Misfolding and aggregation of newly synthesized proteins in the endoplasmic reticulum.
about
Importance of Arg-219 for correct biogenesis of alpha 1 homooligomeric glycine receptorsOrchestration of secretory protein folding by ER chaperonesEnvelopment of varicella-zoster virus: targeting of viral glycoproteins to the trans-Golgi networkHepatitis C virus glycoprotein folding: disulfide bond formation and association with calnexinThe oligomerization reaction of the Semliki Forest virus membrane protein subunitsProper maturation of the Japanese encephalitis virus envelope glycoprotein requires cosynthesis with the premembrane proteinMolecular architecture of the human sperm IZUMO1 and egg JUNO fertilization complexThe alphaviruses: gene expression, replication, and evolutionCo- and Post-Translational Protein Folding in the ERThe role of constant region carbohydrate in the assembly and secretion of human IgD and IgA1Loss of the oxidative stress sensor NPGPx compromises GRP78 chaperone activity and induces systemic diseaseAggresomes: a cellular response to misfolded proteinsN-linked oligosaccharides affect the enzymatic activity of CD39: diverse interactions between seven N-linked glycosylation sitesDomain-specific N-glycosylation of the membrane glycoprotein dipeptidylpeptidase IV (CD26) influences its subcellular trafficking, biological stability, enzyme activity and protein foldingThe complete general secretory pathway in gram-negative bacteriaA misfolded protein conformation is not a sufficient condition for in vivo glucosylation by the UDP-Glc:glycoprotein glucosyltransferase.Role of N-oligosaccharide endoplasmic reticulum processing reactions in glycoprotein folding and degradationIdentification of a trafficking determinant localized to the Kv1 potassium channel poreCharacterization of a foldase, protein disulfide isomerase A, in the protein secretory pathway of Aspergillus niger.How N-linked oligosaccharides affect glycoprotein folding in the endoplasmic reticulum.Conformational implications of asparagine-linked glycosylation.Formation of reversible disulfide bonds with the protein matrix of the endoplasmic reticulum correlates with the retention of unassembled Ig light chainsIdentification of 13 new mutations in the vasopressin-neurophysin II gene in 17 kindreds with familial autosomal dominant neurohypophyseal diabetes insipidusAn endoplasmic reticulum trafficking signal prevents surface expression of a voltage- and Ca2+-activated K+ channel splice variant.Posttranslational folding of vesicular stomatitis virus G protein in the ER: involvement of noncovalent and covalent complexes.Quality control in the secretory pathway: retention of a misfolded viral membrane glycoprotein involves cycling between the ER, intermediate compartment, and Golgi apparatusThe number and location of glycans on influenza hemagglutinin determine folding and association with calnexin and calreticulin.The UDP-Glc:Glycoprotein glucosyltransferase is essential for Schizosaccharomyces pombe viability under conditions of extreme endoplasmic reticulum stress.Early assembly step of a retroviral envelope glycoprotein: analysis using a dominant negative assay.Envelope glycoprotein interactions in coronavirus assemblyHepatitis B surface antigen assembles in a post-ER, pre-Golgi compartment.Specific interaction between the bovine papillomavirus E5 transforming protein and the beta receptor for platelet-derived growth factor in stably transformed and acutely transfected cellsDominant protein interactions that influence the pathogenesis of conformational diseases.Convergent modulation of Kv4.2 