Actin in the brush-border of epithelial cells of the chicken intestine.
about
Actin antibody: the specific visualization of actin filaments in non-muscle cellsPurification of an 80,000-dalton protein that is a component of the isolated microvillus cytoskeleton, and its localization in nonmuscle cellsCordon Bleu serves as a platform at the basal region of microvilli, where it regulates microvillar length through its WH2 domains.Contraction of isolated brush borders from the intestinal epithelium.Organization of an actin filament-membrane complex. Filament polarity and membrane attachment in the microvilli of intestinal epithelial cells.Dynamic assembly of surface structures in living cellsProteins of the kidney microvillus membrane. Identification of subunits after sodium dodecylsullphate/polyacrylamide-gel electrophoresis.The terminal web of the duodenal enterocyte.The form and arrangement of microtubules: an historical, primarily morphological, review.The origin and distribution of membrane-bound vesicles associated with the brush border of chick intestinal mucosa.Immuno-electron microscopical localisation of alpha-actinin and actin in microvilli of prostatic epithelial cells.WASp is required for the correct temporal morphogenesis of rhabdomere microvilli.Cytochalasin B, its interaction with actin and actomyosin from muscle (cell movement-microfilaments-rabbit striated muscle).Patterns of organization of actin and myosin in normal and transformed cultured cellsHuman smooth muscle autoantibody. Its identification as antiactin antibody and a study of its binding to "nonmuscular" cells.The contractile process in the ciliate, Stentor coeruleus. I. The role of microtubules and filaments.Microfilaments in Chaos carolinensis. Membrane association, distribution, and heavy meromyosin binding in the glycerinated cell.The distribution, ultrastructure, and chemistry of microfilaments in cultured chick embryo fibroblastsMicrofilaments in epidermal cancer cellsStudies of muscle proteins in embryonic myocardial cells of cardiac lethal mutant mexican axolotls (Ambystoma mexicanum) by use of heavy meromyosin binding and sodium dodecyl sulfate polyacrylamide gel electrophoresis.Brush border motility. Microvillar contraction in triton-treated brush borders isolated from intestinal epitheliumActin filament-membrane attachment: are membrane particles involved?The contractile basis of ameboid movement. II. Structure and contractility of motile extracts and plasmalemma-ectoplasm ghosts.Actin filaments in sensory hairs of inner ear receptor cells.Synthesis of plasmalemmal glycoproteins in intestinal epithelial cells. Separation of Golgi membranes from villus and crypt cell surface membranes; glycosyltransferase activity of surface membrane.Filamin concentration in cleavage furrow and midbody region: frequency of occurrence compared with that of alpha-actinin and myosin.Regulation of microvillus structure: calcium-dependent solation and cross-linking of actin filaments in the microvilli of intestinal epithelial cells.The polymerization of actin: its role in the generation of the acrosomal process of certain echinoderm sperm.The polymerization of actin. III. Aggregates of nonfilamentous actin and its associated proteins: a storage form of actin.Brush-border alpha-actinin? Comparison of two proteins of the microvillus core with alpha-actinin by two-dimensional peptide mapping.Calcium-regulated cooperative binding of the microvillar 110K-calmodulin complex to F-actin: formation of decorated filaments.Reassociation of microvillar core proteins: making a microvillar core in vitro.Identification of actin filaments in the rhabdomeral microvilli of Drosophila photoreceptors.Morphological changes in liposomes caused by polymerization of encapsulated actin and spontaneous formation of actin bundles.Villin: the major microfilament-associated protein of the intestinal microvillus.Food grade titanium dioxide disrupts intestinal brush border microvilli in vitro independent of sedimentation.Transient opening of brush border membrane vesicles in alkaline media: preservation of D-glucose transport after removal of extrinsic proteins.[Microvilli membrane proteins from dog enterocytes]Synthesis of myosin heavy and light chains in muscle cultures.Actin and myosin and cell movement.
