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The glycoprotease of Pasteurella haemolytica A1 eliminates binding of myeloid cells to P-selectin but not to E-selectin

Data up to Jan 2025

Published1992
Citations42
References13

Total Citations Per Year

Abstract

References (13)

High resolution two-dimensional electrophoresis of proteins.

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Recognition by Elam-1 of the Sialyl-Le x Determinant on Myeloid and Tumor Cells

1990 • 976 citations

The three members of the selectin receptor family recognize a common carbohydrate epitope, the sialyl Lewis(x) oligosaccharide

1992 • 698 citations

An endothelial ligand for L-Selectin is a novel mucin-like molecule

1992 • 660 citations

Identification of a specific glycoprotein ligand for P-selectin (CD62) on myeloid cells.

1992 • 519 citations

A carbohydrate domain common to both sialyl Le(a) and sialyl Le(X) is recognized by the endothelial cell leukocyte adhesion molecule ELAM-1

1991 • 480 citations

Carbohydrate ligands of the LEC cell adhesion molecules

1990 • 338 citations

Selectin GMP-140 (CD62; PADGEM) binds to sialosyl-Lea and sialosyl-Lex, and sulfated glycans modulate this binding

1991 • 134 citations

A neutral glycoprotease of Pasteurella haemolytica A1 specifically cleaves O-sialoglycoproteins

1992 • 130 citations

Cleavage of the cell-surface O-sialoglycoproteins CD34, CD43, CD44, and CD45 by a novel glycoprotease from Pasteurella haemolytica.

1992 • 121 citations

Characterization of human platelet GMP-140 as a heparin-binding protein

1989 • 75 citations

Lymphocyte function-associated antigen 1 (LFA-1) contains sulfated N-linked oligosaccharides.

1985 • 42 citations

Distribution of glycoprotease activity and the glycoprotease gene among serotypes of Pasteurella haemolytica

1990 • 41 citations

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The glycoprotease of Pasteurella haemolytica A1 eliminates binding of myeloid cells to… (1992) – Biochemical and Biophysical Research Communications | Metascience Observatory Explorer