Direct interaction between the Lu/B-CAM adhesion glycoproteins and erythroid spectrin - Wikidata - wikimedia - TriplyDB

Direct interaction between the Lu/B-CAM adhesion glycoproteins and erythroid spectrin

Direct interaction between the Lu/B-CAM adhesion glycoproteins and erythroid spectrin

http://www.wikidata.org/entity/Q28270531

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The Lutheran glycoprotein: a multifunctional adhesion receptor Functions of red cell surface proteins.Ubc9 interacts with Lu/BCAM adhesion glycoproteins and regulates their stability at the membrane of polarized MDCK cells.An antibody to the lutheran glycoprotein (Lu) recognizing the LU4 blood type variant inhibits cell adhesion to laminin α5 αII-spectrin regulates invadosome stability and extracellular matrix degradation.Review: Lutheran/B-CAM: a laminin receptor on red blood cells and in various tissues.The human Kell blood group binds the erythroid 4.1R protein: new insights into the 4.1R-dependent red cell membrane complex.Adhesive activity of Lu glycoproteins is regulated by interaction with spectrin The lutheran/basal cell adhesion molecule promotes tumor cell migration by modulating integrin-mediated cell attachment to laminin-511 protein.Novel role for the Lu/BCAM-spectrin interaction in actin cytoskeleton reorganization.Protein kinase A-dependent phosphorylation of Lutheran/basal cell adhesion molecule glycoprotein regulates cell adhesion to laminin alpha5.Enhanced calreticulin expression in red cells of polycythemia vera patients harboring the JAK2V617F mutation.Genetic inactivation of the laminin alpha5 chain receptor Lu/BCAM leads to kidney and intestinal abnormalities in the mouse.The influence of extracellular matrix proteins and mesenchymal stem cells on erythropoietic cell maturation.Internalization of CD239 highly expressed in breast cancer cells: a potential antigen for antibody-drug conjugates.

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Direct interaction between the Lu/B-CAM adhesion glycoproteins and erythroid spectrin

http://www.wikidata.org/entity/Q28270531

description

2004 nî lūn-bûn

@nan

2004 թուականի Յուլիսին հրատարակուած գիտական յօդուած

@hyw

2004 թվականի հուլիսին հրատարակված գիտական հոդված

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2004年の論文

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2004年論文

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2004年論文

@zh-hant

2004年論文

@zh-hk

2004年論文

@zh-mo

2004年論文

@zh-tw

2004年论文

@wuu

name

Direct interaction between the Lu/B-CAM adhesion glycoproteins and erythroid spectrin

@ast

Direct interaction between the Lu/B-CAM adhesion glycoproteins and erythroid spectrin

@en

Direct interaction between the Lu/B-CAM adhesion glycoproteins and erythroid spectrin

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type

label

Direct interaction between the Lu/B-CAM adhesion glycoproteins and erythroid spectrin

@ast

Direct interaction between the Lu/B-CAM adhesion glycoproteins and erythroid spectrin

@en

Direct interaction between the Lu/B-CAM adhesion glycoproteins and erythroid spectrin

@nl

prefLabel

Direct interaction between the Lu/B-CAM adhesion glycoproteins and erythroid spectrin

@ast

Direct interaction between the Lu/B-CAM adhesion glycoproteins and erythroid spectrin

@en

Direct interaction between the Lu/B-CAM adhesion glycoproteins and erythroid spectrin

@nl

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J.1365-2141.2004.05010.X

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British Journal of Haematology

P1476

Direct interaction between the Lu/B-CAM adhesion glycoproteins and erythroid spectrin

@en

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Cécile Rahuel

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

Emilie Gauthier

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

Jean Pierre Cartron

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Marie Christine Lecomte

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

Pierre Gane

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

Wassim El Nemer

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

Yolande Kroviarski

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

P2860

Rh-RhAG/ankyrin-R, a new interaction site between the membrane bilayer and the red cell skeleton, is impaired by Rh(null)-associated mutation

Ezrin/radixin/moesin (ERM) proteins bind to a positively charged amino acid cluster in the juxta-membrane cytoplasmic domain of CD44, CD43, and ICAM-2

Lutheran blood group glycoprotein and its newly characterized mouse homologue specifically bind alpha5 chain-containing human laminin with high affinity

Characterization of the laminin binding domains of the Lutheran blood group glycoprotein

Identification of the binding site for the Lutheran blood group glycoprotein on laminin alpha 5 through expression of chimeric laminin chains in vivo

Localization of Lutheran, a novel laminin receptor, in normal, knockout, and transgenic mice suggests an interaction with laminin alpha5 in vivo

Lipid domain structure of the plasma membrane revealed by patching of membrane components

New insights into erythrocyte membrane organization and microelasticity.

The role of charged amino acids in the localization of secreted and membrane proteins.

Association of the epithelial sodium channel with Apx and alpha-spectrin in A6 renal epithelial cells.

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255-64

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scholarly article

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10.1111/J.1365-2141.2004.05010.X

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P433

2

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126

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P50

Caroline Le Van Kim

P577

2004-07-01T00:00:00Z

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8471173

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15238148

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