LIVIVO - Search results -

Search results

Result 1 - 10 of total 53

Search options

Article ; Online: Human proteins curing yeast prions.

Wu, Songsong / Edskes, Herman K / Wickner, Reed B

Proceedings of the National Academy of Sciences of the United States of America

2023 Volume 120, Issue 45, Page(s) e2314781120

Abstract: Recognition that common human amyloidoses are prion diseases makes the use of ... ...

Abstract	Recognition that common human amyloidoses are prion diseases makes the use of the
MeSH term(s)	Animals ; Humans ; Saccharomyces cerevisiae/genetics ; Saccharomyces cerevisiae/metabolism ; Saccharomyces cerevisiae Proteins/metabolism ; Prions/genetics ; Prions/metabolism ; HSP70 Heat-Shock Proteins/genetics ; HSP70 Heat-Shock Proteins/metabolism ; Mutation ; Amyloid/genetics ; Amyloid/metabolism ; Glutathione Peroxidase/genetics ; Glutathione Peroxidase/metabolism ; Fungal Proteins/metabolism ; Mammals/metabolism ; RNA Splicing Factors/genetics ; Nuclear Proteins/metabolism ; DNA Repair Enzymes/genetics
Chemical Substances	Saccharomyces cerevisiae Proteins ; Prions ; HSP70 Heat-Shock Proteins ; Amyloid ; Glutathione Peroxidase (EC 1.11.1.9) ; Fungal Proteins ; PRPF19 protein, human (EC 6.5.1.-) ; RNA Splicing Factors ; Nuclear Proteins ; DNA Repair Enzymes (EC 6.5.1.-)
Language	English
Publishing date	2023-10-30
Publishing country	United States
Document type	Journal Article
ZDB-ID	209104-5
ISSN	1091-6490 ; 0027-8424
ISSN (online)	1091-6490
ISSN	0027-8424
DOI	10.1073/pnas.2314781120
Database	MEDical Literature Analysis and Retrieval System OnLINE

In stock of ZB MED Cologne/Königswinter

Zs.A 1148: Show issues

Location:
Je nach Verfügbarkeit (siehe Angabe bei Bestand)
bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular
Jg. 1995 - 2021: Lesesall (1.OG)
ab Jg. 2022: Lesesaal (EG)

Order via subito

This service is chargeable due to the Delivery terms set by subito. Orders including an article and supplementary material will be classified as separate orders. In these cases, fees will be demanded for each order.

Details ▾
- See ZB MED holdings
- Order with fees

Article ; Online: Prions are the greatest protein misfolding problem, and yeast has several solutions.

Wickner, Reed B / Edskes, Herman K / Wu, Songsong / Gregg, Kristen

PLoS pathogens

2023 Volume 19, Issue 5, Page(s) e1011333

MeSH term(s)	Saccharomyces cerevisiae/metabolism ; Prions/metabolism ; Protein Folding ; Saccharomyces cerevisiae Proteins/metabolism
Chemical Substances	Prions ; Saccharomyces cerevisiae Proteins
Language	English
Publishing date	2023-05-04
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Intramural
ZDB-ID	2205412-1
ISSN	1553-7374 ; 1553-7374
ISSN (online)	1553-7374
ISSN	1553-7374
DOI	10.1371/journal.ppat.1011333
Database	MEDical Literature Analysis and Retrieval System OnLINE

Order via subito

Article: Anti-Prion Systems Block Prion Transmission, Attenuate Prion Generation, Cure Most Prions as They Arise and Limit Prion-Induced Pathology in

Wickner, Reed B / Edskes, Herman K / Son, Moonil / Wu, Songsong

Biology

2022 Volume 11, Issue 9

Abstract: All variants of the yeast prions [PSI+] and [URE3] are detrimental to their hosts, as shown by the dramatic slowing of growth (or even lethality) of a majority, by the rare occurrence in wild isolates of even the mildest variants and by the absence of ... ...

