Cloning and expression of a specific human alpha 1,2-mannosidase that trims Man9GlcNAc2 to Man8GlcNAc2 isomer B during N-glycan biosynthesis
about
Characterization of a cDNA encoding a novel human Golgi alpha 1, 2-mannosidase (IC) involved in N-glycan biosynthesisIn vitro mannose trimming property of human ER α-1,2 mannosidase IEndoplasmic reticulum (ER) mannosidase I is compartmentalized and required for N-glycan trimming to Man5-6GlcNAc2 in glycoprotein ER-associated degradationEDEM2 initiates mammalian glycoprotein ERAD by catalyzing the first mannose trimming stepA novel ER alpha-mannosidase-like protein accelerates ER-associated degradationCrystal structure of a class I α1,2-mannosidase involved in N-glycan processing and endoplasmic reticulum quality controlStructural basis for catalysis and inhibition of N-glycan processing class I alpha 1,2-mannosidasesStructure 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 analogueArms Race between Enveloped Viruses and the Host ERAD MachineryA 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-glycansRespiratory distress and neonatal lethality in mice lacking Golgi alpha1,2-mannosidase IB involved in N-glycan maturationElucidation of the molecular logic by which misfolded alpha 1-antitrypsin is preferentially selected for degradation.A Golgi-localized mannosidase (MAN1B1) plays a non-enzymatic gatekeeper role in protein biosynthetic quality control.Organizational 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 degradationGenome-wide expression analysis upon constitutive activation of the HacA bZIP transcription factor in Aspergillus niger reveals a coordinated cellular response to counteract ER stressMammalian ER mannosidase I resides in quality control vesicles, where it encounters its glycoprotein substrates.MAN1B1 deficiency: an unexpected CDG-IIMutations in the alpha 1,2-mannosidase gene, MAN1B1, cause autosomal-recessive intellectual disability.Golgi localization of ERManI defines spatial separation of the mammalian glycoprotein quality control system.N-Glycomic and Microscopic Subcellular Localization Analyses of NPP1, 2 and 6 Strongly Indicate that trans-Golgi Compartments Participate in the Golgi to Plastid Traffic of Nucleotide Pyrophosphatase/Phosphodiesterases in RiceERManI (Endoplasmic Reticulum Class I α-Mannosidase) Is Required for HIV-1 Envelope Glycoprotein Degradation via Endoplasmic Reticulum-associated Protein Degradation PathwayVersatility of the endoplasmic reticulum protein folding factory.Golgi-situated endoplasmic reticulum α-1, 2-mannosidase contributes to the retrieval of ERAD substrates through a direct interaction with γ-COP.The mammalian endoplasmic reticulum-associated degradation systemThe unfolded protein response transducer ATF6 represents a novel transmembrane-type endoplasmic reticulum-associated degradation substrate requiring both mannose trimming and SEL1L proteinThe mammalian UPR boosts glycoprotein ERAD by suppressing the proteolytic downregulation of ER mannosidase I.Glycoprotein folding and quality-control mechanisms in protein-folding diseasesProtein glycosylation in Candida.Human endoplasmic reticulum mannosidase I is subject to regulated proteolysis.Intracellular processing of alpha1-antitrypsin.Protein N-glycosylation, protein folding, and protein quality control.Enhancement of endoplasmic reticulum (ER) degradation of misfolded Null Hong Kong alpha1-antitrypsin by human ER mannosidase I.The Role of Lectin-Carbohydrate Interactions in the Regulation of ER-Associated Protein Degradation.Quality control of glycoprotein folding and ERAD: the role of N-glycan handling, EDEM1 and OS-9.N-glycan structure of a short-lived variant of ribophorin I expressed in the MadIA214 glycosylation-defective cell line reveals the role of a mannosidase that is not ER mannosidase I in the process of glycoprotein degradation.Effects of a defective ERAD pathway on growth and heterologous protein production in Aspergillus niger.Processing of N-linked glycans during endoplasmic-reticulum-associated degradation of a short-lived variant of ribophorin I.
