about
Novel alternatively spliced isoforms of the neurofibromatosis type 2 tumor suppressor are targeted to the nucleus and cytoplasmic granulesA nonerythroid isoform of protein 4.1R interacts with components of the contractile apparatus in skeletal myofibersPhosphorylation of protein 4.1 on tyrosine-418 modulates its function in vitroA nonerythroid isoform of protein 4.1R interacts with the nuclear mitotic apparatus (NuMA) proteinA member of the Plasmodium falciparum PHIST family binds to the erythrocyte cytoskeleton component band 4.1Vesicle transport: the role of actin filaments and myosin motors.Spectrin: the ghost in the machine.Structural protein 4.1R is integrally involved in nuclear envelope protein localization, centrosome-nucleus association and transcriptional signaling.The 10 kDa domain of human erythrocyte protein 4.1 binds the Plasmodium falciparum EBA-181 proteinStructural protein 4.1 in the nucleus of human cells: dynamic rearrangements during cell division.Stopped-flow measurement of cytoskeletal contraction: Dictyostelium myosin II is specifically required for contraction of amoeba cytoskeletons.Role of tissue specific alternative pre-mRNA splicing in the differentiation of the erythrocyte membraneAn alternative domain determines nuclear localization in multifunctional protein 4.1.Characterization of isoforms of protein 4.1 present in the nucleus.Mechanical fluctuations of the membrane-skeleton are dependent on F-actin ATPase in human erythrocytes.4.1R proteins associate with interphase microtubules in human T cells: a 4.1R constitutive region is involved in tubulin binding.Nonequilibrium fluctuations of mechanically stretched single red blood cells detected by optical tweezers.
P2860
Q22010248-AF869208-67B1-4567-9BAD-6CFFC722C269Q24550998-B3C6A180-9734-4E44-B9B0-D36B0E4C9CEBQ24564872-AD195885-FBD5-4695-9135-7F0E03F4225AQ24670276-1456658D-1A68-4A91-8DF4-B74F7F7709DAQ30043144-6523B32B-DE2D-4735-B904-4582331BBD7AQ33752884-73A5FE8A-9B27-4B85-9EBE-7F2311B07F69Q34136096-F7D068F0-E6DD-48E5-9B7D-B64180DBD10BQ34808629-2958DFD5-8367-4656-A4EF-73F575EA880FQ35129141-19A5FCA6-95B0-47D6-B69D-D35E3BBDFD77Q36273829-A333F2EA-F282-4482-B400-3D904203185BQ36530289-67727E34-E0EE-4B24-8691-3475437EEC8AQ36647319-7FB6C53A-EA1A-43EA-A7C4-1D003FB2B20BQ41035102-92F2B1EE-6B40-4735-A97F-4B7063CF97FAQ41660717-E21FC369-1096-46E9-B9B9-913129D15D52Q41890257-D30DF049-3933-4E59-871F-159462E6AF7CQ43752283-FE162F41-1CA0-47E7-B959-269315B6EE29Q50491810-DB971CB0-F112-4EC8-9A44-294C9801DAC3
P2860
description
1989 nî lūn-bûn
@nan
1989 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած
@hyw
1989 թվականի դեկտեմբերին հրատարակված գիտական հոդված
@hy
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
name
Erythrocyte protein 4.1 binds and regulates myosin.
@ast
Erythrocyte protein 4.1 binds and regulates myosin.
@en
Erythrocyte protein 4.1 binds and regulates myosin.
@nl
type
label
Erythrocyte protein 4.1 binds and regulates myosin.
@ast
Erythrocyte protein 4.1 binds and regulates myosin.
@en
Erythrocyte protein 4.1 binds and regulates myosin.
@nl
prefLabel
Erythrocyte protein 4.1 binds and regulates myosin.
@ast
Erythrocyte protein 4.1 binds and regulates myosin.
@en
Erythrocyte protein 4.1 binds and regulates myosin.
@nl
P2860
P356
P1476
Erythrocyte protein 4.1 binds and regulates myosin.
@en
P2093
G R Pasternack
R H Racusen
P2860
P304
P356
10.1073/PNAS.86.24.9712
P407
P577
1989-12-01T00:00:00Z