Results 31 to 40 of about 10,478,036 (300)

The essential endoplasmic reticulum chaperone Rot1 is required for protein N- and O-glycosylation in yeast [PDF]

, 2012
Rot1 is an essential yeast protein originally shown to be implicated in such diverse processes such as β-1,6-glucan synthesis, actin cytoskeleton dynamics, or lysis of autophagic bodies.
Lehle, L., Palamarczyk, G., Palamarczyk, Grazyna, Pasikowska, M., Pasikowska, Monika, Grazyna Palamarczyk, Monika Pasikowska, Ludwig Lehle, Lehle, Ludwig   +8 more
core   +1 more source

Structural characteristics around O-glycosylation sites in mammalian proteins

Journal of Biomechanical Science and Engineering, 2014
The structural characteristic that O-glycan sugars prefer to bind to the regions forming β-strand structures is reported in this paper. While N-acetylglucosamine (GlcNAc) and mannose (Man) modification sites were contained in β-strand structures, fucose (
Kenji ETCHUYA, Yuri MUKAI
doaj   +1 more source

Sugar Type Discrimination in O-glycosylation Based on Protein Primary Sequences

Journal of Biomechanical Science and Engineering, 2013
Glycosylation is one of the most important protein post-translational modifications. O-glycosylation plays important roles in biological functions. There are several variations of O-glycosylation, with each having a different function.
Kenji ETCHUYA, Yuri MUKAI
doaj   +1 more source

A Chemoenzymatic Strategy toward Understanding O-GlcNAc Glycosylation in the Brain [PDF]

, 2007
Posttranslational modification to proteins represents a fundamental mechanism by which protein function is extended and elaborated. In the brain, modifications such as phosphorylation play critical roles in mediating neuronal communication and ...
Khidekel, Nelly
core   +1 more source

RNAi-Mediated Silencing of Pgants Shows Core 1 O-Glycans Are Required for Pupation in Tribolium castaneum

Frontiers in Physiology, 2021
Protein glycosylation is one of the most common and most important post-translational modifications. Despite the growing knowledge on N-glycosylation, the research on O-glycosylation is lagging behind.
Weidong Li, Weidong Li, Kristof De Schutter, Els J. M. Van Damme, Guy Smagghe   +4 more
doaj   +1 more source

O-glycosylation disorders pave the road for understanding the complex human O-glycosylation machinery [PDF]

Current Opinion in Structural Biology, 2019
Over 100 human Congenital Disorders of Glycosylation (CDG) have been described. Of these, about 30% reside in the O-glycosylation pathway. O-glycosylation disorders are characterized by a high phenotypic variability, reflecting the large diversity of O-glycan structures.
van Tol, W., Wessels, H.J., Wessels, H.J., Lefeber, D.J., Lefeber, D.J.   +4 more
openaire   +2 more sources

Cracking the “Sugar Code”: A Snapshot of N- and O-Glycosylation Pathways and Functions in Plants Cells

Frontiers in Plant Science, 2021
Glycosylation is a fundamental co-translational and/or post-translational modification process where an attachment of sugars onto either proteins or lipids can alter their biological function, subcellular location and modulate the development and ...
Richard Strasser, Georg Seifert, Monika S. Doblin, Monika S. Doblin, Kim L. Johnson, Kim L. Johnson, Colin Ruprecht, Fabian Pfrengle, Antony Bacic, Antony Bacic, José M. Estevez, José M. Estevez, José M. Estevez   +12 more
doaj   +1 more source

O-Glycosylation of the V2 vasopressin receptor [PDF]

Glycobiology, 1999
The human V2 vasopressin receptor contains one consensus site for N-linked glycosylation at asparagine 22 in the predicted extracellular amino terminal segment of the protein. This segment also contains clusters of serines and threonines that are potential sites for O-glycosylation.
H, Sadeghi, M, Birnbaumer
openaire   +2 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   +1 more source

GlcNAc inhibits MAPKs pathway in rat corpus cavernosum smooth muscle cells via O-glycosylation-dependent pathway

Di-san junyi daxue xuebao, 2019
Objective To investigate the effect of β-N-acetylglucosamine (GlcNAc) on the mitogen-activated protein kinases (MAPKs) pathway in rat penile cavernosum smooth muscle cells.
LIU Boshen, WANG Yi, GUO Linmin, SUN Zhongyi   +3 more
doaj   +1 more source