P2860
Q22254696-D5895261-A769-4BCA-A59E-5F115645A7B5Q24299633-9853A0FB-E77D-4EA6-8A60-D2AAE2A14F7FQ24300458-BE0AB78D-3605-42D9-BA7E-DFA6D5EE6E2DQ24301651-C1F8F0B7-D2E2-44D9-99B0-59C17E978590Q24522524-46A25E3A-C708-4192-92D8-FB6E8D5C045FQ27621384-BD6A51E9-3BB0-4602-9B0B-F8BFF52B94CBQ27627138-897B68D2-A234-4B04-BC77-31C85659901AQ27636288-D14C6114-4775-40EE-83E3-B54A72CA042EQ27650005-84539695-21E4-48B2-90CE-1CAB00DC4564Q28078319-39CA2F1C-42A8-4D04-9E8B-C339F707E6BEQ28296585-36ECF5F4-1FCF-4F05-A37A-8CAC66D7C5C1Q28510507-0A827BBB-4D66-40D5-B128-553B4C4E7791Q28511719-E70C879B-1303-4494-94B7-E8EAD0FA24CAQ30332997-293DB143-825E-4F96-B2E4-6E9AA5FF8244Q30360183-0C357712-2DCD-4812-BF84-E0E1BF2E4A4EQ33902839-335DB478-854B-4D97-87F8-42D2912E5CA7Q34049758-11D274AE-8230-4065-A2F7-A41EDE38D182Q34356834-88636AD1-A5E5-44B2-9E13-62DCAC1238E1Q34960623-D680A161-7B27-4130-B6C9-C10043308571Q35069214-4C988244-81BB-475C-B139-99598E3CA1E5Q35103799-9619B22B-EEB8-4DEC-8BB8-B51A3A3B691AQ35160707-8D65C1C4-1AB8-4E47-94BF-7BD9C5ABCBBCQ36059457-B7166BD8-F795-4B6C-A5B7-EC1AC25B5714Q36065264-A7C4FBB3-EC67-4A6C-A3D9-F80CD3A95466Q36242585-44D4BE0B-223D-4AE0-A3EF-F1851ADAA891Q36758411-778B61DA-51EA-437B-BF8C-8899B86D898DQ37122324-F9F10B6B-732D-4786-8680-37740A32DD37Q37272082-91B40F26-BD7E-4CFE-8E6A-35CD1F20A9FFQ37289488-4E31F514-0FA1-4A3B-AA8A-102A7539EAEEQ37621073-2FA269FE-985D-4CCE-B9D5-B6CDE6F66268Q37628674-50AC88B9-0C4C-4515-A1D3-793190C38576Q37672299-7D537352-D423-41FB-8E92-A7900C178CF1Q37804624-D9B9E18A-1E4E-49DE-83DE-EA394E295626Q37845738-BC49E75D-A392-406F-B138-AE6BB75B773FQ38354843-B8479C2D-D433-4184-93C9-6B43A705C7FBQ38507330-36893C9A-6789-4A8C-BA9B-1374B870FA3DQ38996383-FA045326-6420-4C03-83E1-5EE3575925D2Q40793481-18C59693-FF75-42AE-AB17-ECA003CD4FBEQ41643911-9C6386A0-3F74-4FE9-869E-9DC1DB358CBCQ42155205-1658AE08-542A-4840-A6F5-803475EB4821
P2860
Cloning and expression of a specific human alpha 1,2-mannosidase that trims Man9GlcNAc2 to Man8GlcNAc2 isomer B during N-glycan biosynthesis
description
1999 nî lūn-bûn
@nan
1999 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած
@hyw
1999 թվականի հոտեմբերին հրատարակված գիտական հոդված
@hy
1999年の論文
@ja
1999年学术文章
@wuu
1999年学术文章
@zh-cn
1999年学术文章
@zh-hans
1999年学术文章
@zh-my
1999年学术文章
@zh-sg
1999年學術文章
@yue
name
Cloning and expression of a sp ...... B during N-glycan biosynthesis
@ast
Cloning and expression of a sp ...... B during N-glycan biosynthesis
@en
Cloning and expression of a sp ...... B during N-glycan biosynthesis
@en-gb
Cloning and expression of a sp ...... B during N-glycan biosynthesis
@nl
type
label
Cloning and expression of a sp ...... B during N-glycan biosynthesis
@ast
Cloning and expression of a sp ...... B during N-glycan biosynthesis
@en
Cloning and expression of a sp ...... B during N-glycan biosynthesis
@en-gb
Cloning and expression of a sp ...... B during N-glycan biosynthesis
@nl
prefLabel
Cloning and expression of a sp ...... B during N-glycan biosynthesis
@ast
Cloning and expression of a sp ...... B during N-glycan biosynthesis
@en
Cloning and expression of a sp ...... B during N-glycan biosynthesis
@en-gb
Cloning and expression of a sp ...... B during N-glycan biosynthesis
@nl
P2860
P3181
P356
P1433
P1476
Cloning and expression of a sp ...... B during N-glycan biosynthesis
@en
P2093
A Herscovics
L O Tremblay
P2860
P304
P3181
P356
10.1093/GLYCOB/9.10.1073
P407
P577
1999-10-01T00:00:00Z