Abstract	All variants of the yeast prions [PSI+] and [URE3] are detrimental to their hosts, as shown by the dramatic slowing of growth (or even lethality) of a majority, by the rare occurrence in wild isolates of even the mildest variants and by the absence of reproducible benefits of these prions. To deal with the prion problem, the host has evolved an array of anti-prion systems, acting in normal cells (without overproduction or deficiency of any component) to block prion transmission from other cells, to lower the rates of spontaneous prion generation, to cure most prions as they arise and to limit the damage caused by those variants that manage to elude these (necessarily) imperfect defenses. Here we review the properties of prion protein sequence polymorphisms Btn2, Cur1, Hsp104, Upf1,2,3, ribosome-associated chaperones, inositol polyphosphates, Sis1 and Lug1, which are responsible for these anti-prion effects. We recently showed that the combined action of ribosome-associated chaperones, nonsense-mediated decay factors and the Hsp104 disaggregase lower the frequency of [PSI+] appearance as much as 5000-fold. Moreover, while Btn2 and Cur1 are anti-prion factors against [URE3] and an unrelated artificial prion, they promote [PSI+] prion generation and propagation.
Language	English
Publishing date	2022-08-26
Publishing country	Switzerland
Document type	Journal Article ; Review
ZDB-ID	2661517-4
ISSN	2079-7737
ISSN	2079-7737
DOI	10.3390/biology11091266
Database	MEDical Literature Analysis and Retrieval System OnLINE

Order via subito

Article ; Online: Innate immunity to yeast prions: Btn2p and Cur1p curing of the [URE3] prion is prevented by 60S ribosomal protein deficiency or ubiquitin/proteasome system overactivity.

Bezsonov, Evgeny E / Edskes, Herman K / Wickner, Reed B

Genetics

2021 Volume 217, Issue 4

Abstract: URE3] is an amyloid-based prion of Ure2p, a negative regulator of poor nitrogen source catabolism in Saccharomyces cerevisiae. Overproduced Btn2p or its paralog Cur1p, in processes requiring Hsp42, cure the [URE3] prion. Btn2p cures by collecting Ure2p ... ...

Abstract	[URE3] is an amyloid-based prion of Ure2p, a negative regulator of poor nitrogen source catabolism in Saccharomyces cerevisiae. Overproduced Btn2p or its paralog Cur1p, in processes requiring Hsp42, cure the [URE3] prion. Btn2p cures by collecting Ure2p amyloid filaments at one place in the cell. We find that rpl4aΔ, rpl21aΔ, rpl21bΔ, rpl11bΔ, and rpl16bΔ (large ribosomal subunit proteins) or ubr2Δ (ubiquitin ligase targeting Rpn4p, an activator of proteasome genes) reduce curing by overproduced Btn2p or Cur1p. Impaired curing in ubr2Δ or rpl21bΔ is restored by an rpn4Δ mutation. No effect of rps14aΔ or rps30bΔ on curing was observed, indicating that 60S subunit deficiency specifically impairs curing. Levels of Hsp42p, Sis1p, or Btn3p are unchanged in rpl4aΔ, rpl21bΔ, or ubr2Δ mutants. Overproduction of Cur1p or Btn2p was enhanced in rpn4Δ and hsp42Δ mutants, lower in ubr2Δ strains, and restored to above wild-type levels in rpn4Δ ubr2Δ strains. As in the wild-type, Ure2N-GFP colocalizes with Btn2-RFP in rpl4aΔ, rpl21bΔ, or ubr2Δ strains, but not in hsp42Δ. Btn2p/Cur1p overproduction cures [URE3] variants with low seed number, but seed number is not increased in rpl4aΔ, rpl21bΔ or ubr2Δ mutants. Knockouts of genes required for the protein sorting function of Btn2p did not affect curing of [URE3], nor did inactivation of the Hsp104 prion-curing activity. Overactivity of the ubiquitin/proteasome system, resulting from 60S subunit deficiency or ubr2Δ, may impair Cur1p and Btn2p curing of [URE3] by degrading Cur1p, Btn2p or another component of these curing systems.
MeSH term(s)	Amino Acid Transport Systems/genetics ; Amino Acid Transport Systems/metabolism ; Glutathione Peroxidase/genetics ; Glutathione Peroxidase/metabolism ; HSP40 Heat-Shock Proteins/genetics ; HSP40 Heat-Shock Proteins/metabolism ; Heat-Shock Proteins/genetics ; Heat-Shock Proteins/metabolism ; Immunity, Innate ; Molecular Chaperones/genetics ; Molecular Chaperones/metabolism ; Prions/genetics ; Prions/metabolism ; Proteasome Endopeptidase Complex/metabolism ; Ribosomal Proteins/deficiency ; Ribosomal Proteins/genetics ; Ribosomal Proteins/metabolism ; Ribosome Subunits, Large, Eukaryotic/metabolism ; Saccharomyces cerevisiae ; Saccharomyces cerevisiae Proteins/genetics ; Saccharomyces cerevisiae Proteins/metabolism ; Ubiquitin-Protein Ligases/genetics ; Ubiquitin-Protein Ligases/metabolism ; Ubiquitination
Chemical Substances	Amino Acid Transport Systems ; BTN2 protein, S cerevisiae ; CUR1 protein, S cerevisiae ; HSP40 Heat-Shock Proteins ; HSP42 protein, S cerevisiae ; Heat-Shock Proteins ; Molecular Chaperones ; Prions ; Ribosomal Proteins ; SIS1 protein, S cerevisiae ; Saccharomyces cerevisiae Proteins ; Glutathione Peroxidase (EC 1.11.1.9) ; URE2 protein, S cerevisiae (EC 1.11.1.9) ; Ubiquitin-Protein Ligases (EC 2.3.2.27) ; Ubr2 protein, S cerevisiae (EC 2.3.2.27) ; Proteasome Endopeptidase Complex (EC 3.4.25.1)
Language	English
Publishing date	2021-05-13
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Intramural
ZDB-ID	2167-2
ISSN	1943-2631 ; 0016-6731
ISSN (online)	1943-2631
ISSN	0016-6731
DOI	10.1093/genetics/iyab013
Database	MEDical Literature Analysis and Retrieval System OnLINE

