Sulfation of lutropin oligosaccharides with a cell-free system. - Wikidata - awgldk - TriplyDB

Sulfation of lutropin oligosaccharides with a cell-free system.

Sulfation of lutropin oligosaccharides with a cell-free system.

http://www.wikidata.org/entity/Q37565072

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Pathways involved in targeting and secretion of a lysosomal enzyme in Dictyostelium discoideum.Gonadotropin beta subunits determine the rate of assembly and the oligosaccharide processing of hormone dimer in transfected cells Secretory trafficking signal encoded in the carboxyl-terminal region of the CGbeta-subunit.Sulfation of LH does not affect intracellular trafficking.Phosphorylation of the secreted, free alpha subunit of human chorionic gonadotropin.Structural requirements for sulfation of asparagine-linked oligosaccharides of lutropin The role of glycosylation in protein recognition. Warner-Lambert Parke-Davis Award lecture.Sulphation of proteins secreted by a human hepatoma-derived cell line. Sulphation of N-linked oligosaccharides on alpha 2HS-glycoprotein.Molecular cloning and enzymatic characterization of a UDP-GalNAc:GlcNAc(beta)-R beta1,4-N-acetylgalactosaminyltransferase from Caenorhabditis elegans.A pituitary N-acetylgalactosamine transferase that specifically recognizes glycoprotein hormones.The subcellular sites of sulfation of mouse thyrotropin and free alpha subunits: studies employing subcellular fractionation and inhibitors of the intracellular translocation of proteins.

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Sulfation of lutropin oligosaccharides with a cell-free system.

http://www.wikidata.org/entity/Q37565072

description

article científic

@ca

article scientifique

@fr

articolo scientifico

@it

artigo científico

@pt

bilimsel makale

@tr

scientific article published on September 1984

@en

vedecký článok

@sk

vetenskaplig artikel

@sv

videnskabelig artikel

@da

vědecký článek

@cs

name

Sulfation of lutropin oligosaccharides with a cell-free system.

@en

Sulfation of lutropin oligosaccharides with a cell-free system.

@nl

type

label

Sulfation of lutropin oligosaccharides with a cell-free system.

@en

Sulfation of lutropin oligosaccharides with a cell-free system.

@nl

prefLabel

Sulfation of lutropin oligosaccharides with a cell-free system.

@en

Sulfation of lutropin oligosaccharides with a cell-free system.

@nl

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P356

PNAS.81.17.5320

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Proceedings of the National Academy of Sciences of the United States of America

P1476

Sulfation of lutropin oligosaccharides with a cell-free system.

@en

P2093

E D Green

http://www.w3.org/2001/XMLSchema#string

I Boime

http://www.w3.org/2001/XMLSchema#string

J Gruenebaum

http://www.w3.org/2001/XMLSchema#string

J U Baenziger

http://www.w3.org/2001/XMLSchema#string

M Bielinska

http://www.w3.org/2001/XMLSchema#string

P2860

Lysosomal enzyme targeting. N-Acetylglucosaminylphosphotransferase selectively phosphorylates native lysosomal enzymes

Tyrosine-O-sulfated proteins of PC12 pheochromocytoma cells and their sulfation by a tyrosylprotein sulfotransferase

In vivo sulfation of the contact site A glycoprotein of Dictyostelium discoideum.

Glycoprotein hormones: structure and function.

Differences between purified ectopic and normal alpha subnits of human glycoprotein hormones.

mRNA-dependent synthesis of authentic precursor to human placental lactogen: conversion to its mature hormone form in ascites cell-free extracts.

Synthesis and localization of two sulphated glycoproteins associated with basement membranes and the extracellular matrix

A subclass of proteins and sulfated macromolecules secreted by AtT-20 (mouse pituitary tumor) cells is sorted with adrenocorticotropin into dense secretory granules

endo-beta-N-acetylglucosaminidase F: endoglycosidase from Flavobacterium meningosepticum that cleaves both high-mannose and complex glycoproteins.

Combination of rat lutropin subunits occurs early in the secretory pathway.

P304

5320-5324

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P31

scholarly article

P356

10.1073/PNAS.81.17.5320

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P407

P433

17

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P478

81

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P577

1984-09-01T00:00:00Z

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P5875

16605508

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P698

6591193

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P921

oligosaccharide

P932

391695

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