Examples of 'n-glycosylation sites' in a sentence
Meaning of "n-glycosylation sites"
N-glycosylation sites are specific locations within a protein where a sugar molecule (glycan) can attach. This post-translational modification plays a crucial role in protein folding, stability, and function. N-glycosylation sites are recognized by enzymes called glycosyltransferases, which add the sugar molecules to the protein backbone
How to use "n-glycosylation sites" in a sentence
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n-glycosylation sites
The five putative N-glycosylation sites are squared.
We note that the protein contains six potential N-glycosylation sites.
The putative N-glycosylation sites are indicated by asterisks.
It also contains four predicted N-glycosylation sites.
The potential N-glycosylation sites are underlined twice.
They all have four potential N-glycosylation sites.
The potential N-glycosylation sites are underlined in each sequence.
We note that the protein contains seven potential N-glycosylation sites.
The potential N-glycosylation sites are shown as green balls.
Exemplary derivatives of hedgehog proteins include polypeptides which lack N-glycosylation sites e . g.
The potential N-glycosylation sites are in bold.
The primary sequence of these fusión proteins contains four possible N-glycosylation sites.
Attachment of glycans at N-glycosylation sites is shown.
Canonical N-glycosylation sites do not appear within the sequence.
Putative transmembrane domains are shaded, and predicted N-glycosylation sites are marked with circles.
See also
Ten potential N-glycosylation sites are marked by closed circles.
Glycosylation sites that can be introduced or eliminated include N-glycosylation sites and O-glycosylation sites.
Four potential N-glycosylation sites are located in the extracelluar region.
We note that the protein is cysteine-rich and contains eleven potential N-glycosylation sites.
The asparagines of the N-glycosylation sites are double underlined.
Computer analysis predicts a long transmembrane domain close to the N-terminus and two N-glycosylation sites.
Four potential N-glycosylation sites are located in the extracellular region.
Asterisks indicate the potential N-glycosylation sites.
There are 6 possible N-glycosylation sites present in the presumed extracellular domain.
The extracellular domain of RET contains nine N-glycosylation sites.
Particular N-glycosylation sites are not required for activity, whereas others are.
There are no potential N-glycosylation sites.
Potential N-glycosylation sites should be conserved if mannosylation of the protein is desired.
Attachment of glycans at each of the N-glycosylation sites accounts for the observed mass.
Potential N-glycosylation sites are underlined and putative transmembrane segments are overlined.
Another option is inactivation of N-glycosylation sites by site-specific mutagenesis.
Potential N-glycosylation sites and an RGD tripeptide, potential cell attachment site are underlined by asterics.
Glycosylation In the sequence of FcYRIIb three potential N-glycosylation sites are found.
In one embodiment, additional N-glycosylation sites are introduced into basiliximab light chain.
N-glycosylation sites were predicted using the algorithm of Brunak Gupta and Brunak, Pac.
Such one or more additional N-glycosylation sites are not always glycosylated.
Table 6 indicates the sequence of the RSV glycoprotein G with potential N-glycosylation sites underlined.
There are nine potential N-glycosylation sites on the extracellular domain of the receptor.
The extracellular domain includes 7 potential N-glycosylation sites.
For example, N-glycosylation sites on the same protein may contain different carbohydrate structures.
The extracellular domain contains four potential N-glycosylation sites and three Cys residues.
The two additional N-glycosylation sites result from amino acid substitutions in the erythropoietin peptide backbone.
No.2 deduced from the nucleotide sequence, where only three N-glycosylation sites were located.
Possible extracellular N-glycosylation sites are marked with an asterisk above the amino acid residue.
There are several potential N-myristorylation sites, 3 phosphorylation sites, and no evidence of N-glycosylation sites.
Four predicted N-glycosylation sites in PSCA are indicated by asterisks.
The extracellular domain contains 3 putative divalent cation-binding sequences and 19 potential N-glycosylation sites.
Three potential N-glycosylation sites are seen.
N-glycosylation sites may be added.
This is a result from the increased N-glycosylation sites on ASIC1a and ASIC2a.
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Examples of using N-glycosylation
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N-glycosylation signals and the stop codon are indicated by asterisks
A potential site of N-glycosylation is present in this loop
N-glycosylation in various host cells has been also addressed in further studies
