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Asparagine and Glycosylation

Shortcuts: Differences, Similarities, Jaccard Similarity Coefficient, References.

Difference between Asparagine and Glycosylation

Asparagine vs. Glycosylation

Asparagine (symbol Asn or N), is an α-amino acid that is used in the biosynthesis of proteins. Glycosylation (see also chemical glycosylation) is the reaction in which a carbohydrate, i.e. a glycosyl donor, is attached to a hydroxyl or other functional group of another molecule (a glycosyl acceptor).

Similarities between Asparagine and Glycosylation

Asparagine and Glycosylation have 5 things in common (in Unionpedia): Amide, Endoplasmic reticulum, N-Acetylglucosamine, Serine, Threonine.

Amide

An amide (or or), also known as an acid amide, is a compound with the functional group RnE(O)xNR′2 (R and R′ refer to H or organic groups).

Amide and Asparagine · Amide and Glycosylation · See more »

Endoplasmic reticulum

The endoplasmic reticulum (ER) is a type of organelle found in eukaryotic cells that forms an interconnected network of flattened, membrane-enclosed sacs or tube-like structures known as cisternae.

Asparagine and Endoplasmic reticulum · Endoplasmic reticulum and Glycosylation · See more »

N-Acetylglucosamine

N-Acetylglucosamine (N-acetyl-D-glucosamine, or GlcNAc, or NAG) is a monosaccharide and a derivative of glucose.

Asparagine and N-Acetylglucosamine · Glycosylation and N-Acetylglucosamine · See more »

Serine

Serine (symbol Ser or S) is an ɑ-amino acid that is used in the biosynthesis of proteins.

Asparagine and Serine · Glycosylation and Serine · See more »

Threonine

Threonine (symbol Thr or T) is an amino acid that is used in the biosynthesis of proteins.

Asparagine and Threonine · Glycosylation and Threonine · See more »

The list above answers the following questions

Asparagine and Glycosylation Comparison

Asparagine has 68 relations, while Glycosylation has 75. As they have in common 5, the Jaccard index is 3.50% = 5 / (68 + 75).

References

This article shows the relationship between Asparagine and Glycosylation. To access each article from which the information was extracted, please visit:

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