Results 21 to 30 of about 182,092 (302)

Extracellular Domain N-Glycosylation Controls Human Thrombopoietin Receptor Cell Surface Levels

open access: yesFrontiers in Endocrinology, 2011
The thrombopoietin receptor (TpoR) is a type I transmembrane protein that mediates the signaling functions of thrombopoietin (Tpo) in regulating megakaryocyte differentiation, platelet formation and hematopoietic stem cell renewal.
Roxana I. Albu   +1 more
doaj   +1 more source

Variation of the serum N‐glycosylation during the pregnancy of a MPI‐CDG patient

open access: yesJIMD Reports, 2021
For the first time the glycosylation of a patient with a MPI‐CDG during pregnancy is monitored. MPI‐CDG, is characterised by a deficiency in mannose‐6‐phosphate isomerase (MPI) leading to a reduced pool of glycosylation precursors, impairing the ...
Elodie Lebredonchel   +4 more
doaj   +1 more source

N-glycosylation requirements in neuromuscular synaptogenesis [PDF]

open access: yesDevelopment, 2013
Neural development requires N-glycosylation regulation of intercellular signaling, but the requirements in synaptogenesis have not been well tested. All complex and hybrid N-glycosylation requires MGAT1 (UDP-GlcNAc:α-3-D-mannoside-β1,2-N-acetylglucosaminyl-transferase I) function, and Mgat1 nulls are the most compromised N-glycosylation condition that ...
William, Parkinson   +3 more
openaire   +2 more sources

Complex -Glycans Influence the Spatial Arrangement of Voltage Gated Potassium Channels in Membranes of Neuronal-Derived Cells [PDF]

open access: yes, 2015
The intrinsic electrical properties of a neuron depend on expression of voltage gated potassium (Kv) channel isoforms, as well as their distribution and density in the plasma membrane.
A Ozaita   +30 more
core   +13 more sources

N-glycosylation is required for secretion and enzymatic activity of human hyaluronidase1

open access: yesFEBS Open Bio, 2014
Hyaluronidase1 (HYAL1) is a hydrolytic enzyme that degrades hyaluronic acid (HA) and has three predicted N-glycosylation sites at Asn99, Asn216, and Asn350. In this report, we show the functional significance of N-glycosylation on HYAL1 functions.
Yuki Goto   +5 more
doaj   +1 more source

Comparison of Fc N-Glycosylation of Pharmaceutical Products of Intravenous Immunoglobulin G. [PDF]

open access: yesPLoS ONE, 2015
Intravenous immunoglobulin (IVIg) products from different pharmaceutical companies vary in composition, in part because of the selected blood donors and production process.
Willem Jan R Fokkink   +5 more
doaj   +1 more source

N-glycosylation site occupancy in serum glycoproteins using multiple reaction monitoring liquid chromatography-mass spectrometry [PDF]

open access: yes, 2007
Congenital disorders of glycosylation (CDGs) are a family of N-linked glycosylation defects associated with severe clinical manifestations. In CDG type-I, deficiency of lipid-linked oligosaccharide assembly leads to the underoccupancy of N-glycosylation ...
Hennet, T   +2 more
core   +1 more source

Protein glycosylation as a diagnostic and prognostic marker of chronic inflammatory gastrointestinal and liver diseases [PDF]

open access: yes, 2020
Glycans are sequences of carbohydrates that are added to proteins or lipids to modulate their structure and function. Glycans modify proteins required for regulation of immune cells, and alterations have been associated with inflammatory conditions.
Callewaert, Nico   +6 more
core   +1 more source

Differential Analysis of N-glycopeptide Abundance and N-glycosylation Site Occupancy for Studying Protein N-glycosylation Dysregulation in Human Disease

open access: yesBio-Protocol, 2021
Protein N-glycosylation plays a vital role in diverse cellular processes, and dysregulated N-glycosylation is implicated in a variety of human diseases including neurodegenerative disorders and cancer.
Qi Zhang   +3 more
doaj   +1 more source

An enzyme-based screening system for the rapid assessment of protein N-glycosylation efficiency in yeast [PDF]

open access: yes, 2017
N-Glycosylation efficiency is a key parameter when studying components of the protein N-glycosylation pathway, but was recently also recognized as an important factor in the production of glycosylated proteins. We have developed a novel assay to quantify
Aebi, Markus, Frey, Alexander D.
core   +1 more source

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