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Nuclear pore complex contains a family of glycoproteins that includes p62: glycosylation through a previously unidentified cellular pathway.

Data up to Jan 2025

Published1987
Citations330
References16

Total Citations Per Year

Abstract

References (16)

Peptide mapping by limited proteolysis in sodium dodecyl sulfate and analysis by gel electrophoresis.

1977 • 5,640 citations

Nuclei from Rat Liver: Isolation Method That Combines Purity with High Yield

1966 • 1,687 citations

Topography and polypeptide distribution of terminal N-acetylglucosamine residues on the surfaces of intact lymphocytes. Evidence for O-linked GlcNAc.

1984 • 1,057 citations

Purification and Properties of an Endo-β-N-acetylglucosaminidase from Streptomyces griseus

1974 • 870 citations

Tunicamycin inhibition of polyisoprenyl N-acetylglucosaminyl pyrophosphate formation in calf-liver microsomes

1975 • 863 citations

Identification and characterization of a nuclear pore complex protein

1986 • 610 citations

TUNICAMYCIN, A NEW ANTIBIOTIC. I

1971 • 535 citations

Monoclonal antibodies identify a group of nuclear pore complex glycoproteins.

1987 • 533 citations

Inhibition of in vitro nuclear transport by a lectin that binds to nuclear pores.

1987 • 510 citations

The subcellular distribution of terminal N-acetylglucosamine moieties. Localization of a novel protein-saccharide linkage, O-linked GlcNAc.

1986 • 481 citations

Nuclear pore complex glycoproteins contain cytoplasmically disposed O-linked N-acetylglucosamine.

1987 • 428 citations

A modified procedure for the isolation of a pore complex-lamina fraction from rat liver nuclei.

1976 • 423 citations

Glycosyltransferases and their Use in Assessing Oligosaccharide Structure and Structure‐Function Relationships

1981 • 221 citations

A nuclear specific glycoprotein representative of a unique pattern of glycosylation.

1987 • 81 citations

Porcine A blood group-specific N-acetylgalactosaminyltransferase.

1977 • 72 citations

Nuclear ribonucleoprotein release and nucleoside triphosphatase activity are inhibited by antibodies directed against one nuclear matrix glycoprotein.

1983 • 69 citations

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Nuclear pore complex contains a family of glycoproteins that includes p62: glycosylation… (1987) – Proceedings of the National Academy of Sciences | Metascience Observatory Explorer