Global transformation of erythrocyte properties via engagement of an SH2-like sequence in band 3.

about

Global transformation of erythrocyte properties via engagement of an SH2-like sequence in band 3.

Item

http://www.wikidata.org/entity/Q37473889

description

2016 nî lūn-bûn

@nan

2016年の論文

@ja

2016年学术文章

@wuu

2016年学术文章

@zh-cn

2016年学术文章

@zh-hans

2016年学术文章

@zh-my

2016年学术文章

@zh-sg

2016年學術文章

@yue

2016年學術文章

@zh

2016年學術文章

@zh-hant

name

Global transformation of eryth ...... n SH2-like sequence in band 3.

@en

Global transformation of eryth ...... n SH2-like sequence in band 3.

@nl

type

Item

label

Global transformation of eryth ...... n SH2-like sequence in band 3.

@en

Global transformation of eryth ...... n SH2-like sequence in band 3.

@nl

prefLabel

Global transformation of eryth ...... n SH2-like sequence in band 3.

@en

Global transformation of eryth ...... n SH2-like sequence in band 3.

@nl

P1476

Global transformation of eryth ...... n SH2-like sequence in band 3.

@en

P2093

Francesco M Turrini

http://www.w3.org/2001/XMLSchema#string

Philip S Low

http://www.w3.org/2001/XMLSchema#string

Yen-Hsing Li

http://www.w3.org/2001/XMLSchema#string

P2860

Crystal structure of the anion exchanger domain of human erythrocyte band 3

Conservation analysis and structure prediction of the SH2 family of phosphotyrosine binding domains

The language of SH2 domain interactions defines phosphotyrosine-mediated signal transduction

Carbonic anhydrase II binds to the carboxyl terminus of human band 3, the erythrocyte C1-/HCO3- exchanger

Mapping the binding sites of human erythrocyte ankyrin for the anion exchanger and spectrin

Highly conserved eight amino acid sequence in SH2 is important for recognition of phosphotyrosine site.

Regulation of membrane-cytoskeletal interactions by tyrosine phosphorylation of erythrocyte band 3.

Analysis of changes in tyrosine and serine phosphorylation of red cell membrane proteins induced by P. falciparum growth.

Irreversible AE1 tyrosine phosphorylation leads to membrane vesiculation in G6PD deficient red cells

Molecular basis for membrane rigidity of hereditary ovalocytosis. A novel mechanism involving the cytoplasmic domain of band 3.

P304

13732-13737

http://www.w3.org/2001/XMLSchema#string

P31

scholarly article

P356

10.1073/PNAS.1611904113

http://www.w3.org/2001/XMLSchema#string

P407

English

P433

http://www.w3.org/2001/XMLSchema#string

P478

113

http://www.w3.org/2001/XMLSchema#string

P50

M Estela Puchulu-Campanella

P577

2016-11-15T00:00:00Z

http://www.w3.org/2001/XMLSchema#dateTime

P698

27856737

http://www.w3.org/2001/XMLSchema#string

P932

5137735

http://www.w3.org/2001/XMLSchema#string