In stock of ZB MED Cologne/Königswinter

Zs.B 767: Show issues

Location:
Je nach Verfügbarkeit (siehe Angabe bei Bestand)
bis Jg. 2021: Bestellungen von Artikeln über das Online-Bestellformular
ab Jg. 2022: Lesesaal (EG)

Order via subito

Details ▾
- See ZB MED holdings
- Order with fees

Article: Anti-Prion Systems Block Prion Transmission, Attenuate Prion Generation, Cure Most Prions as They Arise and Limit Prion-Induced Pathology in Saccharomyces cerevisiae

Wickner, Reed B. / Edskes, Herman K. / Son, Moonil / Wu, Songsong

Biology. 2022 Aug. 26, v. 11, no. 9

2022

Abstract	All variants of the yeast prions [PSI+] and [URE3] are detrimental to their hosts, as shown by the dramatic slowing of growth (or even lethality) of a majority, by the rare occurrence in wild isolates of even the mildest variants and by the absence of reproducible benefits of these prions. To deal with the prion problem, the host has evolved an array of anti-prion systems, acting in normal cells (without overproduction or deficiency of any component) to block prion transmission from other cells, to lower the rates of spontaneous prion generation, to cure most prions as they arise and to limit the damage caused by those variants that manage to elude these (necessarily) imperfect defenses. Here we review the properties of prion protein sequence polymorphisms Btn2, Cur1, Hsp104, Upf1,2,3, ribosome-associated chaperones, inositol polyphosphates, Sis1 and Lug1, which are responsible for these anti-prion effects. We recently showed that the combined action of ribosome-associated chaperones, nonsense-mediated decay factors and the Hsp104 disaggregase lower the frequency of [PSI+] appearance as much as 5000-fold. Moreover, while Btn2 and Cur1 are anti-prion factors against [URE3] and an unrelated artificial prion, they promote [PSI+] prion generation and propagation.
Keywords	Saccharomyces cerevisiae ; amino acid sequences ; death ; inositols ; polyphosphates ; prions ; yeasts
Language	English
Dates of publication	2022-0826
Publishing place	Multidisciplinary Digital Publishing Institute
Document type	Article
ZDB-ID	2661517-4
ISSN	2079-7737
ISSN	2079-7737
DOI	10.3390/biology11091266
Database	NAL-Catalogue (AGRICOLA)

Order via subito

Article: Innate immunity to prions: anti-prion systems turn a tsunami of prions into a slow drip

Wickner, Reed B. / Edskes, Herman K. / Son, Moonil / Wu, Songsong / Niznikiewicz, Madaleine

Current genetics. 2021 Dec., v. 67, no. 6

2021

Abstract: The yeast prions (infectious proteins) [URE3] and [PSI+] are essentially non-functional (or even toxic) amyloid forms of Ure2p and Sup35p, whose normal function is in nitrogen catabolite repression and translation termination, respectively. Yeast has an ... ...

