Russell bodies: a general response of secretory cells to synthesis of a mutant immunoglobulin which can neither exit from, nor be degraded in, the endoplasmic reticulum.
about
Sequential steps and checkpoints in the early exocytic compartment during secretory IgM biogenesisAlternative splicing generates secretory isoforms of human CD1Thiol-mediated protein retention in the endoplasmic reticulum: the role of ERp44BiP/Kar2p serves as a molecular chaperone during carboxypeptidase Y folding in yeastHigh data output and automated 3D correlative light-electron microscopy method.Iris crystals in chronic uveitis.Aggresomes and Russell bodies. Symptoms of cellular indigestion?The role of UDP-Glc:glycoprotein glucosyltransferase 1 in the maturation of an obligate substrate prosaposin.Selective protein degradation in the yeast exocytic pathway.How N-linked oligosaccharides affect glycoprotein folding in the endoplasmic reticulum.A dynamic study of protein secretion and aggregation in the secretory pathway.Endoplasmic reticulum: a dynamic patchwork of specialized subregionsRussell body gastritis associated with Helicobacter pylori infection: a case reportA striking quality control subcompartment in Saccharomyces cerevisiae: the endoplasmic reticulum-associated compartment.Formation of reversible disulfide bonds with the protein matrix of the endoplasmic reticulum correlates with the retention of unassembled Ig light chainsRussell body phenotype is preferentially induced by IgG mAb clones with high intrinsic condensation propensity: relations between the biosynthetic events in the ER and solution behaviors in vitro.Posttranslational folding of vesicular stomatitis virus G protein in the ER: involvement of noncovalent and covalent complexes.A study of the effects of altering the sites for N-glycosylation in alpha-1-proteinase inhibitor variants M and S.Biochemical nature of Russell Bodies.Dynamic association of proteasomal machinery with the centrosome.Protein quality control: the who's who, the where's and therapeutic escapes.Degradation of aggrecan precursors within a specialized subcompartment of the chicken chondrocyte endoplasmic reticulum.Golgi retention of a trans-Golgi membrane protein, galactosyltransferase, requires cysteine and histidine residues within the membrane-anchoring domainA different sort of Mott cellThe endoplasmic reticulum remains functionally connected by vesicular transport after its fragmentation in cells expressing Z-α1-antitrypsin.Arginine vasopressin neuronal loss results from autophagy-associated cell death in a mouse model for familial neurohypophysial diabetes insipidus.The formation, function and fate of protein storage compartments in seeds.Endoplasmic reticulum retention, degradation, and aggregation of olfactory G-protein coupled receptors.Roles of N-glycans in the polymerization-dependent aggregation of mutant Ig-μ chains in the early secretory pathway.Rare Gastric Lesions Associated with Helicobacter pylori Infection: A Histopathological Review.Inhibition of endoplasmic reticulum (ER)-to-Golgi transport induces relocalization of binding protein (BiP) within the ER to form the BiP bodies.The differential effects of dithiothreitol and 2-mercaptoethanol on the secretion of partially and completely assembled immunoglobulins suggest that thiol-mediated retention does not take place in or beyond the Golgi.The luminal part of the murine cytomegalovirus glycoprotein gp40 catalyzes the retention of MHC class I molecules.Overexpression of calsequestrin