Results 41 to 50 of about 10,628,077 (304)

N-glycan breakdown by bacterial CAZymes

open access: yesEssays in Biochemistry, 2023
Abstract The modification of proteins by N-glycans is ubiquitous to most organisms and they have multiple biological functions, including protecting the adjoining protein from degradation and facilitating communication or adhesion between cells, for example. Microbes have evolved CAZymes to deconstruct different types of N-glycans and
openaire   +2 more sources

Co-Expression of NEU2 and GBA3 Causes a Drastic Reduction in Cytosolic Sialyl Free N-glycans in Human MKN45 Stomach Cancer Cells—Evidence for the Physical Interaction of NEU2 and GBA3

open access: yesBiomolecules, 2015
It is well known that the “free” form of glycans that are structurally related to asparagine (N)-linked glycans (“free N-glycans”) are found in a wide variety of organisms.
Li Wang   +5 more
doaj   +1 more source

A Method to the Madness of N-Glycan Complexity? [PDF]

open access: yesCell, 2007
Cell-surface glycoprotein receptors have varying numbers of N-glycan sites. In this issue of Cell, Lau et al. (2007) report that increasing intracellular UDP-GlcNAc leads to increased branching of N-glycans, increased receptor association with cell-surface galectin-3, and enhanced signaling.
openaire   +2 more sources

Structure of Ten Free N-Glycans in Ripening Tomato Fruit (Arabinose Is a Constituent of a Plant N-Glycan) [PDF]

open access: yesPlant Physiology, 1993
The concentration-dependent stimulatory and inhibitory effect of N-glycans on tomato (Lycopersicon esculentum Mill.) fruit ripening was recently reported (B. Priem and K.C. Gross [1992] Plant Physiol 98: 399-401). We report here the structure of 10 free N-glycans in mature green tomatoes.
B, Priem   +3 more
openaire   +2 more sources

Identification and comparison of N-glycome profiles from common dietary protein sources

open access: yesFood Chemistry: X
The N-glycomes of bovine whey, egg white, pea, and soy protein isolates are described here. N-glycans from four protein isolates were analyzed by HILIC high performance liquid chromatography and quadrupole time-of-flight tandem mass spectrometry (HILIC ...
Matthew Bolino   +6 more
doaj   +1 more source

Genomic and Biochemical Analysis of N Glycosylation in the Mushroom-Forming Basidiomycete Schizophyllum commune

open access: yes, 2009
N-linked glycans of Schizophyllum commune consist of Man(5-9)GlcNAc(2) structures. Lack of further glycan maturation is explained by the absence of genes encoding such functions in this and other homobasidiomycetes.
de Jong, J.F.   +14 more
core   +1 more source

Analysis of Invertebrate and Protist N-Glycans [PDF]

open access: yes, 2016
N-glycans from invertebrates and protists have often unusual structures which present analytical challenges. Both core and antennal modifications can be quite different from the more familiar vertebrate glycan motifs; thereby, contrary to the concept that "simple" organisms have "simple" N-glycans, rather complex oligosaccharides structures, including ...
Alba, Hykollari   +3 more
openaire   +2 more sources

Advances in understanding N-glycosylation structure, function, and regulation in health and disease

open access: yesEuropean Journal of Cell Biology, 2021
N-linked glycosylation is a post-translational modification crucial for membrane protein folding, stability and other cellular functions. Alteration of membrane protein N-glycans is implicated in wide range of pathological conditions including cancer ...
Sally Esmail, Morris F. Manolson
doaj   +1 more source

Precursor ion scanning for detection and structural characterization of heterogeneous glycopeptide mixtures

open access: yes, 2002
The structure of N-linked glycans is determined by a complex, anabolic, intracellular pathway but the exact role of individual glycans is not always clear.
Gill, A C   +7 more
core   +1 more source

MALDI-MS/MS with traveling wave ion mobility for the structural analysis of N-Linked glycans [PDF]

open access: yes, 2012
The preference for singly charged ion formation by MALDI makes it a better choice than electrospray ionization for profiling mixtures of N-glycans.
Crispin, Max   +7 more
core   +1 more source

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