P2860
Q24620539-3EA2FD90-94B4-4E0B-AC73-0C7B982DD0FFQ24681337-3AE79416-4962-45E3-88E3-1AE076EAF980Q30009349-06FFA4BE-BF72-4962-9F29-6702ADE42C89Q30442451-17E836B9-CD65-4651-AB0B-767BAE88E8FCQ30442456-AD405E85-6BBF-443B-B50C-5F82D7AF9914Q30477916-AEF65AEA-7A01-4C65-B1A3-F1BED9D8D589Q30988587-2E276023-F531-4259-8A95-6BC47D302749Q33882425-8112FC0C-B272-4A13-9FE1-09EBD33D5FECQ34019778-A209FD4C-C5C4-4FC0-B1C8-2B32A18A755FQ34039732-7CAD2F0C-EB5B-40FF-9D7D-BE8638F50322Q34091391-AD2A5DCA-F71D-4823-96C1-F3849EB2337FQ34292762-8185A152-0C3E-4CCA-A47A-4503DF7ACBFEQ34689547-A9FEE3B5-F310-4998-B01D-2C2581C809CEQ35073060-5DFB4B73-DDA5-4B16-B9F1-8B0711649289Q35864657-131030F5-A867-42B2-817C-7B875D5B5F46Q36195155-C571B7D3-8E45-4E1F-ABEE-45F04E1C478DQ36195313-FBA52AF3-A3DD-4D4C-9CB1-8A0BFC58FFEDQ36195457-BCB4644C-0580-46FF-9700-DE1BF9BC6FBBQ36195890-35834116-CE30-4299-93D1-9B99B8FD91CEQ36197718-6C7ECBF6-DE4B-4299-BE66-CF39BA7282C1Q36198132-35CBD983-453B-4057-9897-7AB82E753B5EQ36198136-51864E8D-B62B-409A-94CD-81C5E4703D4CQ36198351-74310D8B-A362-441F-A3BE-F59A96835655Q36198818-7B05992F-344A-4BD9-AD74-284B1C6EE915Q36199676-1362B2FC-92EC-43B9-B08F-DAA33CA7E958Q36201872-AC270BA2-E61E-475A-95D0-E45E26269ED8Q36202165-6FC75225-436E-4FA4-B2BE-4826EFA5283BQ36202329-E86FD881-BC70-4D7C-B19B-81E443ABD01FQ36202484-BE947C61-14C9-4402-B86F-33F4F03545F7Q36203645-8CFC6711-1A7B-413B-983F-A596EB775E4BQ36218048-E96900D0-4E7D-49AA-BA59-5B3C44BE6989Q36220054-6A9EB079-1427-442D-B96A-53FE53881723Q36223132-CC6B26F7-3BB4-410A-A863-E9521D78C312Q37328277-1E45F84C-4125-45FE-9028-F815F3AD7BEEQ37330654-8D0E5719-0528-48B2-889E-77E63667415EQ38996101-A8F52F25-4D1C-4DCD-9FA5-82AAE7CC5ED5Q39274890-34B754C5-A46B-4094-8161-6172F0109BDFQ39452765-9E0A20FC-50AC-4FE0-8176-CF6DDEB33E69Q39750840-40D1DA0E-D06F-40E7-ABBF-8A048DE90522Q39887629-DE8A8400-5F37-456A-AE2F-786392DE1C13
P2860
Actin in the brush-border of epithelial cells of the chicken intestine.
description
article científic
@ca
article scientifique
@fr
articolo scientifico
@it
artigo científico
@pt
bilimsel makale
@tr
scientific article published on October 1971
@en
vedecký článok
@sk
vetenskaplig artikel
@sv
videnskabelig artikel
@da
vědecký článek
@cs
name
Actin in the brush-border of epithelial cells of the chicken intestine.
@en
Actin in the brush-border of epithelial cells of the chicken intestine.
@nl
type
label
Actin in the brush-border of epithelial cells of the chicken intestine.
@en
Actin in the brush-border of epithelial cells of the chicken intestine.
@nl
prefLabel
Actin in the brush-border of epithelial cells of the chicken intestine.
@en
Actin in the brush-border of epithelial cells of the chicken intestine.
@nl
P2860
P356
P1476
Actin in the brush-border of epithelial cells of the chicken intestine.
@en
P2093
P2860
P304
P356
10.1073/PNAS.68.10.2611
P407
P577
1971-10-01T00:00:00Z