Htm1p, a mannosidase-like protein, is involved in glycoprotein degradation in yeast.
about
Congenital disorders of glycosylation type Ig is defined by a deficiency in dolichyl-P-mannose:Man7GlcNAc2-PP-dolichyl mannosyltransferaseProfile-based data base scanning for animal L-type lectins and characterization of VIPL, a novel VIP36-like endoplasmic reticulum proteinMannose trimming is required for delivery of a glycoprotein from EDEM1 to XTP3-B and to late endoplasmic reticulum-associated degradation stepsHuman 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 BiPGetting in and out from calnexin/calreticulin cyclesMisfolded proteins are sorted by a sequential checkpoint mechanism of ER quality controlEDEM1 reveals a quality control vesicular transport pathway out of the endoplasmic reticulum not involving the COPII exit sitesEndoplasmic 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 analogueELM1 is required for multidrug resistance in Saccharomyces cerevisiae.Free-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.Htm1 protein generates the N-glycan signal for glycoprotein degradation in the endoplasmic reticulumArms Race between Enveloped Viruses and the Host ERAD MachineryEDEM 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 trimmingEDEM2 and OS-9 are required for ER-associated degradation of non-glycosylated sonic hedgehog.Redox diversity in ERAD-mediated protein retrotranslocation from the endoplasmic reticulum: a complex puzzle.The BiP molecular chaperone plays multiple roles during the biogenesis of torsinA, an AAA+ ATPase associated with the neurological disease early-onset torsion dystonia.Capturing protein interactions in the secretory pathway of living cells.Most F508del-CFTR is targeted to degradation at an early folding checkpoint and independently of calnexinOrganizational 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 degradationMutations of an alpha1,6 mannosyltransferase inhibit endoplasmic reticulum-associated degradation of defective brassinosteroid receptors in Arabidopsis.Two distinctly localized p-type ATPases collaborate to maintain organelle homeostasis required for glycoprotein processing and quality controlInositol deacylation by Bst1p is required for the quality control of glycosylphosphatidylinositol-anchored proteins.A novel lectin in the secretory pathway. An elegant mechanism for glycoprotein elimination.Forcible destruction of severely misfolded mammalian glycoproteins by the non-glycoprotein ERAD pathwayFor whom the bell tolls: protein quality control of the endoplasmic reticulum and the ubiquitin-proteasome connection.Ubiquitin-dependent protein degradation at the yeast endoplasmic reticulum and nuclear envelope.
P2860
Q24296242-490AE2B3-F9E2-4E5F-BE18-0B6E37F629FBQ24296321-4D56DC72-CA29-4068-90DC-421341DFC3DAQ24306408-ECFC5C14-82E2-4430-ABEC-DD0F37018EFFQ24313639-82D47D54-ECC6-4FD0-BB00-86B11EFC9F61Q24316328-906E8AA3-2581-4EB5-BF02-7502875259E4Q24646392-858088A9-701B-4ACF-9792-1513D1EC09FDQ24677354-9A3E58FD-B91D-4DC3-8BC7-3956EA4044AFQ24683239-F4E54090-85CC-4AC1-A5A0-C67C16A65092Q26864340-140FF192-AB23-435E-971C-0C2F22C40CEDQ27636288-23C8AB09-D8A0-49F0-97FF-C64EB41E06E4Q27650005-3B8C42CB-3F59-43FF-B2D1-97402A0E3F29Q27930917-DD605404-E407-42DA-BC6E-F5B7F4CBEDDFQ27931323-548E745E-7D98-4275-A982-174E4061AFDBQ27932810-EF1D5968-BDF8-43F0-9D69-3F086BC623DAQ27933526-13826865-B740-4A81-86FB-B989918C9422Q27934273-CE6468EC-299A-4E6B-AE9E-35C0BC2B3859Q27935416-B4B95047-9966-429F-9FF6-78F8FAAF0CF1Q27939066-5CD3254C-A56A-4B3C-858A-5469DE8C9717Q27939524-FBB5096E-1561-47FB-8703-14A788F5C6FEQ28078319-076CB5B2-5E32-4F8C-913B-25B210A16F67Q28235801-40C5978F-67FF-49D5-B0B1-BF1E96339F31Q28255326-56715A66-6E6F-48C9-B8CD-289F3C342867Q28296585-5ECE6E67-AA55-4969-9D31-A235DEBC139EQ28510507-A49EC47B-5E54-42D9-9600-143B54335609Q28590989-AA27469A-6385-45FF-AAFE-4E813CEB3457Q28593084-78275A5F-1A54-4C4D-A82E-02A431B66D66Q31164916-53CA22F6-3D45-46D1-BBD9-86B56891E901Q33360209-09FBE10C-C535-41D4-955C-984A1A1801F9Q33556224-E5857485-7ACB-4A57-8DD7-9E3B72B99DA0Q33758366-0F4D5E80-4908-4CEA-BE93-6E1FDD4670AFQ33836913-8E7DFED9-473A-4AFD-B966-A6E8ADBE2DA3Q33902839-83CD1B43-7DE1-4D15-96BB-D691A8472FDDQ34049758-24EC8AE9-6E45-491D-8ED1-9B3B31F503C7Q34089074-53B6D081-C2A6-4B29-B4D2-FBBD817E5A62Q34274554-89EC86B6-3D2D-49CA-9959-6115E3124D8AQ34325759-D10F69DC-1C86-4B31-8EA7-465A27241843Q34330208-648D1AFE-2928-4937-8181-0B8A1DA59121Q34501894-12B69D62-6F1B-4A05-81AC-BD3A223638D1Q35125892-BB02B750-20AF-4E5C-A26D-7403064F29D5Q35175501-07A31910-2DCA-41C7-911F-5EDB4CF33A7F
P2860
Htm1p, a mannosidase-like protein, is involved in glycoprotein degradation in yeast.
description
2001 nî lūn-bûn
@nan
2001 թուականի Մայիսին հրատարակուած գիտական յօդուած
@hyw
2001 թվականի մայիսին 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
Htm1p, a mannosidase-like protein, is involved in glycoprotein degradation in yeast.
@ast
Htm1p, a mannosidase-like protein, is involved in glycoprotein degradation in yeast.
@en
Htm1p, a mannosidase-like protein, is involved in glycoprotein degradation in yeast.
@nl
type
label
Htm1p, a mannosidase-like protein, is involved in glycoprotein degradation in yeast.
@ast
Htm1p, a mannosidase-like protein, is involved in glycoprotein degradation in yeast.
@en
Htm1p, a mannosidase-like protein, is involved in glycoprotein degradation in yeast.
@nl
prefLabel
Htm1p, a mannosidase-like protein, is involved in glycoprotein degradation in yeast.
@ast
Htm1p, a mannosidase-like protein, is involved in glycoprotein degradation in yeast.
@en
Htm1p, a mannosidase-like protein, is involved in glycoprotein degradation in yeast.
@nl
P2093
P2860
P3181
P356
P1433
P1476
Htm1p, a mannosidase-like protein, is involved in glycoprotein degradation in yeast.
@en
P2093
D Y Thomas
J J Bergeron
P2860
P304
P3181
P356
10.1093/EMBO-REPORTS/KVE089
P407
P577
2001-05-01T00:00:00Z