9BD-05E19A982DBF

P921

Q34539592-7D0BF06C-8B93-4BEC-9923-5D520B012F73

P932

Q34539592-29AF285C-05C3-40A3-BD4F-A4B6B48A06FD

P356

JOURNAL.PBIO.1001451

P1433

P1476

The mechanism of toxicity in HET-S/HET-s prion incompatibility.

@en

P2093

Christian Wasmer

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

Jason Greenwald

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

Roland Riek

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

P2860

Amyloid aggregates of the HET-s prion protein are infectious.

The mechanism of prion inhibition by HET-S

The protein product of the het-s heterokaryon incompatibility gene of the fungus Podospora anserina behaves as a prion analog

ADDA: a domain database with global coverage of the protein universe

Structure of Ustilago maydis killer toxin KP6 alpha-subunit. A multimeric assembly with a central pore

Amyloid fibrils of the HET-s(218-289) prion form a beta solenoid with a triangular hydrophobic core

The structure of a cytolytic alpha-helical toxin pore reveals its assembly mechanism

A common toxin fold mediates microbial attack and plant defense

Atomic-resolution three-dimensional structure of HET-s(218-289) amyloid fibrils by solid-state NMR spectroscopy

Structure of the Aeromonas toxin proaerolysin in its water-soluble and membrane-channel states

P304

e1001451

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

P31

scholarly article

P356

10.1371/JOURNAL.PBIO.1001451

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

P407

P433

12

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

P478

10

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

P50

Carolin Seuring

P577

2012-12-27T00:00:00Z

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

P5875

234089975

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

P698

23300377

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

P921

Prion protein family

P932

3531502

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