Sorting out glycosylation enzymes in the Golgi apparatus.
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The Ras signaling inhibitor LOX-PP interacts with Hsp70 and c-Raf to reduce Erk activation and transformed phenotype of breast cancer cellsRegulation of Golgi Cisternal Progression by Ypt/Rab GTPases.Sugar-free frosting, a homolog of SAD kinase, drives neural-specific glycan expression in the Drosophila embryo.DIA1R is an X-linked gene related to Deleted In Autism-1.Conserved oligomeric Golgi complex specifically regulates the maintenance of Golgi glycosylation machinery.GolgiP: prediction of Golgi-resident proteins in plants.Models for Golgi traffic: a critical assessmentGolgi calcium pump secretory pathway calcium ATPase 1 (SPCA1) is a key regulator of insulin-like growth factor receptor (IGF1R) processing in the basal-like breast cancer cell line MDA-MB-231Rab41 is a novel regulator of Golgi apparatus organization that is needed for ER-to-Golgi trafficking and cell growth.Golgi and related vesicle proteomics: simplify to identify.The origin and function of platelet glycosyltransferases.OsCYP21-4, a novel Golgi-resident cyclophilin, increases oxidative stress tolerance in rice.The Golgi apparatus: an organelle with multiple complex functions.Sub-compartmental organization of Golgi-resident N-glycan processing enzymes in plantsCellular and molecular biology of glycosphingolipid glycosylation.Organization of the synthesis of glycolipid oligosaccharides in the Golgi complex.Evolutionary forces shaping the Golgi glycosylation machinery: why cell surface glycans are universal to living cellsGolgi glycosylation and human inherited diseases.Cell biology of the endoplasmic reticulum and the Golgi apparatus through proteomicsThe plant secretory pathway seen through the lens of the cell wall.Functional organization of Golgi N- and O-glycosylation pathways involves pH-dependent complex formation that is impaired in cancer cells.Sialylation of N-glycans: mechanism, cellular compartmentalization and function.Land-locked mammalian Golgi reveals cargo transport between stable cisternae.Organizational interplay of Golgi N-glycosyltransferases involves organelle microenvironment-dependent transitions between enzyme homo- and heteromers.Extrinsic Functions of Lectin Domains in O-N-Acetylgalactosamine Glycan Biosynthesis.A brief history of the cisternal progression-maturation model.Targeting Cysteine Thiols for in Vitro Site-specific Glycosylation of Recombinant Proteins.Artificial organelles: digital microfluidic platform for proteoglycan and glycoprotein biosynthesis.
P2860
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P2860
Sorting out glycosylation enzymes in the Golgi apparatus.
description
article científic
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article scientifique
@fr
articolo scientifico
@it
artigo científico
@pt
bilimsel makale
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scientific article published on 28 October 2009
@en
vedecký článok
@sk
vetenskaplig artikel
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videnskabelig artikel
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vědecký článek
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name
Sorting out glycosylation enzymes in the Golgi apparatus.
@en
Sorting out glycosylation enzymes in the Golgi apparatus.
@nl
type
label
Sorting out glycosylation enzymes in the Golgi apparatus.
@en
Sorting out glycosylation enzymes in the Golgi apparatus.
@nl
prefLabel
Sorting out glycosylation enzymes in the Golgi apparatus.
@en
Sorting out glycosylation enzymes in the Golgi apparatus.
@nl
P2093
P2860
P1433
P1476
Sorting out glycosylation enzymes in the Golgi apparatus.
@en
P2093
Catherine E Au
John J M Bergeron
Tommy Nilsson
P2860
P304
P356
10.1016/J.FEBSLET.2009.10.064
P407
P577
2009-10-28T00:00:00Z