Add to ORKGOver half of all proteins are glycosylated, and alterations in glycosylation have been observed in numerous physiological and pathological processes. Attached glycans significantly affect protein function; but, contrary to polypeptides, they are not directly encoded by genes, and the complex processes that regulate their assembly are poorly understood. A novel approach combining genome-wide association and high-throughput glycomics analysis of 2,705 individuals in three population cohorts showed that common variants in the Hepatocyte Nuclear Factor 1a (HNF1a) and fucosyltransferase genes FUT6 and FUT8 influence N-glycan levels in human plasma. We show that HNF1a and its downstream target HNF4
Glycosylation is among the most common post-translational protein modifications. Glycans are complex...
<div><p>N-linked glycosylation is one of the most frequent post-translational modifications of prote...
Current estimates indicate that genes that regulate N- and O-glycosylation of glycoproteins make up ...
Over half of all proteins are glycosylated, and alterations in glycosylation have been observed in n...
Glycosylation is a common post-translational modification of proteins. Glycosylation is associated w...
Protein glycosylation is a ubiquitous modification that affects the structure and function of protei...
Human protein glycosylation is a complex process, and its in vivo regulation is poorly understood. C...
A recent genome-wide association study identified hepatocyte nuclear factor 1-a (HNF1A) as a key reg...
Human protein glycosylation is a complex process, and its in vivo regulation is poorly understood. C...
The majority of human proteins are post-translationally modified by covalent addition of one or mor...
The majority of human proteins are post-translationally modified by covalent addition of one or more...
Most human proteins are glycosylated. Attachment of complex oligosaccharides to the polypeptide part...
Human protein glycosylation is a complex process, and its in vivo regulation is poorly understood. C...
HPLC analysis of N-glycans quantified levels of the biantennary glycan (A2) in plasma proteins of 92...
Effector functions of immunoglobulin G (IgG) are regulated by the composition of a glycan moiety, th...
Glycosylation is among the most common post-translational protein modifications. Glycans are complex...
<div><p>N-linked glycosylation is one of the most frequent post-translational modifications of prote...
Current estimates indicate that genes that regulate N- and O-glycosylation of glycoproteins make up ...
Over half of all proteins are glycosylated, and alterations in glycosylation have been observed in n...
Glycosylation is a common post-translational modification of proteins. Glycosylation is associated w...
Protein glycosylation is a ubiquitous modification that affects the structure and function of protei...
Human protein glycosylation is a complex process, and its in vivo regulation is poorly understood. C...
A recent genome-wide association study identified hepatocyte nuclear factor 1-a (HNF1A) as a key reg...
Human protein glycosylation is a complex process, and its in vivo regulation is poorly understood. C...
The majority of human proteins are post-translationally modified by covalent addition of one or mor...
The majority of human proteins are post-translationally modified by covalent addition of one or more...
Most human proteins are glycosylated. Attachment of complex oligosaccharides to the polypeptide part...
Human protein glycosylation is a complex process, and its in vivo regulation is poorly understood. C...
HPLC analysis of N-glycans quantified levels of the biantennary glycan (A2) in plasma proteins of 92...
Effector functions of immunoglobulin G (IgG) are regulated by the composition of a glycan moiety, th...
Glycosylation is among the most common post-translational protein modifications. Glycans are complex...
<div><p>N-linked glycosylation is one of the most frequent post-translational modifications of prote...
Current estimates indicate that genes that regulate N- and O-glycosylation of glycoproteins make up ...