channel alpha subunits by structurally distinct DPPX and KChIP auxiliary subunits.Association with BiP and aggregation of class II MHC molecules synthesized in the absence of invariant chain.Calnexin fails to associate with substrate proteins in glucosidase-deficient cell lines.Site-directed removal of N-glycosylation sites in the bovine cation-dependent mannose 6-phosphate receptor: effects on ligand binding, intracellular targetting and association with binding immunoglobulin protein.Functional analysis of the glycosylation of murine acid sphingomyelinase.Glycan-dependent and -independent association of vesicular stomatitis virus G protein with calnexin.Carbohydrates facilitate correct disulfide bond formation and folding of rotavirus VP7
P2860
Q24304967-B6A4CE59-059A-4195-8701-0E3B6D104A3BQ27013551-96F1ECDD-39D9-4E2A-8B76-46EB33B75B39Q27480319-307B4B7A-7513-4536-AB4E-BD98909E8E1FQ27480329-05F1C489-35F0-49B5-8701-162B1F165026Q27482650-53377155-ECB3-430E-BD36-C5EA7C0CB6A6Q27486024-D9F8B983-9FDE-4F68-8796-1A027425256FQ27710997-4F6FDCC9-4FAE-41FE-82FF-A2F018009B08Q27860954-DB8AD25E-41D9-4B42-B0FF-69D70988A491Q28078736-38B7F789-E6F9-4DBE-BD49-4509CE666B95Q28218758-D39AF388-9879-4055-B6D4-808C4EE1DA0FQ28278638-216D19C3-BDDD-4B51-BB5B-7F42EF28447FQ28292275-C6490876-881F-4887-8610-A3DF7B8805A7Q28571719-BDDF6D3E-849B-4BF3-AB48-2C52F7806DE9Q28582112-FE18E760-8E6E-46BC-B5B0-F9BE2638B018Q29615298-0C90D081-2F85-45E2-97D1-244CC25398D1Q33889672-31A4BA82-6B88-4F9F-8D18-8BE488C26791Q33905603-2EFF43B0-1F26-4813-891B-B7DB02FD8C08Q33950345-3F5FDD14-338A-484F-8943-C25962F8E4ABQ33986656-1C779105-ACC5-4601-A80F-0CE8A643E3BBQ34441056-052A5DE8-E144-4986-A72A-F03831A171FFQ34805791-FC6029DD-814D-4A43-A28A-0BC5CC7535F4Q35848909-896F1D63-EB4D-42D1-BB53-0B57BFED754AQ35882453-64DF2808-8489-426D-B990-00F65EB44B59Q35971079-043D3323-23BF-4225-B050-AB1BAA84BF56Q36232426-59AC3E65-780A-46BB-B91E-7F4CED3C04C5Q36234402-914EE641-9116-4DE2-BA60-AC5BA2288C69Q36276590-97782105-F776-4AFE-8257-F31AF39306B0Q36288216-F0A7B905-D819-4B44-BD6A-ABF19D50D7D3Q36288363-B26F29F9-78A8-41B1-BE35-E36EE1AC0AD8Q36382749-B242CD7A-7BB7-46DA-A538-978CAEF8AEF2Q36531845-75E9B03D-B9C1-432C-93A4-256C2DBA0468Q36634049-ADDD1BDD-0C50-4C4E-AA4C-F790D96C27E4Q36966865-9ECFB0E9-F680-4422-92FE-31E62D7D9E84Q37322213-323C5883-9DAA-477F-BE16-86B5876ABB2CQ37628980-60B5036A-22F3-4DEA-891B-425EE0DC453FQ38289520-F7824716-4986-460C-94EC-B61F1D41DC63Q38314670-AFD56FDB-8FCB-4DBB-AAC1-E2E86340273AQ38350610-20589C5B-F235-47A6-ACD1-4E2F919DD051Q38356606-938838DB-7CBE-4BAF-9871-8F7C8C28E671Q39578370-EFD1828D-11CB-4F21-ADD5-D4BD4F0CC74D
P2860
Misfolding and aggregation of newly synthesized proteins in the endoplasmic reticulum.
description
1992 nî lūn-bûn
@nan
1992年の論文
@ja
1992年論文
@yue
1992年論文
@zh-hant
1992年論文
@zh-hk
1992年論文
@zh-mo
1992年論文
@zh-tw
1992年论文
@wuu
1992年论文
@zh
1992年论文
@zh-cn
name
Misfolding and aggregation of newly synthesized proteins in the endoplasmic reticulum.
@ast
Misfolding and aggregation of newly synthesized proteins in the endoplasmic reticulum.
@en
type
label
Misfolding and aggregation of newly synthesized proteins in the endoplasmic reticulum.
@ast
Misfolding and aggregation of newly synthesized proteins in the endoplasmic reticulum.
@en
prefLabel
Misfolding and aggregation of newly synthesized proteins in the endoplasmic reticulum.
@ast
Misfolding and aggregation of newly synthesized proteins in the endoplasmic reticulum.
@en
P2860
P356
P1476
Misfolding and aggregation of newly synthesized proteins in the endoplasmic reticulum.
@en
P2093
A Helenius
T Marquardt
P2860
P304
P356
10.1083/JCB.117.3.505
P407
P577
1992-05-01T00:00:00Z