Results 231 to 240 of about 73,712 (251)
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Polymorphism of mannose‐6‐phosphate isomerase in cattle

Animal Blood Groups and Biochemical Genetics, 1973
SummaryEnzymo‐electrophoresis and enzymo‐electrofocusing of white cells and of muscular extracts of cattle has revealed four kinds of phenotypic patterns. Evidence presented here indicates that three of these phenotypes are controlled by two codominant, autosomal alleles, MPIB and MPIC.
M, Ansay, R, Hanset
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46 kd mannose 6-phosphate receptor: Cloning, expression, and homology to the 215 kd mannose 6-phosphate receptor

Cell, 1987
We have isolated cDNA clones encoding the entire sequence of the bovine 46 kd cation-dependent mannose 6-phosphate (CD Man-6-P) receptor. Translation of CD Man-6-P receptor mRNA in Xenopus laevis oocytes results in a protein that binds specifically to phosphomannan-Sepharose, thus demonstrating that our cDNA clones encode a functional receptor.
N M, Dahms   +4 more
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Mannose-6-Phosphate: A Regulator of LLO Destruction

2013
Oligosaccharyltransferase (OT) catalyzes the signature reaction of the asparagine-linked glycosylation pathway, namely, the transfer of preformed glycans from the lipid-linked oligosaccharide Glc3Man9GlcNAc2-P-P-Dolichol (G3M9Gn2-LLO) to appropriate asparaginyl residues on acceptor polypeptides.
Ningguo, Gao, Mark A, Lehrman
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Mannose 6-phosphate receptors in an ancient vertebrate, zebrafish

Development Genes and Evolution, 2006
The endosome/lysosome system plays key roles in embryonic development, but difficulties posed by inaccessible mammalian embryos have hampered detailed studies. The accessible, transparent embryos of Danio rerio, together with the genetic and experimental approaches possible with this organism, provide many advantages over rodents. In mammals, mannose 6-
Catherine M, Nolan   +4 more
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Mannose 6-phosphate receptors: new twists in the tale

Nature Reviews Molecular Cell Biology, 2003
The two mannose 6-phosphate (M6P) receptors were identified because of their ability to bind M6P-containing soluble acid hydrolases in the Golgi and transport them to the endosomal-lysosomal system. During the past decade, we have started to understand the structural features of these receptors that allow them to do this job, and how the receptors ...
Pradipta, Ghosh   +2 more
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SYNTHÈSE DE MANNOSE 6-PHOSPHONATES, ANALOGUES ISOSTÈRES DU MANNOSE 6-PHOSPHATE

Phosphorus, Sulfur, and Silicon and the Related Elements, 2000
Abstract Nous decrivons la syntese de deux phosphonates analogues isosteres du Mannose 6-Phosphate (M6P). Ce dernier est un marqueur de reconnaissance pre dans la structure des enzymes lysosomales et est indispensable a leur transport vers les lysosomes.
Carole Vidil   +3 more
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Domain 5 of the Cation-Independent Mannose 6-Phosphate Receptor Preferentially Binds Phosphodiesters (Mannose 6-Phosphate N-Acetylglucosamine Ester)

Biochemistry, 2007
The 300 kDa cation-independent mannose 6-phosphate receptor (CI-MPR) and the 46 kDa cation-dependent MPR (CD-MPR) are key components of the lysosomal enzyme targeting system that bind newly synthesized mannose 6-phosphate (Man-6-P)-containing acid hydrolases and divert them from the secretory pathway.
Carrie A, Chavez   +5 more
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The mannose 6‐phosphate receptor: function, biosynthesis and translocation

Biology of the Cell, 1984
This report summarizes studies concerning the role of the lysosomal protein: Man‐6‐P receptor and describes some recent data on its biosynthesis and cellular translocation. The receptor functions both in the Golgi apparatus (or GERL) and on the cell surface where it binds lysosomal proteins and mediates their transport to lysosomes. Consistent with its
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Mannose-6-Phosphate Receptor Homologous Protein Family

2012
Protein quality control in the endoplasmic reticulum (ER) is an elaborate process conserved from yeast to mammals, ensuring that only newly synthesized proteins with correct conformations in the ER are sorted further into the secretory pathway. The ER discriminates between native and nonnative protein conformations, selectively transporting properly ...
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