Redistribution of membrane proteins in isolated mouse intestinal epithelial cells.
about
Methods for the study of ionic currents and Ca2+-signals in isolated colonic cryptsBiochemical localization of hepatic surface-membrane Na+,K+-ATPase activity depends on membrane lipid fluidity.Viruses budding from either the apical or the basolateral plasma membrane domain of MDCK cells have unique phospholipid compositions.Ischemia induces partial loss of surface membrane polarity and accumulation of putative calcium ionophores.Amino acids stimulate cholecystokinin release through the Ca2+-sensing receptorPerturbation of podocyte plasma membrane domains in experimental nephrosis. A lectin-binding and freeze-fracture studyGalactose-specific recognition system of mammalian liver: receptor distribution on the hepatocyte cell surface.Cell surface distribution and intracellular fate of asialoglycoproteins: a morphological and biochemical study of isolated rat hepatocytes and monolayer cultures.Assembly of enveloped viruses in Madin-Darby canine kidney cells: polarized budding from single attached cells and from clusters of cells in suspension.A domain-specific marker for the hepatocyte plasma membrane: localization of leucine aminopeptidase to the bile canalicular domain.Diffusion rates of cell surface antigens of mouse-human heterokaryons. III. Regulation of lateral diffusion rates by calcium ionsStudies on the development and maintenance of epithelial cell surface polarity with monoclonal antibodies.A domain-specific marker for the hepatocyte plasma membrane. II. Ultrastructural localization of leucine aminopeptidase to the bile canalicular domain of isolated rat liver plasma membranesMicrodomains of distinctive glycoprotein composition in the kidney proximal tubule brush border.Characterization of a 36,000-dalton protein from the surface of Madin-Darby canine kidney cells involved in cell attachment and spreadingEffects of cell density and extracellular matrix on the lateral diffusion of major histocompatibility antigens in cultured fibroblastsFormation of the apical pole of epithelial (Madin-Darby canine kidney) cells: polarity of an apical protein is independent of tight junctions while segregation of a basolateral marker requires cell-cell interactions.Modulation of the expression of an apical plasma membrane protein of Madin-Darby canine kidney epithelial cells: cell-cell interactions control the appearance of a novel intracellular storage compartment.Histamine type I receptor occupancy increases endothelial cytosolic calcium, reduces F-actin, and promotes albumin diffusion across cultured endothelial monolayers.Development of tight junctions de novo in the mouse early embryo: control of assembly of the tight junction-specific protein, ZO-1The polarized distribution of an apical cell surface glycoprotein is maintained by interactions with the cytoskeleton of Madin-Darby canine kidney cells.Selective anchoring in the specific plasma membrane domain: a role in epithelial cell polarity.Membrane domains of intestinal epithelial cells: distribution of Na+,K+-ATPase and the membrane skeleton in adult rat intestine during fetal development and after epithelial isolation.Heparan sulfate and syndecan-1 are essential in maintaining murine and human intestinal epithelial barrier functionA requirement for membrane-associated phospholipase A2 in platelet cytotoxicity activated by receptors for immunoglobulin G and complement.Maxi K+ channels and their relationship to the apical membrane conductance in Necturus gallbladder epithelium.Voltage- and time-dependent K+ channel currents in the basolateral membrane of villus enterocytes isolated from guinea pig small intestine.Endocytosis via coated pits mediated by glycoprotein receptor in which the cytoplasmic tail is replaced by unrelated sequencesRecent progress on lipid lateral heterogeneity in plasma membranes: From rafts to submicrometric domainsLocalization of sialic acid in kidney glomeruli: regionalization in the podocyte plasma membrane and loss in experimental nephrosis.Cholesterol segregates into submicrometric domains at the living erythrocyte membrane: evidence and regulation.The molecular and cellular basis of preimplantation mouse development.Ischemia-induced loss of epithelial polarity. Role of the tight junction.Different modes of internalization of proteins associated with adhaerens junctions and desmosomes: experimental separation of lateral contacts induces endocytosis of desmosomal plaque material.Endogenous sphingomyelin segregates into submicrometric domains in the living erythrocyte membrane.Actin microfilaments play a critical role in endocytosis at the apical but not the basolateral surface of polarized epithelial cells.Development of cell surface polarity in the epithelial Madin-Darby canine kidney (MDCK) cell line.A high-resolution, fluorescence-based method for localization of endogenous alkaline phosphatase activity.
