Lysosomal enzyme phosphorylation. Recognition of a protein-dependent determinant allows specific phosphorylation of oligosaccharides present on lysosomal enzymes
about
The DMAP interaction domain of UDP-GlcNAc:lysosomal enzyme N-acetylglucosamine-1-phosphotransferase is a substrate recognition moduleFunctions of the alpha, beta, and gamma subunits of UDP-GlcNAc:lysosomal enzyme N-acetylglucosamine-1-phosphotransferaseTwo crystal structures for cathepsin D: the lysosomal targeting signal and active siteA cluster of basic amino acids within an alpha-helix is essential for alpha-subunit recognition by the glycoprotein hormone N-acetylgalactosaminyltransferase.Glucosidase II and MRH-domain containing proteins in the secretory pathway.An Active 32-kDa Cathepsin L Is Secreted Directly from HT 1080 Fibrosarcoma Cells and Not via Lysosomal Exocytosis.Lysosomal enzyme trafficking in mannose 6-phosphate receptor-positive mouse L-cells: demonstration of a steady state accumulation of phosphorylated acid hydrolasesGene dosage-dependent secretion of yeast vacuolar carboxypeptidase Y.Multiple carbohydrate receptors on lymphocytes revealed by adhesion to immobilized polysaccharides.Expression of human cathepsin D in Xenopus oocytes: phosphorylation and intracellular targetingRenin, a secretory glycoprotein, acquires phosphomannosyl residuesYeast carboxypeptidase Y vacuolar targeting signal is defined by four propeptide amino acids.Human beta-hexosaminidase alpha chain: coding sequence and homology with the beta chainStructural requirements for sulfation of asparagine-linked oligosaccharides of lutropinMannose 6-phosphate receptor homology (MRH) domain-containing lectins in the secretory pathway.The "old" Euonymus europaeus agglutinin represents a novel family of ubiquitous plant proteins.Trafficking of lysosomal enzymes in normal and disease states.The role of glycosylation in protein recognition. Warner-Lambert Parke-Davis Award lecture.Mucolipidoses II and III variants with normal N-acetylglucosamine 1-phosphotransferase activity toward alpha-methylmannoside are due to nonallelic mutationsLysosomal enzyme phosphorylation in human fibroblasts. Kinetic parameters offer a biochemical rationale for two distinct defects in the uridine diphospho-N-acetylglucosamine:lysosomal enzyme precursor N-acetylglucosamine-1-phosphotransferase.Characterization of the mannose 6-phosphate-dependent pathway of lysosomal enzyme routing in an invertebrate.Phosphorylation of arylsulphatase A occurs through multiple interactions with the UDP-N-acetylglucosamine-1-phosphotransferase proximal and distal to its retrieval site by the KDEL receptorFour monoclonal antibodies inhibit the recognition of arylsulphatase A by the lysosomal enzyme phosphotransferase.Glycosylation of procathepsin L does not account for species molecular-mass differences and is not required for proteolytic activity.A short domain of the plant vacuolar protein phytohemagglutinin targets invertase to the yeast vacuole.Role of spacer-1 in the maturation and function of GlcNAc-1-phosphotransferase.
P2860
Q24294454-6BDA422A-69FF-40D9-8F51-DBFFC85CC481Q24324179-D8E71D68-B085-4ECB-B032-8A97FDD8D396Q28267848-D505760A-112C-4A12-91BF-202285D196CCQ34774666-96B4A151-119B-46EC-8002-AD6E216CF6C2Q35542842-29E5E31E-5D39-429E-9EF6-3A2558F5D72DQ35870565-D80FE456-A416-4BDA-BD13-061ED080F399Q36214600-BAF146A7-5796-414E-90A6-CAD3B3A30C81Q36214972-4DEEEDD7-30EA-4E15-87FD-F5339982544AQ36217439-2E1985ED-FA45-4091-BFF4-3062A1C49159Q36217785-5BDD807C-D8DC-4139-85D8-9E160D84D4D7Q36217859-D3BB6910-78F8-4E4E-BCB5-DEB3D7FBB884Q36223409-1556EEED-8F05-4A8F-9A86-3DF97CB555BAQ36418433-0D3EE314-3F5B-4C56-8712-3E05A4428E71Q37537260-90425C57-C0C6-4BFD-A391-836F2168880CQ37896955-6F5CD368-6224-43E4-B45D-2F247E8E73AAQ38291364-A21DD7A7-6734-4657-94A7-B830B6A14F21Q38351553-67BF61B2-9BFB-4AD9-AB64-3311AA7E6901Q38351709-7C027877-0F5F-4B14-862D-548FFB48B529Q40544769-B1E05D2F-C402-45A6-96A6-46AA4662C791Q40921782-5A8BB9FB-4557-4449-873F-33C4B78D123CQ41848502-79D879BF-A83F-4ADE-9A11-292740893FF9Q41923933-027EB466-4091-48AF-A96D-168BE8933A48Q42147468-DC23B64E-6350-439B-9429-936F95966BA2Q42795813-401A0EC1-4522-4B14-8DF9-E279B6C249ADQ46080275-81D06FDD-9FEE-4908-AB88-FE9C27BD3402Q47193487-D9EAA9D2-E768-428F-8321-DD2ACB996DC2
P2860
Lysosomal enzyme phosphorylation. Recognition of a protein-dependent determinant allows specific phosphorylation of oligosaccharides present on lysosomal enzymes
description
1984 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած
@hyw
1984 թվականի դեկտեմբերին հրատարակված գիտական հոդված
@hy
article publié dans la revue scientifique Journal of Biological Chemistry
@fr
artículu científicu espublizáu en 1984
@ast
im Dezember 1984 veröffentlichter wissenschaftlicher Artikel
@de
scientific journal article
@en
vedecký článok (publikovaný 1984/12/10)
@sk
vědecký článek publikovaný v roce 1984
@cs
wetenschappelijk artikel (gepubliceerd op 1984/12/10)
@nl
наукова стаття, опублікована в грудні 1984
@uk
name
Lysosomal enzyme phosphorylati ...... s present on lysosomal enzymes
@ast
Lysosomal enzyme phosphorylati ...... s present on lysosomal enzymes
@en
Lysosomal enzyme phosphorylati ...... s present on lysosomal enzymes
@nl
type
label
Lysosomal enzyme phosphorylati ...... s present on lysosomal enzymes
@ast
Lysosomal enzyme phosphorylati ...... s present on lysosomal enzymes
@en
Lysosomal enzyme phosphorylati ...... s present on lysosomal enzymes
@nl
prefLabel
Lysosomal enzyme phosphorylati ...... s present on lysosomal enzymes
@ast
Lysosomal enzyme phosphorylati ...... s present on lysosomal enzymes
@en
Lysosomal enzyme phosphorylati ...... s present on lysosomal enzymes
@nl
P2093
P1476
Lysosomal enzyme phosphorylati ...... s present on lysosomal enzymes
@en
P2093
P304
14663-14671
P407
P577
1984-12-01T00:00:00Z