Mnl1p, an alpha -mannosidase-like protein in yeast Saccharomyces cerevisiae, is required for endoplasmic reticulum-associated degradation of glycoproteins.
about
Profile-based data base scanning for animal L-type lectins and characterization of VIPL, a novel VIP36-like endoplasmic reticulum proteinHuman EDEM2, a novel homolog of family 47 glycosidases, is involved in ER-associated degradation of glycoproteinsHuman XTP3-B forms an endoplasmic reticulum quality control scaffold with the HRD1-SEL1L ubiquitin ligase complex and BiPA dual role for EDEM1 in the processing of rod opsinGetting in and out from calnexin/calreticulin cyclesMisfolded proteins are sorted by a sequential checkpoint mechanism of ER quality controlEndoplasmic reticulum stress in the β-cell pathogenesis of type 2 diabetesStructure of Penicillium citrinum alpha 1,2-mannosidase reveals the basis for differences in specificity of the endoplasmic reticulum and Golgi class I enzymesModulation of activity by Arg407: structure of a fungal α-1,2-mannosidase in complex with a substrate analogueFree-oligosaccharide control in the yeast Saccharomyces cerevisiae: roles for peptide:N-glycanase (Png1p) and vacuolar mannosidase (Ams1p).Defining the glycan destruction signal for endoplasmic reticulum-associated degradationAn HRD/DER-independent ER quality control mechanism involves Rsp5p-dependent ubiquitination and ER-Golgi transportRoles of protein-disulfide isomerase-mediated disulfide bond formation of yeast Mnl1p in endoplasmic reticulum-associated degradationA Complex of Htm1 and the Oxidoreductase Pdi1 Accelerates Degradation of Misfolded Glycoproteins.Yos9p and Hrd1p mediate ER retention of misfolded proteins for ER-associated degradation.EDEM accelerates ERAD by preventing aberrant dimer formation of misfolded alpha1-antitrypsinRoles of molecular chaperones in endoplasmic reticulum (ER) quality control and ER-associated degradation (ERAD)A novel stress-induced EDEM variant regulating endoplasmic reticulum-associated glycoprotein degradationEDEM1 accelerates the trimming of alpha1,2-linked mannose on the C branch of N-glycansFbs2 is a new member of the E3 ubiquitin ligase family that recognizes sugar chainsEDEM3, a soluble EDEM homolog, enhances glycoprotein endoplasmic reticulum-associated degradation and mannose trimmingA genome-wide screen identifies Yos9p as essential for ER-associated degradation of glycoproteins.EDEM2 and OS-9 are required for ER-associated degradation of non-glycosylated sonic hedgehog.Modularity of the Hrd1 ERAD complex underlies its diverse client range.Capturing protein interactions in the secretory pathway of living cells.Evasion of endoplasmic reticulum surveillance makes Wsc1p an obligate substrate of Golgi quality controlOrganizational diversity among distinct glycoprotein endoplasmic reticulum-associated degradation programsCharacterization of Schizosaccharomyces pombe ER alpha-mannosidase: a reevaluation of the role of the enzyme on ER-associated degradationA novel lectin in the secretory pathway. An elegant mechanism for glycoprotein elimination.For whom the bell tolls: protein quality control of the endoplasmic reticulum and the ubiquitin-proteasome connection.Protein disulfide isomerases contribute differentially to the endoplasmic reticulum-associated degradation of apolipoprotein B and other substratesThe evolution of N-glycan-dependent endoplasmic reticulum quality control factors for glycoprotein folding and degradationSearch and destroy: ER quality control and ER-associated protein degradation.Versatility of the endoplasmic reticulum protein folding factory.Haploid yeast cells undergo a reversible phenotypic switch associated with chromosome II copy numberSingle, context-specific glycans can target misfolded glycoproteins for ER-associated degradationThe endoplasmic reticulum-associated degradation pathways of budding yeast.Protein quality control: the who's who, the where's and therapeutic escapes.N-linked glycan recognition and processing: the molecular basis of endoplasmic reticulum quality controlGlycoprotein folding and the role of EDEM1, EDEM2 and EDEM3 in degradation of folding-defective glycoproteins.
