Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Critical Factors in Basal Cell Adhesion Molecule/Lutheran-mediated Adhesion to Laminin

1 Jan 1999

Abstract excerpt

Basal cell adhesion molecule (B-CAM) and Lutheran (LU) are two spliceoforms of a single immunoglobulin superfamily protein containing five Ig domains and comprise the sickle (SS) red cell receptor for laminin. We have now analyzed laminin binding to murine erythroleukemia cells transfected with various human B-CAM/LU constructs. B-CAM and LU bound equally well to laminin, indicating that the longer cytoplasmic...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Blood groups and transfusion
Share to Erythrocyte Function and Pathophysiology
Share to Hemoglobinopathies and Related Disorders

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Source

Identifiers

PMID: 9873008
DOI: 10.1074/jbc.274.2.728

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 2 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Critical Factors in Basal Cell Adhesion Molecule/Lutheran-mediated Adhesion to LamininPMID 9873008Read ↗

The Lutheran glycoprotein: a multifunctional adhesion receptorSemantic proximity Read ↗

Protein kinase A-dependent phosphorylation of Lutheran/basal cell adhesion molecule glycoprotein regulates cell adhesion to laminin alpha5.Semantic proximity Read ↗

An antibody to the lutheran glycoprotein (Lu) recognizing the LU4 blood type variant inhibits cell adhesion to laminin α5.Semantic proximity Read ↗

Identification of the Binding Site for the Lutheran Blood Group Glycoprotein on Laminin α5 through Expression of Chimeric Laminin Chains in VivoSemantic proximity Read ↗

Characterization of the laminin binding domains of the Lutheran blood group glycoprotein.Semantic proximity Read ↗

Red cell adhesion in human diseasesSemantic proximity Read ↗

Role of Rap1 in promoting sickle red blood cell adhesion to laminin via BCAM/LUSemantic proximity Read ↗

beta(2)-Adrenergic receptor and adenylate cyclase gene polymorphisms affect sickle red cell adhesion.Semantic proximity Read ↗

Laminin isoforms in human embryonic stem cells: synthesis, receptor usage and growth supportSemantic proximity Read ↗

Erythroid adhesion molecules in sickle cell disease: Effect of hydroxyureaSemantic proximity Read ↗

Crucial role of the specificity-determining loop of the integrin beta4 subunit in the binding of cells to laminin-5 and outside-in signal transduction.Semantic proximity Read ↗

Molecular mechanisms regulating the hyaluronan binding activity of the adhesion protein CD44.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.