All terms in GO
| Label | Id | Description |
|---|---|---|
| neutrophil degranulation | GO_0043312 |
The regulated exocytosis of secretory granules containing preformed mediators such as proteases, lipases, and inflammatory mediators by a neutrophil.
|
| inulin fructotransferase (DFA-I-forming) activity | GO_0033997 |
Catalysis of the reaction: [(2->1)-beta-D-fructosyl](n) = [(2->1)-beta-D-fructosyl](n-1) + alpha-D-fructofuranose-beta-D-fructofuranose 1,2':1,2'-dianhydride. This reaction is the production of alpha-D-fructofuranose beta-D-fructofuranose 1,2':2,1'-dianhydride (DFA I) by successively eliminating the diminishing (2->1)-beta-D-fructan (inulin) chain from the terminal D-fructosyl-D-fructosyl disaccharide.
|
| positive regulation of eosinophil degranulation | GO_0043311 |
Any process that activates or increases the frequency, rate or extent of eosinophil degranulation.
|
| positive regulation of eosinophil activation | GO_1902568 |
Any process that activates or increases the frequency, rate or extent of eosinophil activation.
|
| negative regulation of eosinophil degranulation | GO_0043310 |
Any process that stops, prevents, or reduces the rate of eosinophil degranulation.
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| negative regulation of eosinophil activation | GO_1902567 |
Any process that stops, prevents or reduces the frequency, rate or extent of eosinophil activation.
|
| chondroitin B lyase activity | GO_0033999 |
Catalysis of the reaction: dermatan sulfate = n 4-deoxy-beta-D-gluc-4-enuronosyl-(1,3)-N-acetyl-D-galactosamine 4-sulfate. This reaction is the eliminative cleavage of dermatan sulfate containing 1,4-beta-D-hexosaminyl and 1,3-beta-D-glucurosonyl or 1,3-alpha-L-iduronosyl linkages to disaccharides containing 4-deoxy-beta-D-gluc-4-enuronosyl groups to yield a 4,5-unsaturated dermatan-sulfate disaccharide (DeltaUA-GalNAC-4S). Chondroitin sulfate B is also known as dermatan sulfate.
|
| GO_0043349 | GO_0043349 | |
| GO_0043348 | GO_0043348 | |
| GO_0043347 | GO_0043347 | |
| N-terminal peptidyl-valine deamination | GO_0018389 |
The deamination of the N-terminal valine residue of a protein to form isobutyrate.
|
| N-terminal protein amino acid deamination, from amino carbon | GO_0018058 |
The oxidative deamination of the alpha carbon of an encoded N-terminal amino acid, to form pyruvic acid retaining an amide bond between its 1-carboxyl group and the adjacent residue. The pyruvate 2-oxo group may become an enzyme active site, or it may be reduced to an alcohol.
|
| N-terminal peptidyl-valine condensation with pyruvate to form N-pyruvic acid 2-iminyl-L-valine | GO_0018388 |
The condensation of pyruvate through the 2-oxo group with the N-terminal valine of proteins to form the derivative N-pyruvic acid 2-iminyl-L-valine.
|
| peptidyl-valine modification | GO_0018213 |
The modification of peptidyl-valine.
|
| N-terminal peptidyl-amino acid deamination to pyruvic acid | GO_0018387 |
The oxidative deamination of N-terminal peptidyl-cysteine, or peptidyl-serine, to form pyruvic acid with an amide bond between its 1-carboxyl group and the N-terminal residue.
|
| N-terminal peptidyl-cysteine condensation with pyruvate to form N-pyruvic acid 2-iminyl-L-cysteine | GO_0018386 |
The condensation of pyruvate through the 2-oxo group with the N-terminal cysteine of proteins to form the derivative N-pyruvic acid 2-iminyl-L-cysteine.
|
| GO_0018385 | GO_0018385 | |
| GO_0018384 | GO_0018384 | |
| GO_0018383 | GO_0018383 | |
| peptidyl-lysine acetylation | GO_0018394 |
The acetylation of peptidyl-lysine.
|