Examples of 'o-linked glycosylation' in a sentence
Meaning of "o-linked glycosylation"
O-linked glycosylation: A type of post-translational modification of proteins where a sugar molecule is added to the oxygen atom of serine or threonine residues. This modification plays a crucial role in protein folding, stability, and function
How to use "o-linked glycosylation" in a sentence
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o-linked glycosylation
O-linked glycosylation is similar to that in humans.
There is no consensus sequence for O-linked glycosylation.
O-linked glycosylation is difficult to predict due to lack of consensus recognition sequences.
These sites are both for O-linked glycosylation.
O-linked glycosylation occurs in the Golgi apparatus.
Five sites were identified as possible O-linked glycosylation sites.
Plant O-linked glycosylation may be attached at serine, threonine or hydroxyproline residues.
There is no evidence for O-linked glycosylation.
Normally, O-linked glycosylation occurs on the side chain of a serine or threonine residue.
A mucin domain comprises or alternatively consists of an O-linked glycosylation site.
Several sites for O-linked glycosylation occur in each tandem repeat.
There is great diversity in the structures created by O-linked glycosylation.
There is no known or documented O-linked glycosylation on the extracellular domain of human GITR.
In some embodiments the therapeutic proteins include an O-linked glycosylation site.
By modified it is meant that the O-linked glycosylation domain has an altered glycosylation pattern.
See also
Glycosylating said human growth hormone polypeptide at the O-linked glycosylation site.
O-linked glycosylation occurs at a later stage during protein processing, probably in the Golgi apparatus.
This amino acid is found within the O-linked glycosylation sequence.
There are five O-linked glycosylation sites available within each MUC1 VNTR monomer.
The sequon polypeptide comprises an exogenous O-linked glycosylation sequence of the invention.
O-linked glycosylation is not detected in naturally occurring KLK1.
One of the most striking features of the MUC1 molecule is its extensive O-linked glycosylation.
MUC1 is a glycoprotein with extensive O-linked glycosylation of its extracellular domain.
Analysis of the cDNA sequences revealed 2 potential N-linked glycosylation sites and possible O-linked glycosylation sites.
Similarly, sites for O-linked glycosylation can also be added.
Keratan sulfate may modify core proteins through N-linked glycosylation or O-linked glycosylation of the proteoglycan.
O-linked glycosylation takes place at serine or threonine residues Tanner et al ., Biochim.
Substitutional or deletional mutagenesis is employed to eliminate N - or O-linked glycosylation sites.
To affect O-linked glycosylation of a polypeptide, one would modify serine and / or threonine residues.
The hydroxyl side-chain can undergo O-linked glycosylation.
Several possible O-linked glycosylation sites are present in the IGF-1 sequence.
In fact, there is no prior art regarding O-linked glycosylation in GPCRs.
However, the O-linked glycosylation site is exclusively in the Golgi complex.
Preferred sites for substitution are the N - and O-linked glycosylation sites.
The known N-linked and O-linked glycosylation sites for belatacept are shown in Figure 1A.
Wild type Factor VIIa contains two N-linked and two O-linked glycosylation sites.
Interestingly, O-linked glycosylation analysis did demonstrate existence of additional O-linked sites ( Figure 3C ).
FGF-21 muteins may comprise a lesser number for O-linked glycosylation sites.
At Thr 71, a potential O-linked glycosylation site is located.
Post-translational modifications include, but is not limited to, N-and O-linked glycosylation.
Therefore, it was determined whether O-linked glycosylation affects the binding of 28F3 to human GITR.
PH20 hyaluronidases also contains O-linked glycosylation sites.
Figure 3A - 3D identify the O-linked glycosylation at hidden sites.
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Examples of using Glycosylation
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Further glycosylation of specific hydroxylysine residues occurs
Several methods of modulating glycosylation of proteins are known
Protein glycosylation may be analyzed in a number of ways
