Results 11 to 20 of about 14,762,033 (298)

Mucin-Type O-Glycosylation in Gastric Carcinogenesis [PDF]

open access: yesBiomolecules, 2016
Mucin-type O-glycosylation plays a crucial role in several physiological and pathological processes of the gastric tissue. Modifications in enzymes responsible for key glycosylation steps and the consequent abnormal biosynthesis and expression of their ...
Celso Reis   +13 more
core   +6 more sources

N- and O-glycosylation analysis of human C1-inhibitor reveals extensive mucin-type O-glycosylation

open access: yesMolecular & Cellular Proteomics, 2018
Human C1-inhibitor (C1-Inh) is a serine protease inhibitor and the major regulator of the contact activation pathway as well as the classical and lectin complement pathways. It is known to be a highly glycosylated plasma glycoprotein.
Engel, R.   +28 more
core   +8 more sources

O-Glycosylation [PDF]

open access: yesMedical Mycology, 2001
O-Glycosylation in many fungal species is initiated in the endoplasmic reticulum by protein mannosyltransferases (Pmt-proteins), which transfer mannose to serine or threonine residues, and it is completed by mannosyltransferases (Mnt-proteins) in the Golgi.
J F, Ernst, S K, Prill
openaire   +2 more sources

O-Glycosylation of snails [PDF]

open access: yesGlycoconjugate Journal, 2012
The glycosylation abilities of snails deserve attention, because snail species serve as intermediate hosts in the developmental cycles of some human and cattle parasites. In analogy to many other host-pathogen relations, the glycosylation of snail proteins may likewise contribute to these host-parasite interactions. Here we present an overview on the O-
Stepan, Herwig   +5 more
openaire   +2 more sources

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

open access: yes, 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.   +8 more
core   +2 more sources

Chemical O‐Glycosylations: An Overview [PDF]

open access: yesChemistryOpen, 2016
AbstractThe development of glycobiology relies on the sources of particular oligosaccharides in their purest forms. As the isolation of the oligosaccharide structures from natural sources is not a reliable option for providing samples with homogeneity, chemical means become pertinent.
Das, Rituparna, Mukhopadhyay, Balaram
openaire   +2 more sources

Nucleocytoplasmic O-glycosylation in protists [PDF]

open access: yesCurrent Opinion in Structural Biology, 2019
O-Glycosylation is an increasingly recognized modification of intracellular proteins in all kingdoms of life, and its occurrence in protists has been investigated to understand its evolution and its roles in the virulence of unicellular pathogens. We focus here on two kinds of glycoregulation found in unicellular eukaryotes: one is a simple O-fucose ...
Christopher M, West, Hyun W, Kim
openaire   +2 more sources

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

open access: yes, 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   +100 more
core   +5 more sources

N- and O-Glycosylation in the Murine Synaptosome [PDF]

open access: yesMolecular & Cellular Proteomics, 2013
We present the first large scale study characterizing both N- and O-linked glycosylation in a site-specific manner on hundreds of proteins. We demonstrate that a lectin-affinity fractionation step using wheat germ agglutinin enriches not only peptides carrying intracellular O-GlcNAc, but also those bearing ER/Golgi-derived N- and O-linked carbohydrate ...
Trinidad, Jonathan C   +3 more
openaire   +3 more sources

A Sweet Warning: Mucin-Type O-Glycans in Cancer

open access: yesCells, 2022
Glycosylation is a common post-translational modification process of proteins. Mucin-type O-glycosylation is an O-glycosylation that starts from protein serine/threonine residues.
Yuhan Zhang   +6 more
doaj   +1 more source

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