Spectrin self-association site: characterization and study of beta-spectrin mutations associated with hereditary elliptocytosis.
about
Crystal structure and functional interpretation of the erythrocyte spectrin tetramerization domain complexSpectrin alpha II and beta II isoforms interact with high affinity at the tetramerization siteRecessive mutations in SPTBN2 implicate β-III spectrin in both cognitive and motor developmentThe ring-infected erythrocyte surface antigen (RESA) of Plasmodium falciparum stabilizes spectrin tetramers and suppresses further invasionRed blood cell membrane disordersCalpain-induced proteolysis of beta-spectrinsThe transitional junction: a new functional subcellular domain at the intercalated discThe spectrin-based membrane skeleton stabilizes mouse megakaryocyte membrane systems and is essential for proplatelet and platelet formation.Identification of the main ubiquitination site in human erythroid alpha-spectrin.Structural and functional effects of hereditary hemolytic anemia-associated point mutations in the alpha spectrin tetramer site.Apparent structural differences at the tetramerization region of erythroid and nonerythroid beta spectrin as discriminated by phage displayed scFvs.Mammalian alpha I-spectrin is a neofunctionalized polypeptide adapted to small highly deformable erythrocytesSlow, reversible, coupled folding and binding of the spectrin tetramerization domain.Spectrin functions upstream of ankyrin in a spectrin cytoskeleton assembly pathway.Conformational changes at the tetramerization site of erythroid alpha-spectrin upon binding beta-spectrin: a spin label EPR studyAssociation studies of erythroid alpha-spectrin at the tetramerization siteThe spectrin-ankyrin-4.1-adducin membrane skeleton: adapting eukaryotic cells to the demands of animal life.Dystrophin and Spectrin, Two Highly Dissimilar Sisters of the Same Family.Genotype-phenotype correlations in hereditary elliptocytosis and hereditary pyropoikilocytosis.Shear-response of the spectrin dimer-tetramer equilibrium in the red blood cell membrane.
P2860
Q24301548-7E5EEE8C-FB2F-493F-A33E-712582F0CC04Q24306190-2B670CD4-54B6-4734-B3A9-968BEE6D19F1Q27329788-0A84428D-85FB-40BB-A26D-D0AE58D2D350Q27972724-C23D65E5-E4C6-42C7-AEC4-3C7FEF9F8829Q28137658-70B6164E-E481-47A1-BC52-4CD8A7AEC519Q28297300-15439D3E-7730-452D-9748-6B80506ECB6BQ28297685-5B82D3D1-0B5D-42E9-8E64-358B1465A79CQ30503467-B83B1682-36FA-415D-8C00-6EEC755D0987Q31877707-10F85798-94A5-490A-BADC-A48F64E29821Q33316438-8F7A59EE-67C8-4752-9CEF-542947EA914CQ33849124-C03E25D4-AF0F-4277-B4FB-2C92B72A1467Q34270862-F6690C93-724E-4620-8BC0-AF37B1EAE17EQ34314714-C4760057-9C44-4531-B268-D9DFE1ED238FQ36119149-10F63091-AEA7-4D10-80EF-569EF733CE49Q37138304-D945D89F-712D-4C7A-90B5-4866D62A114AQ37389723-4D7F0F4B-DBDD-4B59-AF56-A3CDDF2FC5B7Q37776425-11E6CB80-A727-44D8-872B-561A349756B1Q39094614-0EBC6AB3-921D-4A9F-B004-A2B90967E13AQ41634665-7D3C4058-D9E4-4665-A709-E51CE28AE211Q51711540-79043DE3-5E1C-447A-B43B-AE91589E3B23
P2860
Spectrin self-association site: characterization and study of beta-spectrin mutations associated with hereditary elliptocytosis.
description
1998 nî lūn-bûn
@nan
1998年の論文
@ja
1998年論文
@yue
1998年論文
@zh-hant
1998年論文
@zh-hk
1998年論文
@zh-mo
1998年論文
@zh-tw
1998年论文
@wuu
1998年论文
@zh
1998年论文
@zh-cn
name
Spectrin self-association site ...... ith hereditary elliptocytosis.
@en
type
label
Spectrin self-association site ...... ith hereditary elliptocytosis.
@en
prefLabel
Spectrin self-association site ...... ith hereditary elliptocytosis.
@en
P2093
P2860
P356
P1433
P1476
Spectrin self-association site ...... ith hereditary elliptocytosis.
@en
P2093
Fournier C
Lecomte MC
P2860
P356
10.1042/BJ3320081
P407
P478
332 ( Pt 1)
P577
1998-05-01T00:00:00Z