A nonerythroid isoform of protein 4.1R interacts with the nuclear mitotic apparatus (NuMA) protein
about
GAKIN, a novel kinesin-like protein associates with the human homologue of the Drosophila discs large tumor suppressor in T lymphocytesGAS41, a highly conserved protein in eukaryotic nuclei, binds to NuMAProtein 4.1 R-135 interacts with a novel centrosomal protein (CPAP) which is associated with the gamma-tubulin complexA new spectrin, beta IV, has a major truncated isoform that associates with promyelocytic leukemia protein nuclear bodies and the nuclear matrixSpectrin and ankyrin-based pathways: metazoan inventions for integrating cells into tissuesIdentification of a novel microtubule-destabilizing motif in CPAP that binds to tubulin heterodimers and inhibits microtubule assemblyA nonerythroid isoform of protein 4.1R interacts with components of the contractile apparatus in skeletal myofibersFormation of spindle poles by dynein/dynactin-dependent transport of NuMAFRMD3 gene: its role in diabetic kidney disease. A narrative reviewAnd the dead shall rise: actin and myosin return to the spindleCharacterization of the interaction between protein 4.1R and ZO-2. A possible link between the tight junction and the actin cytoskeletonThe prototypical 4.1R-10-kDa domain and the 4.1g-10-kDa paralog mediate fodrin-actin complex formationbeta III spectrin binds to the Arp1 subunit of dynactinProtein 4.1N is required for translocation of inositol 1,4,5-trisphosphate receptor type 1 to the basolateral membrane domain in polarized Madin-Darby canine kidney cellsThe LFA-1-associated molecule PTA-1 (CD226) on T cells forms a dynamic molecular complex with protein 4.1G and human discs largeThe protein 4.1, ezrin, radixin, moesin (FERM) domain of Drosophila Coracle, a cytoplasmic component of the septate junction, provides functions essential for embryonic development and imaginal cell proliferationRegulated Fox-2 isoform expression mediates protein 4.1R splicing during erythroid differentiationNMR characterisation of the minimal interacting regions of centrosomal proteins 4.1R and NuMA1: effect of phosphorylationNuMA interacts with phosphoinositides and links the mitotic spindle with the plasma membrane.Cortical dynein and asymmetric membrane elongation coordinately position the spindle in anaphaseMitotic regulation of protein 4.1R involves phosphorylation by cdc2 kinaseBrain proteins interacting with the tetramerization region of non-erythroid alpha spectrin.An internal ribosome entry site element directs the synthesis of the 80 kDa isoforms of protein 4.1R.Inositol trisphosphate receptor Ca2+ release channels.Properties of the C-terminal domain of 4.1 proteins.Re-examination of the mechanisms regulating nuclear inositol lipid metabolism.Automated local bright feature image analysis of nuclear protein distribution identifies changes in tissue phenotype.Structural protein 4.1R is integrally involved in nuclear envelope protein localization, centrosome-nucleus association and transcriptional signaling.ICln: a new regulator of non-erythroid 4.1R localisation and functionProtein 4.1R links E-cadherin/beta-catenin complex to the cytoskeleton through its direct interaction with beta-catenin and modulates adherens junction integrity.Hereditary haemolytic anaemias: unexpected sequelae of mutations in the genes for erythroid membrane skeletal proteins.Activation of Stat3 in endothelial cells following hypoxia-reoxygenation is mediated by Rac1 and protein Kinase C.Downregulation of protein 4.1R, a mature centriole protein, disrupts centrosomes, alters cell cycle progression, and perturbs mitotic spindles and anaphase.The C terminus of the nuclear protein NuMA: phylogenetic distribution and structure.PIKE GTPase are phosphoinositide-3-kinase enhancers, suppressing programmed cell death.The N-terminal 209-aa domain of high molecular-weight 4.1R isoforms abrogates 4.1R targeting to the nucleus.Chromosomal instability and cytoskeletal defects in oral cancer cells.Inhibition of protein 4.1 R and NuMA interaction by mutagenization of their binding-sites abrogates nuclear localization of 4.1 R.A CH domain-containing N terminus in NuMA?Protein 4.1R Influences Myogenin Protein Stability and Skeletal Muscle Differentiation.
P2860
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P2860
A nonerythroid isoform of protein 4.1R interacts with the nuclear mitotic apparatus (NuMA) protein
description
1999 nî lūn-bûn
@nan
1999 թուականի Ապրիլին հրատարակուած գիտական յօդուած
@hyw
1999 թվականի ապրիլին հրատարակված գիտական հոդված
@hy
1999年の論文
@ja
1999年学术文章
@wuu
1999年学术文章
@zh-cn
1999年学术文章
@zh-hans
1999年学术文章
@zh-my
1999年学术文章
@zh-sg
1999年學術文章
@yue
name
A nonerythroid isoform of prot ...... totic apparatus (NuMA) protein
@ast
A nonerythroid isoform of prot ...... totic apparatus (NuMA) protein
@en
A nonerythroid isoform of prot ...... totic apparatus (NuMA) protein
@nl
type
label
A nonerythroid isoform of prot ...... totic apparatus (NuMA) protein
@ast
A nonerythroid isoform of prot ...... totic apparatus (NuMA) protein
@en
A nonerythroid isoform of prot ...... totic apparatus (NuMA) protein
@nl
prefLabel
A nonerythroid isoform of prot ...... totic apparatus (NuMA) protein
@ast
A nonerythroid isoform of prot ...... totic apparatus (NuMA) protein
@en
A nonerythroid isoform of prot ...... totic apparatus (NuMA) protein
@nl
P2093
P2860
P356
P1476
A nonerythroid isoform of prot ...... totic apparatus (NuMA) protein
@en
P2093
J S Hartenstein
S N Mattagajasingh
V T Marchesi
P2860
P356
10.1083/JCB.145.1.29
P407
P577
1999-04-05T00:00:00Z