Results 31 to 40 of about 13,659,719 (307)

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

Frontiers 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, Stefan N. eConstantinescu   +1 more
doaj   +1 more source

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

PLoS 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, David Falck, Tom C M Santbergen, Ruth Huizinga, Manfred Wuhrer, Bart C Jacobs   +5 more
doaj   +1 more source

SRD5A3 is required for converting polyprenol to dolichol and is mutated in a congenital glycosylation disorder. [PDF]

, 2010
N-linked glycosylation is the most frequent modification of secreted and membrane-bound proteins in eukaryotic cells, disruption of which is the basis of the congenital disorders of glycosylation (CDGs).
Hudson H. Freeze, Silhavy, J.L., Christian R.H. Raetz, Al-Gazali, Lihadh, Swistun, Dominika, Dusica Babovic-Vuksanovic, Guan, Z., Blümel, Peter, Sykut-Cegielska, J., Hans van Bokhoven, Bokhoven, J.H.L.M. van, Ludwig Lehle, Lehle, Ludwig, Wevers, R.A., Al-Gazali, L., Houliston, S., Dobyns, W.B., Bassam R. Ali, Lefeber, D.J., Ali, Bassam R., Raetz, Christian R.H., Dirk J. Lefeber, Guan, Ziqiang, Ron A. Wevers, Hans Hombauer, Maciej Adamowicz, Jolanta Sykut-Cegielska, Stephanie L. Bielas, Ng, B.G., Freeze, H.H., Ewa Swiezewska, Wevers, Ron A., William B. Dobyns, Gleeson, Joseph G., Bobby G. Ng, Cantagrel, Vincent, Ng, Bobby G., Swiezewska, Ewa, Lefeber, Dirk J., De Brouwer, Arjan P., Houliston, Scott, Adamowicz, M., Silhavy, Jennifer L., Lihadh Al-Gazali, Ziqiang Guan, Éva Morava, Dobyns, William B., Adamowicz, Maciej, Morava, E., Babovic-Vuksanovic, Dusica, Raetz, C.R., Vincent Cantagrel, Lehle, L., Hombauer, H., Scott Houliston, Freeze, Hudson H., Jennifer L. Silhavy, Swistun, D., Blumel, P., Babovic-Vuksanovic, D., Cantagrel, V., Gleeson, J.G., Peter Blümel, Sykut-Cegielska, Jolanta, Arjan P. De Brouwer, Morava, Éva, Joseph G. Gleeson, Brouwer, A.P.M. de, van Bokhoven, Hans, Swiezewska, E., Hombauer, Hans, Dominika Swistun, Bielas, S.L., Ali, B.R., Bielas, Stephanie L.   +74 more
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N-glycosylation is required for secretion and enzymatic activity of human hyaluronidase1

FEBS 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, Yuki Niwa, Takehiro Suzuki, Shiho Uematsu, Naoshi Dohmae, Siro Simizu   +5 more
doaj   +1 more source

Proteome-wide analysis of single-nucleotide variations in the N-glycosylation sequon of human genes. [PDF]

PLoS ONE, 2012
N-linked glycosylation is one of the most frequent post-translational modifications of proteins with a profound impact on their biological function.
Raja Mazumder, Krishna Sudeep Morampudi, Mona Motwani, Sona Vasudevan, Radoslav Goldman   +4 more
doaj   +1 more source

LINC00173 promotes Wilms’ tumor progression through MGAT1-mediated MUC3A N-glycosylation

, 2022
Recent studies have unveiled that LINC00173 promotes small cell lung cancer progression. However, LINC00173 has not been studied in Wilms’ tumor (WT).
Qingliang Zhu (12484975), Deming Zhan (12484978), Haoliang Xue (6033464), Yongguo Yang (11021152), Yankun Chong (12484981), Peng Zhu (277243)   +5 more
core   +1 more source

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

JIMD 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, Sandrine Duvet, Claire Douillard, François Foulquier, André Klein   +4 more
doaj   +1 more source

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

Bio-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, Cheng Ma, Lian Li, Lih-Shen Chin   +3 more
doaj   +1 more source

Role of N-Glycosylation in Human Angiotensinogen [PDF]

Journal of Biological Chemistry, 1998
Human angiotensinogen, the specific substrate of renin, is a heterogeneous glycoprotein constitutively secreted by the liver. Different glycosylation levels may be responsible for its heterogeneity. It contains four putative asparagine-linked glycosylation sites (Asn-X-Ser/Thr). Systematic site-directed mutagenesis (Asn replaced with Gln) of these four
A P, Gimenez-Roqueplo, J, Célérier, G, Lucarelli, P, Corvol, X, Jeunemaitre   +4 more
openaire   +2 more sources

Research advances of protein N-glycosylation’s biological functions and analytical methods and its role in kidney disease

Linchuang shenzangbing zazhi, 2021
As one of the most important post-translational modifications, glycosylation plays a significant role in the functions of proteins.N-glycosylation exerts critical effects in different biological processes among various forms of glycosylation, whereas ...
任伟夫, 边琪
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