The 110-kD protein-calmodulin complex of the intestinal microvillus (brush border myosin I) is a mechanoenzyme.
about
Shigella flexneri enters human colonic Caco-2 epithelial cells through the basolateral poleIdentification, characterization and cloning of myr 1, a mammalian myosin-IMyosin-1a powers the sliding of apical membrane along microvillar actin bundles.Control of cell membrane tension by myosin-I.Myosin VI: an innovative motor that challenged the swinging lever arm hypothesisActin cores of hair-cell stereocilia support myosin motility.Measuring orientation of actin filaments within a cell: orientation of actin in intestinal microvilli.Non-muscle myosins in tumor progression, cancer cell invasion, and metastasis.WASp is required for the correct temporal morphogenesis of rhabdomere microvilli.Interspecies comparison of calmodulin binding proteins throughout the gastrointestinal tract: comparison with human colon adenomas and adenocarcinomas.The enterocyte microvillus is a vesicle-generating organelleThe co-workers of actin filaments: from cell structures to signals.Partial deduced sequence of the 110-kD-calmodulin complex of the avian intestinal microvillus shows that this mechanoenzyme is a member of the myosin I familyCalcium regulation of myosin-I tension sensingCharacterization of intestinal microvillar membrane disks: detergent-resistant membrane sheets enriched in associated brush border myosin I (110K-calmodulin).Calmodulin dissociation regulates brush border myosin I (110-kD-calmodulin) mechanochemical activity in vitro.Identification of actin filaments in the rhabdomeral microvilli of Drosophila photoreceptors.Binding of brush border myosin I to phospholipid vesicles.Calcium-calmodulin and regulation of brush border myosin-I MgATPase and mechanochemistryMammalian myosin I alpha, I beta, and I gamma: new widely expressed genes of the myosin I family.Do unconventional myosins exert functions in dynamics of membrane compartments?myoA of Aspergillus nidulans encodes an essential myosin I required for secretion and polarized growthMyosin-I moves actin filaments on a phospholipid substrate: implications for membrane targeting.Localization of capping protein in chicken epithelial cells by immunofluorescence and biochemical fractionation.Purification and characterization of a mammalian myosin IRegulation and control of myosin-I by the motor and light chain-binding domains.A sialoglycoprotein complex linked to the microvillus cytoskeleton acts as a receptor for pilus (AF/R1) mediated adhesion of enteropathogenic Escherichia coli (RDEC-1) in rabbit small intestine.Zipper protein, a B-G protein with the ability to regulate actin/myosin 1 interactions in the intestinal brush border.The unconventional myosin encoded by the myoA gene plays a role in Dictyostelium motility.Multiple actin-based motor genes in Dictyostelium.Actin microfilaments play a critical role in endocytosis at the apical but not the basolateral surface of polarized epithelial cells.Golgi-derived vesicles from developing epithelial cells bind actin filaments and possess myosin-I as a cytoplasmically oriented peripheral membrane proteinActin binding to lipid-inserted alpha-actinin.A second isoform of chicken brush border myosin I contains a 29-residue inserted sequence that binds calmodulin.
P2860
Q24646749-BB9D12CC-613B-4CFA-9325-3532B54524C1Q24674123-F13A17FD-5C2B-4213-B7DE-DB62E066AF79Q30480441-3DED5EFF-C08E-45CF-8EEE-61E24FB8041FQ30489048-808B025B-1D92-4B70-AB52-FBF1CD78FB3CQ33809113-E85E82F0-8BE2-4751-8326-1EA42939B0C0Q33882585-FE8CE77F-D3E5-48A8-95F5-0250A9E5E9BFQ34019385-16543A1B-C518-4935-9537-7A1911089073Q34207052-191BC6B9-C880-4ED7-A34E-245CFA39355DQ34292762-365A62FC-2289-4837-B76D-75982B24F8ECQ34395584-A9A24D93-AC59-4BF7-A45A-7C6D4519FE72Q34989756-C5153420-A310-4EF4-930A-BB75899E8387Q35887294-5A0E5724-D912-4A6E-873A-5E0AAD671E87Q35922823-32960B29-11F1-41BE-8269-1A522CA175AEQ36047360-2E7A9ABD-9717-4A7D-8FAF-8EC4EBF24E7EQ36221523-E0DC69E5-A6A3-4DB0-AA64-3FE8EC99A8FFQ36222736-9896550B-219E-4D74-932F-81DEE0374B92Q36223132-B9F35657-79A0-471A-B6E4-EC6BDCE71816Q36223375-7FDB3122-92F8-4ED8-85F5-57936940318CQ36232765-C70C3123-5861-4341-8506-6CFAE4098C88Q36233141-D628A394-E465-4354-9C90-3947D0117BC8Q36360098-5C6BBE63-BF1B-42C5-A696-0AD0798121DCQ36382420-797B169E-5C74-447C-9787-AB1CF1E81223Q36530778-1390B668-5112-4F72-AD9C-AD397CDEAC8DQ36533207-4EA9EA64-7B2D-463E-9182-6B145CFAF15CQ36783029-E188BFBE-EE74-4C7E-9CC3-36BB94C900C8Q38064119-31DD2EA0-ED08-48CC-9CAF-D93576C3CFE5Q38332698-68779AC9-FBE1-400A-9D6C-D4CFAC193C9AQ38359097-D4A59E7C-ED5F-40C5-874E-F4FA130A08B3Q40365389-EC332BC2-9A8E-442D-A19D-5C87951F94BCQ40640770-62C29D20-3817-4847-B200-1679DCED7B7CQ41576870-5718D812-0C6E-4B84-8D8D-2E4C16D93D5BQ42769452-DBF925D6-97AD-4BAB-83A5-363CAD336F84Q43006181-0913D551-4961-4730-B093-55B1279953A5Q54711253-B27FF18F-36B8-4B78-8984-1B4C3A9EF568
P2860
The 110-kD protein-calmodulin complex of the intestinal microvillus (brush border myosin I) is a mechanoenzyme.
description
1989 nî lūn-bûn
@nan
1989年の論文
@ja
1989年論文
@yue
1989年論文
@zh-hant
1989年論文
@zh-hk
1989年論文
@zh-mo
1989年論文
@zh-tw
1989年论文
@wuu
1989年论文
@zh
1989年论文
@zh-cn
name
The 110-kD protein-calmodulin ...... myosin I) is a mechanoenzyme.
@ast
The 110-kD protein-calmodulin ...... myosin I) is a mechanoenzyme.
@en
type
label
The 110-kD protein-calmodulin ...... myosin I) is a mechanoenzyme.
@ast
The 110-kD protein-calmodulin ...... myosin I) is a mechanoenzyme.
@en
prefLabel
The 110-kD protein-calmodulin ...... myosin I) is a mechanoenzyme.
@ast
The 110-kD protein-calmodulin ...... myosin I) is a mechanoenzyme.
@en
P2860
P356
P1476
The 110-kD protein-calmodulin ...... myosin I) is a mechanoenzyme.
@en
P2093
M S Mooseker
T R Coleman
P2860
P304
P356
10.1083/JCB.108.6.2395
P407
P577
1989-06-01T00:00:00Z