Interaction of Cap Z with actin. The NH2-terminal domains of the alpha 1 and beta subunits are not required for actin capping, and alpha 1 beta and alpha 2 beta heterodimers bind differentially to actin.
about
An order of magnitude faster AIP1-associated actin disruption than nucleation by the Arp2/3 complex in lamellipodiaCrystal structure of CapZ: structural basis for actin filament barbed end cappingDifferential localization and sequence analysis of capping protein beta-subunit isoforms of vertebratesCapzb2 interacts with beta-tubulin to regulate growth cone morphology and neurite outgrowthTargeted deletion of alpha-adducin results in absent beta- and gamma-adducin, compensated hemolytic anemia, and lethal hydrocephalus in miceA missense mutation in the Capza3 gene and disruption of F-actin organization in spermatids of repro32 infertile male miceActin turnover-dependent fast dissociation of capping protein in the dendritic nucleation actin network: evidence of frequent filament severing.Subunits of the Drosophila actin-capping protein heterodimer regulate each other at multiple levels.Thiolutin inhibits endothelial cell adhesion by perturbing Hsp27 interactions with components of the actin and intermediate filament cytoskeleton.F-actin, a model polymer for semiflexible chains in dilute, semidilute, and liquid crystalline solutions.Mutations in the Drosophila orthologs of the F-actin capping protein alpha- and beta-subunits cause actin accumulation and subsequent retinal degeneration.Muscle giants: molecular scaffolds in sarcomerogenesis.Actin capping protein alpha maintains vestigial-expressing cells within the Drosophila wing disc epitheliumDynamics of capping protein and actin assembly in vitro: uncapping barbed ends by polyphosphoinositides.Nebulin interacts with CapZ and regulates thin filament architecture within the Z-discMutational analysis of capping protein function in Saccharomyces cerevisiae.Overview of Single-Molecule Speckle (SiMS) Microscopy and Its Electroporation-Based Version with Efficient Labeling and Improved Spatiotemporal Resolution.
P2860
Q27350224-CF043287-B624-400F-90A2-88BFB540959AQ27640829-9AE66040-94F9-4CD1-B9F5-6670A20E5F94Q28239066-3252324C-7267-4575-8B65-3EB9AF9BAA3FQ28505608-37505BD8-C9D8-4E7A-9047-7FCE62C2C199Q28585644-DD270647-F769-4367-99EB-FCFB9CD98629Q28588250-DB6BE2FF-523F-427A-BD8F-880134F1EA83Q30480569-DF2C51E4-15A3-449C-BA5D-1E481D91FED3Q33560457-7D9188F2-97EF-4791-8587-55375554FE84Q33838914-3200A3CE-F6EB-431B-859E-2AE810767FF0Q34017105-DFF56F3B-36F8-446E-8471-3B24A18EEB90Q34586909-C5667323-DAEC-42B8-8371-6BBDA80DAA67Q34793699-9FC57130-7CE5-4DFC-A658-C4D5C4F49237Q34984873-D9083A80-2342-41B2-9950-3621AF1B5386Q36237502-E3A7F23E-E11E-47EA-96AC-A02722CB4C4FQ36631194-35D3F2E4-6AF7-42B6-A315-50FFA0D7E0D0Q37449811-72FBE24A-6232-407C-86B7-C7683FF4ED8CQ39419483-6CE084E9-2CD4-4CD5-A238-2BA83F5126A0
P2860
Interaction of Cap Z with actin. The NH2-terminal domains of the alpha 1 and beta subunits are not required for actin capping, and alpha 1 beta and alpha 2 beta heterodimers bind differentially to actin.
description
1994 nî lūn-bûn
@nan
1994年の論文
@ja
1994年論文
@yue
1994年論文
@zh-hant
1994年論文
@zh-hk
1994年論文
@zh-mo
1994年論文
@zh-tw
1994年论文
@wuu
1994年论文
@zh
1994年论文
@zh-cn
name
Interaction of Cap Z with acti ...... bind differentially to actin.
@en
type
label
Interaction of Cap Z with acti ...... bind differentially to actin.
@en
prefLabel
Interaction of Cap Z with acti ...... bind differentially to actin.
@en
P1476
Interaction of Cap Z with acti ...... s bind differentially to actin
@en
P2093
P304
P407
P577
1994-03-01T00:00:00Z