A genome-wide screen identifies Yos9p as essential for ER-associated degradation of glycoproteins. - Wikidata - awgldk - TriplyDB

A genome-wide screen identifies Yos9p as essential for ER-associated degradation of glycoproteins.

A genome-wide screen identifies Yos9p as essential for ER-associated degradation of glycoproteins.

http://www.wikidata.org/entity/Q31130967

about

The MRH protein Erlectin is a member of the endoplasmic reticulum synexpression group and functions in N-glycan recognition OS-9 and GRP94 deliver mutant alpha1-antitrypsin to the Hrd1-SEL1L ubiquitin ligase complex for ERAD Human OS-9, a lectin required for glycoprotein endoplasmic reticulum-associated degradation, recognizes mannose-trimmed N-glycans Human XTP3-B forms an endoplasmic reticulum quality control scaffold with the HRD1-SEL1L ubiquitin ligase complex and BiP A dual task for the Xbp1-responsive OS-9 variants in the mammalian endoplasmic reticulum: inhibiting secretion of misfolded protein conformers and enhancing their disposal Multiprotein complexes that link dislocation, ubiquitination, and extraction of misfolded proteins from the endoplasmic reticulum membrane.Inhibition of p97-dependent protein degradation by Eeyarestatin I One step at a time: endoplasmic reticulum-associated degradation Recent technical developments in the study of ER-associated degradation Selective destruction of abnormal proteins by ubiquitin-mediated protein quality control degradation Defining the glycan destruction signal for endoplasmic reticulum-associated degradation Ubx4 modulates cdc48 activity and influences degradation of misfolded proteins of the endoplasmic reticulum Degradation of misfolded protein in the cytoplasm is mediated by the ubiquitin ligase Ubr1.Htm1 protein generates the N-glycan signal for glycoprotein degradation in the endoplasmic reticulum EDEM2 and OS-9 are required for ER-associated degradation of non-glycosylated sonic hedgehog.Free oligosaccharides to monitor glycoprotein endoplasmic reticulum-associated degradation in Saccharomyces cerevisiae Modularity of the Hrd1 ERAD complex underlies its diverse client range.Delivery of ubiquitinated substrates to protein-unfolding machines.Proteomic analysis of solid pseudopapillary tumor of the pancreas reveals dysfunction of the endoplasmic reticulum protein processing pathway The Unfolded Protein Response, Degradation from Endoplasmic Reticulum and Cancer Exposed hydrophobicity is a key determinant of nuclear quality control degradation.Absence of the Yeast Hsp31 Chaperones of the DJ-1 Superfamily Perturbs Cytoplasmic Protein Quality Control in Late Growth Phase.The evolution of N-glycan-dependent endoplasmic reticulum quality control factors for glycoprotein folding and degradation OS9 Protein Interacts with Na-K-2Cl Co-transporter (NKCC2) and Targets Its Immature Form for the Endoplasmic Reticulum-associated Degradation Pathway.Aberrant substrate engagement of the ER translocon triggers degradation by the Hrd1 ubiquitin ligase.SEL1L, the homologue of yeast Hrd3p, is involved in protein dislocation from the mammalian ER.Ubiquitin ligases, critical mediators of endoplasmic reticulum-associated degradation The endoplasmic reticulum-associated degradation pathways of budding yeast.Protein quality control: the who's who, the where's and therapeutic escapes.Protein quality control in the early secretory pathway Architecture and biosynthesis of the Saccharomyces cerevisiae cell wall.F-box proteins that contain sugar-binding domains.Intrinsic conformational determinants signal protein misfolding to the Hrd1/Htm1 endoplasmic reticulum-associated degradation system Sorting things out through endoplasmic reticulum quality control.ERAD ubiquitin ligases: multifunctional tools for protein quality control and waste disposal in the endoplasmic reticulum.Protein N-glycosylation, protein folding, and protein quality control.Making new out of old: recycling and modification of an ancient protein translocation system during eukaryotic evolution. Mechanistic comparison and phylogenetic analysis of ERAD, SELMA and the peroxisomal importomer.Endoplasmic reticulum lectin XTP3-B inhibits endoplasmic reticulum-associated degradation of a misfolded α1-antitrypsin variant.Proteolytic regulation of metabolic enzymes by E3 ubiquitin ligase complexes: lessons from yeast.Glycosylation-directed quality control of protein folding.