Abstract	The yeast prions (infectious proteins) [URE3] and [PSI+] are essentially non-functional (or even toxic) amyloid forms of Ure2p and Sup35p, whose normal function is in nitrogen catabolite repression and translation termination, respectively. Yeast has an array of systems working in normal cells that largely block infection with prions, block most prion formation, cure most nascent prions and mitigate the toxic effects of those prions that escape the first three types of systems. Here we review recent progress in defining these anti-prion systems, how they work and how they are regulated. Polymorphisms of the prion domains partially block infection with prions. Ribosome-associated chaperones ensure proper folding of nascent proteins, thus reducing [PSI+] prion formation and curing many [PSI+] variants that do form. Btn2p is a sequestering protein which gathers [URE3] amyloid filaments to one place in the cells so that the prion is often lost by progeny cells. Proteasome impairment produces massive overexpression of Btn2p and paralog Cur1p, resulting in [URE3] curing. Inversely, increased proteasome activity, by derepression of proteasome component gene transcription or by 60S ribosomal subunit gene mutation, prevents prion curing by Btn2p or Cur1p. The nonsense-mediated decay proteins (Upf1,2,3) cure many nascent [PSI+] variants by associating with Sup35p directly. Normal levels of the disaggregating chaperone Hsp104 can also cure many [PSI+] prion variants. By keeping the cellular levels of certain inositol polyphosphates / pyrophosphates low, Siw14p cures certain [PSI+] variants. It is hoped that exploration of the yeast innate immunity to prions will lead to discovery of similar systems in humans.
Keywords	amyloid ; catabolite repression ; genes ; innate immunity ; inositols ; mutation ; nitrogen ; prions ; progeny ; proteasome endopeptidase complex ; pyrophosphates ; toxicity ; transcription (genetics) ; tsunamis ; yeasts
Language	English
Dates of publication	2021-12
Size	p. 833-847.
Publishing place	Springer Berlin Heidelberg
Document type	Article
Note	Review
ZDB-ID	282876-5
ISSN	1432-0983 ; 0172-8083
ISSN (online)	1432-0983
ISSN	0172-8083
DOI	10.1007/s00294-021-01203-1
Database	NAL-Catalogue (AGRICOLA)

Full text online

Accessible to users with ZB MED library card

In stock of ZB MED Bonn / Germany

Z 81/707: Show issues

Order via subito

Inter-library loan at ZB MED

Your chosen title can be delivered directly to ZB MED Cologne location if you are registered as a user at ZB MED Cologne.

Details ▾

Article ; Online: Prion Variants of Yeast are Numerous, Mutable, and Segregate on Growth, Affecting Prion Pathogenesis, Transmission Barriers, and Sensitivity to Anti-Prion Systems.

Wickner, Reed B / Son, Moonil / Edskes, Herman K

Viruses

2019 Volume 11, Issue 3

Abstract: The known amyloid-based prions ... ...

Abstract	The known amyloid-based prions of
MeSH term(s)	Amyloid/chemistry ; Amyloid/genetics ; Genetic Variation ; Molecular Chaperones ; Mutation ; Prions/genetics ; Prions/pathogenicity ; Protein Conformation ; Saccharomyces cerevisiae/genetics ; Saccharomyces cerevisiae Proteins/genetics
Chemical Substances	Amyloid ; Molecular Chaperones ; Prions ; Saccharomyces cerevisiae Proteins
Language	English
Publishing date	2019-03-09
Publishing country	Switzerland
Document type	Journal Article ; Research Support, N.I.H., Intramural ; Review
ZDB-ID	2516098-9
ISSN	1999-4915 ; 1999-4915
ISSN (online)	1999-4915
ISSN	1999-4915
DOI	10.3390/v11030238
Database	MEDical Literature Analysis and Retrieval System OnLINE

Order via subito

Article ; Online: Proteasome Control of [URE3] Prion Propagation by Degradation of Anti-Prion Proteins Cur1 and Btn2 in Saccharomyces cerevisiae.

Edskes, Herman K / Stroobant, Emily E / DeWilde, Morgan P / Bezsonov, Evgeny E / Wickner, Reed B

Genetics

2021 Volume 218, Issue 1

Abstract: URE3] is a prion of the nitrogen catabolism controller, Ure2p, and [PSI+] is a prion of the translation termination factor Sup35p in S. cerevisiae. Btn2p cures [URE3] by sequestration of Ure2p amyloid filaments. Cur1p, paralogous to Btn2p, also cures [ ... ...

