Pub. Date : 1997 Feb
PMID : 9003039
6 Functional Relationships(s)Download |
Sentence | Compound Name | Protein Name | Organism |
| 1 | L1/HNK-1 carbohydrate- and beta 1 integrin-dependent neural cell adhesion to laminin-1. | Carbohydrates | beta-1,3-glucuronyltransferase 1 (glucuronosyltransferase P) | Mus musculus |
| 2 | We have shown recently that mouse small cerebellar neurons adhere to a short amino acid sequence of the G2 domain of the laminin alpha 1 chain via the cell surface-expressed HNK-1 carbohydrate. | Carbohydrates | beta-1,3-glucuronyltransferase 1 (glucuronosyltransferase P) | Mus musculus |
| 3 | Therefore, we were interested in identifying glycoproteins carrying the HNK-1 carbohydrate at the cell surface of these neurons. | Carbohydrates | beta-1,3-glucuronyltransferase 1 (glucuronosyltransferase P) | Mus musculus |
| 4 | The binding could be partially inhibited by Fab fragments of monoclonal antibodies against the HNK-1 carbohydrate and against the Ig-like domains of L1. | Carbohydrates | beta-1,3-glucuronyltransferase 1 (glucuronosyltransferase P) | Mus musculus |
| 5 | Determination of the association of L1, beta 1 integrin, and the HNK-1 carbohydrate on the cell surface of live cerebellar neurons by antibody-induced patching and copatching revealed HNK-1 to be linked to L1, but less so to beta 1 integrin. | Carbohydrates | beta-1,3-glucuronyltransferase 1 (glucuronosyltransferase P) | Mus musculus |
| 6 | Determination of the association of L1, beta 1 integrin, and the HNK-1 carbohydrate on the cell surface of live cerebellar neurons by antibody-induced patching and copatching revealed HNK-1 to be linked to L1, but less so to beta 1 integrin. | Carbohydrates | beta-1,3-glucuronyltransferase 1 (glucuronosyltransferase P) | Mus musculus |