Literature summary extracted from

Choi, Y.; Lee, J.H.; Hwang, S.; Kim, J.K.; Jeong, K.; Jung, S.
Retardation of the unfolding process by single N-glycosylation of ribonuclease A based on molecular dynamics simulations (2008), Biopolymers, 89, 114-123.

Organism

EC Number	Organism	UniProt	Comment	Textmining
4.6.1.18	Bos taurus	P61823	-	-

Posttranslational Modification

EC Number	Posttranslational Modification	Comment	Organism
4.6.1.18	glycoprotein	unfolding molecular dynamics simulations of glycosylated and unglycosylated enzyme. Attachment of monomeric N-acetylglucosyamine to residue N34 results in a change of denaturing process. The glycosylated enzyme remains more stable due to preserved non-local interactions	Bos taurus

Renatured (Commentary)

EC Number	Renatured (Comment)	Organism
4.6.1.18	unfolding molecular dynamics simulations of glycosylated and unglycosylated enzyme. Attachment of monomeric N-acetylglucosyamine to residue N34 results in a change of denaturing process. The glycosylated enzyme remains more stable due to preserved non-local interactions	Bos taurus

Source Tissue

EC Number	Source Tissue	Comment	Organism	Textmining
4.6.1.18	pancreas	-	Bos taurus	-

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Release 2023.1 (January 2023)