Abstract	[URE3] is a prion of the nitrogen catabolism controller, Ure2p, and [PSI+] is a prion of the translation termination factor Sup35p in S. cerevisiae. Btn2p cures [URE3] by sequestration of Ure2p amyloid filaments. Cur1p, paralogous to Btn2p, also cures [URE3], but by a different (unknown) mechanism. We find that an array of mutations impairing proteasome assembly or MG132 inhibition of proteasome activity result in loss of [URE3]. In proportion to their prion-curing effects, each mutation affecting proteasomes elevates the cellular concentration of the anti-prion proteins Btn2 and Cur1. Of >4,600 proteins detected by SILAC, Btn2p was easily the most overexpressed in a pre9Δ (α3 core subunit) strain. Indeed, deletion of BTN2 and CUR1 prevents the prion-curing effects of proteasome impairment. Surprisingly, the 15 most unstable yeast proteins are not increased in pre9Δ cells suggesting altered proteasome specificity rather than simple inactivation. Hsp42, a chaperone that cooperates with Btn2 and Cur1 in curing [URE3], is also necessary for the curing produced by proteasome defects, although Hsp42p levels are not substantially altered by a proteasome defect. We find that pre9Δ and proteasome chaperone mutants that most efficiently lose [URE3], do not destabilize [PSI+] or alter cellular levels of Sup35p. A tof2 mutation or deletion likewise destabilizes [URE3], and elevates Btn2p, suggesting that Tof2p deficiency inactivates proteasomes. We suggest that when proteasomes are saturated with denatured/misfolded proteins, their reduced degradation of Btn2p and Cur1p automatically upregulates these aggregate-handling systems to assist in the clean-up.
MeSH term(s)	Amino Acid Transport Systems/genetics ; Amino Acid Transport Systems/metabolism ; Amyloid/metabolism ; Cytoplasm/metabolism ; Fungal Proteins/metabolism ; Glutathione Peroxidase/genetics ; Glutathione Peroxidase/metabolism ; Heat-Shock Proteins/genetics ; Molecular Chaperones/genetics ; Molecular Chaperones/metabolism ; Peptide Termination Factors/genetics ; Peptide Termination Factors/metabolism ; Prion Proteins/metabolism ; Prions/genetics ; Prions/metabolism ; Proteasome Endopeptidase Complex/metabolism ; Saccharomyces cerevisiae/genetics ; Saccharomyces cerevisiae Proteins/genetics ; Saccharomyces cerevisiae Proteins/metabolism
Chemical Substances	Amino Acid Transport Systems ; Amyloid ; BTN2 protein, S cerevisiae ; CUR1 protein, S cerevisiae ; Fungal Proteins ; HSP42 protein, S cerevisiae ; Heat-Shock Proteins ; Molecular Chaperones ; Peptide Termination Factors ; Prion Proteins ; Prions ; SUP35 protein, S cerevisiae ; Saccharomyces cerevisiae Proteins ; Glutathione Peroxidase (EC 1.11.1.9) ; URE2 protein, S cerevisiae (EC 1.11.1.9) ; Proteasome Endopeptidase Complex (EC 3.4.25.1)
Language	English
Publishing date	2021-03-19
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Intramural
ZDB-ID	2167-2
ISSN	1943-2631 ; 0016-6731
ISSN (online)	1943-2631
ISSN	0016-6731
DOI	10.1093/genetics/iyab037
Database	MEDical Literature Analysis and Retrieval System OnLINE

In stock of ZB MED Cologne/Königswinter

Zs.B 767: Show issues

Location:
Je nach Verfügbarkeit (siehe Angabe bei Bestand)
bis Jg. 2021: Bestellungen von Artikeln über das Online-Bestellformular
ab Jg. 2022: Lesesaal (EG)

Order via subito

Details ▾
- See ZB MED holdings
- Order with fees

Article ; Online: Innate immunity to prions: anti-prion systems turn a tsunami of prions into a slow drip.

Wickner, Reed B / Edskes, Herman K / Son, Moonil / Wu, Songsong / Niznikiewicz, Madaleine

