Mammalian alpha I-spectrin is a neofunctionalized polypeptide adapted to small highly deformable erythrocytes
about
Spectrin-based skeleton as an actor in cell signalingProcessing of Plasmodium falciparum Merozoite Surface Protein MSP1 Activates a Spectrin-Binding Function Enabling Parasite Egress from RBCsThe dimensions and composition of stereociliary rootlets in mammalian cochlear hair cells: comparison between high- and low-frequency cells and evidence for a connection to the lateral membrane.The spectrin-based membrane skeleton stabilizes mouse megakaryocyte membrane systems and is essential for proplatelet and platelet formation.Structural and functional effects of hereditary hemolytic anemia-associated point mutations in the alpha spectrin tetramer site.Slow, reversible, coupled folding and binding of the spectrin tetramerization domain.Erythrocyte stiffness during morphological remodeling induced by carbon ion radiationControl of erythrocyte membrane-skeletal cohesion by the spectrin-membrane linkage.Conformational change of erythroid alpha-spectrin at the tetramerization site upon binding beta-spectrin.Unexpected complexity in the mechanisms that target assembly of the spectrin cytoskeletonα-Spectrin and integrins act together to regulate actomyosin and columnarization, and to maintain a monolayered follicular epithelium.Thermal stabilities of brain spectrin and the constituent repeats of subunits.Phosphorylation of a threonine unique to the short C-terminal isoform of betaII-spectrin links regulation of alpha-beta spectrin interaction to neuritogenesis.Image-based model of the spectrin cytoskeleton for red blood cell simulation.Creep and stress relaxation of human red cell membrane.
P2860
Q24616347-D3DE752A-D669-430C-BD09-ADFBFADCC0D4Q27972787-F499FC4A-8BCB-4FAA-8161-09E24E5B0AE5Q30478611-799E0354-7FB3-4BF1-9D17-F7CFBCB84923Q30503467-E04DA6EC-4F62-4CDA-9DCB-9680EAC387B1Q33316438-49919CFB-49A6-4AB8-B6FE-4C56C3CBC35FQ34314714-913B1DAF-680B-4B20-9972-98FFCEA8B480Q34524784-611FEE0A-A06B-45C3-9E48-56107CFC7A0EQ34664087-492FEB20-F3EC-4C75-8A5D-863406D34128Q36398821-FA152C67-D335-4AD8-84C1-7229E5E63B5FQ36585585-0887092A-83E2-4B30-87CB-E3E691D8EB0DQ36856066-0FAE94AB-C91E-47B9-9723-B17E0F3997BCQ39737881-DD44CB69-1837-48ED-9C98-22422B21007DQ40211489-3984C3C7-9675-4D4E-92AB-0AEA0FA4FAE5Q47162034-FB2A913D-9373-420D-AEA8-677A5A3E4469Q50231271-367AD956-9BC9-43F7-9840-CAF1AD7FED38
P2860
Mammalian alpha I-spectrin is a neofunctionalized polypeptide adapted to small highly deformable erythrocytes
description
2006 nî lūn-bûn
@nan
2006 թուականի Յունուարին հրատարակուած գիտական յօդուած
@hyw
2006 թվականի հունվարին հրատարակված գիտական հոդված
@hy
2006年の論文
@ja
2006年論文
@yue
2006年論文
@zh-hant
2006年論文
@zh-hk
2006年論文
@zh-mo
2006年論文
@zh-tw
2006年论文
@wuu
name
Mammalian alpha I-spectrin is ...... highly deformable erythrocytes
@ast
Mammalian alpha I-spectrin is ...... highly deformable erythrocytes
@en
Mammalian alpha I-spectrin is ...... highly deformable erythrocytes
@nl
type
label
Mammalian alpha I-spectrin is ...... highly deformable erythrocytes
@ast
Mammalian alpha I-spectrin is ...... highly deformable erythrocytes
@en
Mammalian alpha I-spectrin is ...... highly deformable erythrocytes
@nl
prefLabel
Mammalian alpha I-spectrin is ...... highly deformable erythrocytes
@ast
Mammalian alpha I-spectrin is ...... highly deformable erythrocytes
@en
Mammalian alpha I-spectrin is ...... highly deformable erythrocytes
@nl
P2093
P2860
P356
P1476
Mammalian alpha I-spectrin is ...... highly deformable erythrocytes
@en
P2093
Anthony J Baines
Marcela Salomao
Walter B Gratzer
Xinhua Guo
P2860
P304
P356
10.1073/PNAS.0507661103
P407
P577
2006-01-09T00:00:00Z