in L6 myoblasts: formation of endoplasmic reticulum subdomains and their evolution into discrete vacuoles where aggregates of the protein are specifically accumulated.ERAD of proteins containing aberrant transmembrane domains requires ubiquitylation of cytoplasmic lysine residues.Quality control of ER synthesized proteins: an exposed thiol group as a three-way switch mediating assembly, retention and degradation.HLA-DR beta chains enter into an aggregated complex containing GRP-78/BiP prior to their degradation by the pre-Golgi degradative pathway.Aggregates, crystals, gels, and amyloids: intracellular and extracellular phenotypes at the crossroads of immunoglobulin physicochemical property and cell physiology.COPII machinery cooperates with ER-localized Hsp40 to sequester misfolded membrane proteins into ER-associated compartmentsFunctional Characterization of DNA Methylation in the Oligodendrocyte Lineage
P2860
Q24292949-D2756019-CC08-4945-90B5-7275024B75C4Q24561530-FA0A9B7B-F058-4D12-B86B-E5883766E3EEQ24672358-41BFA1EE-7133-496B-8C47-091829E682EAQ28303811-5D82B1A1-3B20-42B4-93D5-10056A31D95DQ30485811-91DAE3B8-48CE-49F1-916A-707BE3F4DC5FQ33643025-B109F852-2C44-4CA7-BDBB-E14BD8EDAACDQ33757033-FAF612B3-A992-493C-B212-2C7012D18041Q33886809-09F94ECF-1454-4155-AE37-D7DADE6B4BECQ34438486-A2620C35-C62D-413F-8C98-317129A9B2D8Q34441056-89090C16-A8E0-4563-84C3-E3F3F3D098BDQ35298457-AA7F71AD-47DA-4017-9DC7-55A9EB8A0B93Q35465738-4B3B136C-8DCF-466F-ABC3-9E0DFED6719EQ35770455-A35D36FC-CD8E-4633-9F7B-CC4666872B76Q35803161-EFABD568-6B11-4448-98C1-80DC27AC58EAQ35848909-1844AF80-02EE-4A3F-A5FB-55312D0BBCD2Q36212910-A4DFD5BD-541E-4FFD-BEA7-DFB75F9F890FQ36232426-C39406BA-10CC-49B9-97FB-5B722EAD3FF6Q36278201-454155D4-7382-4688-8EFB-BB3FF0DBE319Q36292351-4A73FD14-625B-4A40-AEE8-825BE2466E0DQ36342153-3073F86E-2877-4E3D-935B-8C595C1028C7Q36432134-2B045F93-0D7B-4854-8A2C-B8B4B8EBC54CQ36805689-6A2A1B83-4D66-4F92-A021-CD521C077E70Q37002762-1C3B3745-57A2-45DA-93DD-30E46CFC8527Q37335544-B58F4909-C734-4E5E-AC2A-181275D2EF54Q37403714-9BF6C552-563C-48EB-8197-8A70B930CF33Q37680208-19CC9756-7E5C-44FE-A9FF-5404627BB7FDQ37879991-80DC425B-A051-4FF1-80DD-F4FE42CFE13BQ38354536-54FD8244-2F93-46E8-A8C8-AAE645E220CBQ38981329-7A2F12A6-7D4E-401F-AE5C-4D5FC79FEDEAQ39358514-49C86DF0-ADA9-434B-8C94-2E04D3C53787Q40366396-79056B28-4687-45B0-A20F-58C30645FD21Q40366520-9DA27D0D-0E44-4F43-A67D-0271F520C45EQ40387185-9C947082-BA41-4CA2-8B88-84A56242A5B8Q40387730-5E0E5DCB-620D-4D8C-9990-D6C3751B39E7Q40455975-A4D781B4-0484-42D1-A902-B09707EB23CBQ40875183-CCD5BAE3-8F5D-4598-B627-9DE25BBC1AB8Q41370939-759F65BE-FEBC-4E07-88DA-210720AB1B44Q41831737-8A87A4EE-5CB4-46B2-855D-A479FDA8D2D8Q41881232-EACFA75E-8A6C-45EB-861D-3F5BBDB505BEQ42067835-9E6707B3-6349-4830-A511-FD57E893DFA0
P2860
Russell bodies: a general response of secretory cells to synthesis of a mutant immunoglobulin which can neither exit from, nor be degraded in, the endoplasmic reticulum.
description
1991 nî lūn-bûn
@nan
1991年の論文
@ja
1991年論文
@yue
1991年論文
@zh-hant
1991年論文
@zh-hk
1991年論文
@zh-mo
1991年論文
@zh-tw
1991年论文
@wuu
1991年论文
@zh
1991年论文
@zh-cn
name
Russell bodies: a general resp ...... in, the endoplasmic reticulum.
@en
type
label
Russell bodies: a general resp ...... in, the endoplasmic reticulum.
@en
prefLabel
Russell bodies: a general resp ...... in, the endoplasmic reticulum.
@en
P2093
P2860
P356
P1476
Russell bodies: a general resp ...... in, the endoplasmic reticulum.
@en
P2093
P2860
P304
P356
10.1083/JCB.115.4.983
P407
P577
1991-11-01T00:00:00Z