Current genetics

2021 Volume 67, Issue 6, Page(s) 833–847

Abstract	The yeast prions (infectious proteins) [URE3] and [PSI+] are essentially non-functional (or even toxic) amyloid forms of Ure2p and Sup35p, whose normal function is in nitrogen catabolite repression and translation termination, respectively. Yeast has an array of systems working in normal cells that largely block infection with prions, block most prion formation, cure most nascent prions and mitigate the toxic effects of those prions that escape the first three types of systems. Here we review recent progress in defining these anti-prion systems, how they work and how they are regulated. Polymorphisms of the prion domains partially block infection with prions. Ribosome-associated chaperones ensure proper folding of nascent proteins, thus reducing [PSI+] prion formation and curing many [PSI+] variants that do form. Btn2p is a sequestering protein which gathers [URE3] amyloid filaments to one place in the cells so that the prion is often lost by progeny cells. Proteasome impairment produces massive overexpression of Btn2p and paralog Cur1p, resulting in [URE3] curing. Inversely, increased proteasome activity, by derepression of proteasome component gene transcription or by 60S ribosomal subunit gene mutation, prevents prion curing by Btn2p or Cur1p. The nonsense-mediated decay proteins (Upf1,2,3) cure many nascent [PSI+] variants by associating with Sup35p directly. Normal levels of the disaggregating chaperone Hsp104 can also cure many [PSI+] prion variants. By keeping the cellular levels of certain inositol polyphosphates / pyrophosphates low, Siw14p cures certain [PSI+] variants. It is hoped that exploration of the yeast innate immunity to prions will lead to discovery of similar systems in humans.
MeSH term(s)	Amyloid/chemistry ; Amyloid/immunology ; Amyloid/metabolism ; Amyloidogenic Proteins/chemistry ; Amyloidogenic Proteins/immunology ; Amyloidogenic Proteins/metabolism ; Animals ; Autophagy ; Disease Resistance/immunology ; Disease Susceptibility/immunology ; Fungal Proteins/chemistry ; Fungal Proteins/genetics ; Fungal Proteins/immunology ; Host-Pathogen Interactions/genetics ; Host-Pathogen Interactions/immunology ; Humans ; Immunity, Innate ; Molecular Chaperones/metabolism ; Mutation ; Nonsense Mediated mRNA Decay ; Prion Diseases/etiology ; Prion Diseases/metabolism ; Prions/chemistry ; Prions/genetics ; Prions/immunology ; Prions/metabolism ; Protein Binding ; Protein Conformation ; Protein Folding ; Ribosomes/metabolism
Chemical Substances	Amyloid ; Amyloidogenic Proteins ; Fungal Proteins ; Molecular Chaperones ; Prions
Language	English
Publishing date	2021-07-28
Publishing country	United States
Document type	Journal Article ; Review
ZDB-ID	282876-5
ISSN	1432-0983 ; 0172-8083
ISSN (online)	1432-0983
ISSN	0172-8083
DOI	10.1007/s00294-021-01203-1
Database	MEDical Literature Analysis and Retrieval System OnLINE

Full text online

Accessible to users with ZB MED library card

In stock of ZB MED Cologne/Königswinter

Zs.A 2586: Show issues

Location:
Je nach Verfügbarkeit (siehe Angabe bei Bestand)
bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular
Jg. 1995 - 2021: Lesesall (2.OG)
ab Jg. 2022: Lesesaal (EG)

Order via subito

Details ▾

Article ; Online: Yeast killer elements hold their hosts hostage.

Wickner, Reed B / Edskes, Herman K

PLoS genetics

2015 Volume 11, Issue 5, Page(s) e1005139

MeSH term(s)	Cytoplasm/metabolism ; Killer Factors, Yeast/metabolism ; Kluyveromyces/metabolism ; Pichia/metabolism ; Ribonucleases/genetics ; Saccharomycetales/metabolism
Chemical Substances	Killer Factors, Yeast ; Ribonucleases (EC 3.1.-) ; anticodon nuclease (EC 3.1.-)
Language	English
Publishing date	2015-05
Publishing country	United States
Document type	Comment ; Journal Article ; Research Support, N.I.H., Intramural
ZDB-ID	2186725-2
ISSN	1553-7404 ; 1553-7390
ISSN (online)	1553-7404
ISSN	1553-7390
DOI	10.1371/journal.pgen.1005139
Database	MEDical Literature Analysis and Retrieval System OnLINE

Full text online

Full text

Order via subito

Details ▾
- Full text online
- Order with fees

To top

More links

Kategorien

In stock of ZB MED Cologne/Königswinter

Order via subito

More links

Kategorien

Order via subito

More links

Kategorien

Order via subito

More links

Kategorien

In stock of ZB MED Cologne/Königswinter

Order via subito

More links

Kategorien

Order via subito

Full text online

More links

Kategorien

In stock of ZB MED Bonn / Germany

Order via subito

Inter-library loan at ZB MED

More links

Kategorien

Order via subito

More links

Kategorien

In stock of ZB MED Cologne/Königswinter

Order via subito

Full text online

More links

Kategorien

In stock of ZB MED Cologne/Königswinter

Order via subito

Full text online

More links

Kategorien

Order via subito