P2860
Q24797273-E6C38277-7527-46F3-8561-7B87C54F9137Q33672150-750C82D5-B65C-4FB1-92D0-E512294E7F2DQ34055378-F6A29964-6887-4AB2-A307-49D3CCC2C11CQ34568030-60621573-B223-49DC-82A1-6F1BCD72ACEAQ34783968-7DA36E68-61C4-478F-BF38-FB74F1687F61Q35858146-12DB21A3-8929-4A8F-A29F-4E75F8B9A619Q36205271-391C8ED4-6A9E-481C-BDB1-2BA527AFFCF1Q36205775-2AD09CED-87DB-496D-ACD6-8F2EFDA080E9Q36207208-4EDC1146-D5E5-424A-9E45-C97539FA7ACAQ36207387-54AA5324-2E79-4246-B770-7CE17526B4ECQ36209457-9E9C489A-E12A-47C9-A71C-601D50697A3CQ36210403-3610F9C8-399E-4942-AA97-74C52DFD8E4DQ36210623-481689D4-AC2A-467F-8370-15E3402462CFQ36210654-5AC22418-71B3-48C6-8827-BFBE34D1C7D3Q36212268-BB2F3BEB-0B4D-4480-8FAF-C9316A9945EAQ36212998-6D487D44-9C95-441C-94DE-118B20B3CD85Q36216030-E525CBF2-FCB1-4D26-B412-86643C14E785Q36216068-CED48FA5-E8F7-4EB4-92B3-67F4B68095B8Q36216693-4287EECC-5208-486E-AE6C-FD4EA7A0C572Q36220478-242AC961-C92C-4B0A-8D90-CB783AF0F804Q36220951-29E3F632-6F3B-46CD-930E-6942D1FD565EQ36221176-A540FADA-84C6-4DC7-9B2B-3769059911E7Q36221759-9570815A-6957-4087-B237-1C4AB583624CQ36227233-5757295A-3CBE-4E60-A434-4D77E9979F4AQ36361569-7B14DB9F-B42B-4F28-8063-BD071054EC3DQ36410528-D6240C5F-469E-43AF-941D-16ABC199AB89Q36411466-18B79579-D211-4FD5-9601-3F64426A476FQ36737272-B79A5532-A7A5-49CC-8457-D42D9C10B67FQ36854004-41D34310-0FE2-4F0D-BDE9-2CD95AFD0812Q37539840-4AFF7208-2D7E-435D-AACD-3FB20598F3CFQ38863796-86C0DC34-7E77-45EA-AA82-3A74B0A4CC09Q40319530-B066B517-DE20-4E31-ABA1-7EE6D03C8940Q40511743-6833DE73-CC92-402C-A256-39459A20AF60Q41323428-3CF0D37A-6917-4B73-9B08-F7CE16B98802Q41517934-CC522441-91B6-497A-9BEE-701D549070A6Q41576870-6EB7DD9A-C3A4-41D5-B101-AC93932CD27CQ41584376-AE73A380-94D7-4F42-B245-C16FD6E12D9FQ50516067-810549B1-9BCD-464A-9086-D2595F2F115C
P2860
Redistribution of membrane proteins in isolated mouse intestinal epithelial cells.
description
1980 nî lūn-bûn
@nan
1980年の論文
@ja
1980年論文
@yue
1980年論文
@zh-hant
1980年論文
@zh-hk
1980年論文
@zh-mo
1980年論文
@zh-tw
1980年论文
@wuu
1980年论文
@zh
1980年论文
@zh-cn
name
Redistribution of membrane proteins in isolated mouse intestinal epithelial cells.
@ast
Redistribution of membrane proteins in isolated mouse intestinal epithelial cells.
@en
type
label
Redistribution of membrane proteins in isolated mouse intestinal epithelial cells.
@ast
Redistribution of membrane proteins in isolated mouse intestinal epithelial cells.
@en
prefLabel
Redistribution of membrane proteins in isolated mouse intestinal epithelial cells.
@ast
Redistribution of membrane proteins in isolated mouse intestinal epithelial cells.
@en
P2093
P2860
P356
P1476
Redistribution of membrane proteins in isolated mouse intestinal epithelial cells.
@en
P2093
P2860
P304
P356
10.1083/JCB.86.3.849
P407
P577
1980-09-01T00:00:00Z