P2860

Q24307679-1637DED3-2B12-421B-8658-5905270BD3E3 Q24312778-75BB684F-0AB9-4B26-8AB3-0CFD4EBF5E21 Q24313146-75596B54-7DB6-49C1-AA5C-207338F99C85 Q24316328-A1A06111-18E1-40CE-B383-D419AD3CC0A9 Q24322193-F2304876-AD5E-432B-9ECA-EA6129D59D3A Q24530318-DA735CFA-102B-44B4-9DDF-2A614AD01BE5 Q24648805-1CBACD0A-3DEB-4527-A7F1-35D831046501 Q24658302-3512F382-ABE2-4827-97AC-3FBB45748B1C Q26823514-8E549781-2A9F-489E-A0FE-10882A194142 Q26824733-FB894AE5-ACC1-4F17-9A45-DA06510E5C8B Q27932810-A084A8CF-8F1A-4F40-A604-50EE07A4A448 Q27939043-241AE23B-8460-44B1-9706-3648A6387121 Q27939178-04798F6A-309A-4AB3-A2B1-D898A21D3194 Q27939524-7587B85A-A954-49E6-A717-7273D62591F4 Q31164916-C2098225-F04C-4EEA-B18A-26D550D319D1 Q33530815-9027BFD6-242F-4191-A986-790CFAFB5C4C Q33717057-C013CB18-06E0-4ABE-A3E6-12FC8425AFBE Q33989072-C13F8056-ECF2-40CD-AE0B-FF3B3831C6E6 Q34303343-F3A7F3D1-CABF-4528-8CDF-082B2B12903D Q34576070-EA9B97DF-8A4B-443C-B4B6-B4202FF567BB Q35083477-4DA9B5B8-6AC7-49AC-A084-BF7AC7182079 Q35806855-8ABC9BEC-047F-4125-9E5A-615E3312CDBD Q35867639-476B1430-8379-4F06-8A1C-67104AD03807 Q35882928-03D4504D-84A0-469E-8209-D4B1FCE866E9 Q36027390-2A20C51B-D871-4CBE-8B65-23943534D508 Q36119119-127D7364-C1B6-4338-A33F-DE873BECE860 Q36384570-B9080767-8852-4BA8-BC22-E995B8871A83 Q36418006-E38D072F-5099-4EEE-BB63-4A793CAC7B14 Q36432134-E44BAB0B-6F00-4497-9149-9BAAC480C8B1 Q36446833-0E5C3D35-F575-43F9-9F99-1D76BA61F257 Q36466304-AC501C17-2B4E-4796-AC00-39C611665390 Q36994894-2A92EAEF-0340-43D6-97F2-5DAEDB851CD3 Q37262161-E675D087-543B-49DF-8237-360137EA2257 Q37765593-90AFF41F-78F3-47AA-AEA4-21792F28DAC1 Q37784156-BFBBA423-53CF-4B71-8108-3DBCB956CF84 Q37845738-6777ED84-C77C-42B6-8452-1C682A646718 Q37855729-9E1F3B2C-A3D4-45AB-8E13-5EB78F161DA1 Q38318154-5CC385D3-90EA-40A3-A6A1-BC2170B00B0F Q38585206-08B553C9-EE74-40C7-BF23-0FC1219B0A6E Q38606832-5715FD92-AD0F-402D-A7B8-6F3464D04C40

P2860

A genome-wide screen identifies Yos9p as essential for ER-associated degradation of glycoproteins.

http://www.wikidata.org/entity/Q31130967

description

2004 nî lūn-bûn

@nan

2004 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած

@hyw

2004 թվականի նոյեմբերին հրատարակված գիտական հոդված

@hy

2004年の論文

@ja

2004年論文

@yue

2004年論文

@zh-hant

2004年論文

@zh-hk

2004年論文

@zh-mo

2004年論文

@zh-tw

2004年论文

@wuu

name

A genome-wide screen identifie ...... degradation of glycoproteins.

@ast

A genome-wide screen identifie ...... degradation of glycoproteins.

