Results 21 to 30 of about 13,659,719 (307)

ERO1 alpha deficiency impairs angiogenesis by increasing N-glycosylation of a proangiogenic VEGFA

Redox Biology, 2022
N-glycosylation and disulfide bond formation are two essential steps in protein folding that occur in the endoplasmic reticulum (ER) and reciprocally influence each other.
Ersilia Varone, Alexander Chernorudskiy, Alessandro Cherubini, Angela Cattaneo, Angela Bachi, Stefano Fumagalli, Gizem Erol, Marco Gobbi, Michael J. Lenardo, Nica Borgese, Ester Zito   +10 more
doaj   +1 more source

Differential Effects of D-Galactose Supplementation on Golgi Glycosylation Defects in TMEM165 Deficiency

Frontiers in Cell and Developmental Biology, 2022
Glycosylation is a ubiquitous and universal cellular process in all domains of life. In eukaryotes, many glycosylation pathways occur simultaneously onto proteins and lipids for generating a complex diversity of glycan structures.
Zoé Durin, Marine Houdou, Willy Morelle, Lydia Barré, Aurore Layotte, Dominique Legrand, Mohamed Ouzzine, François Foulquier   +7 more
doaj   +1 more source

Studying Lactoferrin N-Glycosylation [PDF]

International Journal of Molecular Sciences, 2017
Lactoferrin is a multifunctional glycoprotein found in the milk of most mammals. In addition to its well-known role of binding iron, lactoferrin carries many important biological functions, including the promotion of cell proliferation and differentiation, and as an anti-bacterial, anti-viral, and anti-parasitic protein.
Sercan Karav, J. German, Camille Rouquié, Annabelle Le Parc, Daniela Barile   +4 more
openaire   +5 more sources

Autosomal Recessive Dilated Cardiomyopathy due to DOLK Mutations Results from Abnormal Dystroglycan O-Mannosylation [PDF]

, 2011
Genetic causes for autosomal recessive forms of dilated cardiomyopathy (DCM) are only rarely identified, although they are thought to contribute considerably to sudden cardiac death and heart failure, especially in young children.
van Reeuwijk, Jeroen, Schuurs-Hoeijmakers, Janneke H. M., Lehle Ludwig, Schuurs-Hoeijmakers, J.H., Lorber, A., Lorber, Avraham, Zucker, N., Janneke H M Schuurs-Hoeijmakers, Zucker Nili, Grünewald Stephanie, de Brouwer Arjan P. M., Wevers, R.A., Steenbergen, Gerry, Lefeber, D.J., Steenbergen, G.C., Lammens, M.M.Y., Ron A Wevers, Adam Jozwiak, Schuurs-Hoeijmakers, Janneke H M, Wevers, Ron A., Huijben, K., Grunewald, S., Lefeber, Dirk J, Gruenewald, Stephanie, Wevers, Ron A, Willem M R van den Akker, van den Akker, Willem M. R., de Brouwer, Arjan P. M., van Bokhoven, H., Steenbergen Gerry, Hanna Mandel, Riemersma Moniek, Riemersma, Moniek, Gerry Steenbergen, Riemersma, M., Stephanie Grünewald, Lammens, Martin, Dirk J Lefeber, Eva Morava, Absmanner, B., Morava Eva, Verrijp, K., Knopf, Carlos, Verrijp, Kiek, Knopf, C., van Bokhoven, Hans, Brouwer, A.P.M. de, van den Akker Willem M. R., Nili Zucker, Jeroen van Reeuwijk, Mandel, H., Lammens Martin, Martin Lammens, Jozwiak, Adam, Carlos Knopf, de Brouwer, A.P., Absmanner, Birgit, Mandel Hanna, Hans van Bokhoven, Reeuwijk, J. van, Jozwiak, A., Ludwig Lehle, Schuurs-Hoeijmakers Janneke H. M., Lehle, Ludwig, Lorber Avraham, Huijben Karin, van Reeuwijk, J., Zucker, Nili, Hijben, K., van den Akker, Willem M R, Birgit Absmanner, Absmanner Birgit, Avraham Lorber, Steenbergen, G., Huijben, Karin, Wevers Ron A., Mandel, Hanna, Knopf Carlos, Kapusta, Livia, Lefeber, Dirk J., Livia Kapusta, Verrijp Kiek, van den Akker, W.M., Grunewald, Stephanie, van Bokhoven Hans, Morava, E., Akker, W.M.R. van den, Moniek Riemersma, Bokhoven, H. van, Lefeber Dirk J., Jozwiak Adam, Lehle, L., Kapusta, L., Lammens, M., van Reeuwijk Jeroen, Karin Huijben, Schuurs-Hoeijmakers, J.H.M., Morava, Eva, Kapusta Livia, Arjan P M de Brouwer, Kiek Verrijp   +100 more
core   +4 more sources

Expanding roles of N-glycosylation in the endoplasmic reticulum. [PDF]

Trends Cell Biol
N-linked glycosylation in the endoplasmic reticulum (ER), catalyzed by two oligosaccharyltransferase (OST) complexes, has long been viewed as a constitutive post-translational modification. Recent discoveries suggest that OST complexes play a much more plastic and directive role in regulating ER processes.
Ma M, Rohatgi R.
europepmc   +4 more sources

Stereoselective N-Glycosylation by Staudinger Ligation [PDF]

Organic Letters, 2004
AbstractFor Abstract see ChemInform Abstract in Full Text.
Yi, He, Ronald J, Hinklin, Jiyoung, Chang, Laura L, Kiessling   +3 more
openaire   +2 more sources

Unraveling the Mechanism of Protein N-Glycosylation [PDF]

Journal of Biological Chemistry, 2005
Asparagine-linked glycosylation is the most ubiquitous protein co-translational modification in the endoplasmic reticulum (ER). The enzyme that catalyzes this process is called oligosaccharyl transferase (OT). It catalyzes the transfer of an oligosaccharyl moiety (Glc3Man9GlcNAc2) from the dolichol-linked pyrophosphate donor to the side chain of Asn ...
Lennarz, WJ, Yan, A
openaire   +4 more sources

Analysis of N-Glycosylation Sites in HIV glycoprotein 160 [PDF]

, 2011
HIV infection is a condition caused by the human immunodeficiency virus. The condition gradually destroys the immune system, which makes it harder for the body to fight infections. HIV presents a complex knot for scientists to unravel.
Rajendra Mandage
core   +1 more source

Route Efficiency Assessment and Review of the Synthesis of β-Nucleosides via N-Glycosylation of Nucleobases [PDF]

, 2020
Instead of focusing on maximizing glycosylation yield, future syntheses of nucleosides via N-glycosylation should aim to use shorter routes, fewer protecting groups and less chromatography to achieve more efficient and sustainable processes, as this E ...
Anke, Kurreck, M. Rhia L., Stone, Peter, Neubauer, Felix, Kaspar   +3 more
core   +2 more sources

The Impact of N-Glycosylation on the Functions of Polysialyltransferases [PDF]

Journal of Biological Chemistry, 2001
Poly-alpha-2,8-sialic acid (polysialic acid) is a post-translational modification of the neural cell adhesion molecule (NCAM) and an important regulator of neuronal cell-cell interactions. The synthesis of polysialic acid depends on the two polysialyltransferases ST8SiaII and ST8SiaIV.
M, Mühlenhoff, A, Manegold, M, Windfuhr, B, Gotza, R, Gerardy-Schahn   +4 more
openaire   +2 more sources