P2860
Q24296321-93275208-4AE9-473C-971A-FBD87573A6F7Q24313639-AE91945B-29D9-4CAC-85EE-FEA4A4000166Q24316328-B2825513-1429-46B7-A904-4390CA179AE4Q24320047-462A3A86-1C20-4FD5-832F-E49256AAFD1FQ24646392-A77BD1B3-8EC6-42CA-A003-0BDE0969E86FQ24677354-441DAC8E-D2DA-4B09-B81D-F5F121FE0042Q26864340-E6D7BBC7-ECCA-4B5D-9AAA-4A32A3FC7F30Q27636288-2B3BD0BF-38C8-41A6-A1DC-5F5CE42806CEQ27650005-B01F48A0-FC55-4CFA-A2A5-26F97BE1CBFEQ27931323-19928A2A-3FEA-4B94-8E64-A8C4A98CA92EQ27932810-61C2B1E8-7D33-4B5B-B22D-AB9F57296F0EQ27933526-9B462EB3-4484-4BD2-81C9-999A0A6159C6Q27934273-BB0C57F6-DD0F-4CBC-AF88-80885D0AA2DEQ27935416-5ED7F321-2F44-429B-A110-701A53A30EB3Q27939066-44D4FF4E-0522-4540-8B21-BBA1BC85B1B0Q28235801-56B48C32-05EF-48D4-9A46-80686328B38EQ28255326-D77F2330-A3CA-477A-85AF-15D9C4EF0546Q28296585-6020073B-551F-454C-B7D8-29C057B5F66DQ28510507-A32647EC-03BA-4718-9039-3199A49EA560Q28590989-244BA333-7E6C-4588-9DB9-E69C56EB2CD6Q28593084-2D66E65F-7B7C-49A7-AD1F-FA5C2C7DE75BQ31130967-FC863573-E645-4DCB-A879-885326A1692CQ31164916-F408064E-6506-421B-B93D-AECC78BBC386Q33717057-CBF81170-B2A1-4D0F-8098-E92E175FC8A0Q33758366-A40FB7CE-E583-4B5C-8F32-FFBFA590321EQ33761462-6B1459FE-6FF4-47F2-83B9-A5D06C76A1EFQ33902839-5F4230B8-4103-4CC4-A561-6A879050541CQ34049758-32725DBE-0EB2-4120-89E6-6FE21C91159FQ34330208-BA0C784D-D8A7-4439-8B95-AA62E91BB69CQ35125892-A921FA01-A4E2-48B8-9C64-CF33C9A17E12Q35756661-61C04485-AE0E-41E6-8AF4-F8782B37FE53Q35867639-21935328-288D-41F9-89DE-6B2D41605FD6Q36090973-4CD9445E-A95C-47A9-8609-7C687EA8FEE7Q36242585-91BC50D8-7219-4A70-9CD4-2EAAC22825CCQ36255022-9E4DCF4D-FF49-4808-9104-80FA0EB0C16DQ36321616-8819A194-1892-49C0-B701-307722EDBC54Q36418006-0C7AD699-0B25-4700-B3EF-2069431A3FE0Q36432134-D8DF6719-7B43-4A3B-ADE7-599C3D86DDAAQ36580003-5F5605CF-6C5A-4C82-9210-4770FBA73DC1Q36820743-E31DB000-6852-4629-9308-047857051BBA
P2860
Mnl1p, an alpha -mannosidase-like protein in yeast Saccharomyces cerevisiae, is required for endoplasmic reticulum-associated degradation of glycoproteins.
description
2001 nî lūn-bûn
@nan
2001 թուականի Մարտին հրատարակուած գիտական յօդուած
@hyw
2001 թվականի մարտին հրատարակված գիտական հոդված
@hy
2001年の論文
@ja
2001年論文
@yue
2001年論文
@zh-hant
2001年論文
@zh-hk
2001年論文
@zh-mo
2001年論文
@zh-tw
2001年论文
@wuu
name
Mnl1p, an alpha -mannosidase-l ...... degradation of glycoproteins.
@ast
Mnl1p, an alpha -mannosidase-l ...... degradation of glycoproteins.
@en
Mnl1p, an alpha -mannosidase-l ...... degradation of glycoproteins.
@nl
type
label
Mnl1p, an alpha -mannosidase-l ...... degradation of glycoproteins.
@ast
Mnl1p, an alpha -mannosidase-l ...... degradation of glycoproteins.
@en
Mnl1p, an alpha -mannosidase-l ...... degradation of glycoproteins.
@nl
prefLabel
Mnl1p, an alpha -mannosidase-l ...... degradation of glycoproteins.
@ast
Mnl1p, an alpha -mannosidase-l ...... degradation of glycoproteins.
@en
Mnl1p, an alpha -mannosidase-l ...... degradation of glycoproteins.
@nl
P2093
P2860
P356
P1476
Mnl1p, an alpha -mannosidase-l ...... degradation of glycoproteins.
@en
P2093
P2860
P304
P356
10.1074/JBC.C100023200
P407
P577
2001-03-23T00:00:00Z