@en

type

label

A genome-wide screen identifie ...... degradation of glycoproteins.

@ast

A genome-wide screen identifie ...... degradation of glycoproteins.

@en

prefLabel

A genome-wide screen identifie ...... degradation of glycoproteins.

@ast

A genome-wide screen identifie ...... degradation of glycoproteins.

@en

P1433

Q31130967-B86A360B-CC9B-4846-BC15-B221DD84DA05

P1476

Q31130967-A499BD35-21D6-4051-BBC6-97259F117F40

P2093

Q31130967-0C9CF9DE-9AED-4B86-A0D4-646194CF727A

Q31130967-2B636C16-86D5-47E6-A318-7339494518DE

Q31130967-606C05D7-388B-45B5-B8F9-57AADE057A78

Q31130967-9EF0B35A-313E-457A-A5B0-302088A8EE15

P2860

Q31130967-06CF2966-66E2-4BF3-BA7C-E77496BF1C2D

Q31130967-119D97CB-EB2C-429D-B940-1327F3FC0800

Q31130967-1CE7AFF8-AD3D-4A90-9035-1EC0728C31EA

Q31130967-21567065-9E50-4285-A39C-FDB3E53B09D2

Q31130967-2979F2FE-8BC0-46D8-8077-C2FDB9B9CF0E

Q31130967-2A00B813-A925-45DF-9F78-9A662FDA84B2

Q31130967-2D1A69E3-9D6A-4ED4-B6E3-508CBD7A40CE

Q31130967-37D68B11-3B1B-4C7C-B996-10B8801BB8ED

Q31130967-4438B45E-DAEA-4F48-98AD-20289A953BF6

Q31130967-5D3E22F5-3F4D-4AD6-93C7-5869CF89C4E2

P304

Q31130967-6FCF7353-2FCE-49B7-94AD-CF48F2829918

P31

Q31130967-3E6A2461-C476-45B0-9425-DB1772CF3004

P356

Q31130967-25F12F7C-7EC3-4093-B239-34A322E79BDE

P407

Q31130967-3DC8528B-D827-40A7-B053-1A9856DFBF79

P433

Q31130967-2DA04044-D778-45DF-BFE5-BBA12CB25915

P478

Q31130967-DA3B1FD2-3F94-4ADA-BBF4-979B5CDB328D

P577

Q31130967-552E37E9-7323-412F-931C-63B97A75C237

P5875

Q31130967-09BE197C-A4C0-41D0-8ABF-DED4031B59B7

P698

Q31130967-7D4FF5C8-DE6B-4523-B59F-01F59EDBDFE6

P356

J.FEBSLET.2004.10.039

P1433

P1476

A genome-wide screen identifie ...... degradation of glycoproteins.

@en

P2093

Balasubrahmanyam Medicherla

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

Bettina A Buschhorn

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

Dieter H Wolf

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

Zlatka Kostova

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

P2860

Role of EDEM in the release of misfolded glycoproteins from the calnexin cycle

ER degradation of a misfolded luminal protein by the cytosolic ubiquitin-proteasome pathway.

N-Glycosylation affects endoplasmic reticulum degradation of a mutated derivative of carboxypeptidase yscY in yeast.

A genomic screen identifies Dsk2p and Rad23p as essential components of ER-associated degradation

Mnl1p, an alpha -mannosidase-like protein in yeast Saccharomyces cerevisiae, is required for endoplasmic reticulum-associated degradation of glycoproteins.

Degradation of misfolded endoplasmic reticulum glycoproteins in Saccharomyces cerevisiae is determined by a specific oligosaccharide structure.

A selective interaction between OS-9 and the carboxyl-terminal tail of meprin beta

EDEM as an acceptor of terminally misfolded glycoproteins released from calnexin

Lectin control of protein folding and sorting in the secretory pathway

Additional modules for versatile and economical PCR-based gene deletion and modification in Saccharomyces cerevisiae

P304

422-426

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

P31

scholarly article

P356

10.1016/J.FEBSLET.2004.10.039

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

P407

P433

3

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

P478

577

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

P577

2004-11-01T00:00:00Z

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

P5875

8169956

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

P698

15556621

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