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

scientific article published on October 30, 1992

The glycoprotease of Pasteurella haemolytica A1 eliminates binding of myeloid cells to P-selectin but not to E-selectin is …
instance of (P31):
scholarly articleQ13442814

External links are
P356DOI10.1016/0006-291X(92)91121-6
P953full work available at URLhttps://api.elsevier.com/content/article/PII:0006291X92911216?httpAccept=text/xml
https://api.elsevier.com/content/article/PII:0006291X92911216?httpAccept=text/plain
P698PubMed publication ID1280121

P2093author name stringC. A. Eddy
R. M. Leimgruber
A. Mellors
J. K. Welply
C. N. Steininger
P2860cites workAn endothelial ligand for L-selectin is a novel mucin-like moleculeQ28187110
Identification of a specific glycoprotein ligand for P-selectin (CD62) on myeloid cellsQ36533177
Carbohydrate ligands of the LEC cell adhesion moleculesQ36611203
The three members of the selectin receptor family recognize a common carbohydrate epitope, the sialyl Lewis(x) oligosaccharideQ38329123
Selectin GMP-140 (CD62; PADGEM) binds to sialosyl-Lea and sialosyl-Lex, and sulfated glycans modulate this bindingQ38331669
Recognition by Elam-1 of the Sialyl-Le x Determinant on Myeloid and Tumor CellsQ38338272
A neutral glycoprotease of Pasteurella haemolytica A1 specifically cleaves O-sialoglycoproteinsQ40148484
Distribution of glycoprotease activity and the glycoprotease gene among serotypes of Pasteurella haemolyticaQ45066622
Characterization of human platelet GMP-140 as a heparin-binding proteinQ69116662
P433issue2
P407language of work or nameEnglishQ1860
P921main subjectbiochemistryQ7094
biophysicsQ7100
cell biologyQ7141
Pasteurella haemolyticaQ62904115
P304page(s)760-766
P577publication date1992-10-01
1992-10-30
P1433published inBiochemical and Biophysical Research CommunicationsQ864228
P1476titleThe glycoprotease of Pasteurella haemolytica A1 eliminates binding of myeloid cells to P-selectin but not to E-selectin
P478volume188

Reverse relations

cites work (P2860)
Q7205929447 O-sialoglycoprotease from Pasteurella haemolytica
Q24679247CD44 is a major E-selectin ligand on human hematopoietic progenitor cells
Q38304606Cloning and functional characterization of recombinant equine P-selectin.
Q36234852Distinct cell surface ligands mediate T lymphocyte attachment and rolling on P and E selectin under physiological flow.
Q33784012Epstein-Barr virus recombinant lacking expression of glycoprotein gp150 infects B cells normally but is enhanced for infection of epithelial cells.
Q34169805Inflammatory roles of P-selectin
Q53862042Inhibition of allospecific response in pancreatic islet transplantation: the glycan approach.
Q52344563Lifetime of the P-selectin-carbohydrate bond and its response to tensile force in hydrodynamic flow.
Q36234196Monospecific and common glycoprotein ligands for E- and P-selectin on myeloid cells
Q35764552Neutrophils use both shared and distinct mechanisms to adhere to selectins under static and flow conditions
Q36382391P-selectin glycoprotein ligand-1 mediates rolling of human neutrophils on P-selectin
Q34171030P-selectin mediates adhesion of platelets to neuroblastoma and small cell lung cancer
Q35634175Selectin ligands
Q36237657Sialylated, fucosylated ligands for L-selectin expressed on leukocytes mediate tethering and rolling adhesions in physiologic flow conditions
Q38317579Structural and functional characterization of monomeric soluble P-selectin and comparison with membrane P-selectin
Q28644133The P-selectin glycoprotein ligand from human neutrophils displays sialylated, fucosylated, O-linked poly-N-acetyllactosamine
Q34523324The chemistry of oligosaccharide ligands of selectins: significance for the development of new immunomodulatory medicines

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