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obsolete peptidyl-D-alanine racemization, direct
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GO_0019916 |
[OBSOLETE. The racemization of peptidyl-alanine.] |
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obsolete peptide cross-linking via 3-(S-L-cysteinyl)-L-aspartic acid
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GO_0019928 |
[OBSOLETE. The cross-linking of a cysteine residue to an aspartic acid residue to form 3-(S-L-cysteinyl)-L-aspartic acid.] |
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obsolete peptide cross-linking via 4-(S-L-cysteinyl)-L-glutamic acid
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GO_0019929 |
[OBSOLETE. The cross-linking of a cysteine residue to a glutamic acid residue to form 4-(S-L-cysteinyl)-L-glutamic acid.] |
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obsolete peptidyl-1-thioglycine biosynthetic process, internal
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GO_0019920 |
[OBSOLETE. The chemical reactions and pathways resulting in the formation of internal peptidyl-1-thioglycine, which has an internal C=S bond, instead of an internal C=O bond, in the peptide.] |
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obsolete peptidyl-1-thioglycine biosynthetic process, carboxy-terminal
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GO_0019921 |
[OBSOLETE. The chemical reactions and pathways resulting in the formation of carboxy-terminal peptidyl-1-thioglycine, which has a carboxy-terminal thiocarboxy-C(=O)-SH bond.] |
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obsolete protein-chromophore linkage via peptidyl-cysteine
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GO_0019922 |
[OBSOLETE. The covalent linking of a chromophore to a protein via peptidyl-cysteines.] |
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obsolete alpha-1-microglobulin-chromophore linkage
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GO_0019923 |
[OBSOLETE. The covalent linking of the alpha-1-microglobulin chromophore to the protein; the structure of the chromophore is not known. It is probably heterogeneous and involving two cysteines in thioether bonds.] |
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GO_0019924
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GO_0019924 |
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GO_0019925
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GO_0019925 |
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obsolete peptidyl-tryptophan oxidation to tryptophyl quinone
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GO_0019926 |
[OBSOLETE. The oxidation of peptidyl-tryptophan to form tryptophan-6,7-dione, otherwise known as tryptophyl quinone, which is further modified by cross-linking to either tryptophan or cysteine.] |
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obsolete peptide cross-linking via 4'-(S-L-cysteinyl)-L-tryptophyl quinone
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GO_0019927 |
[OBSOLETE. The cross-linking of a cysteine residue to tryptophyl quinone to form 4'-(S-L-cysteinyl)-L-tryptophyl quinone, a cofactor found at the active site of amine dehydrogenase.] |
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obsolete peptidyl-S-palmitoleyl-L-cysteine biosynthetic process from peptidyl-cysteine
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GO_0019939 |
[OBSOLETE. The modification of peptidyl-cysteine to form peptidyl-S-palmitoleyl-L-cysteine specifically.] |
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obsolete cis-14-hydroxy-10,13-dioxo-7-heptadecenoic acid peptidyl-aspartate ester biosynthetic process from peptidyl-aspartic acid
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GO_0019930 |
[OBSOLETE. The modification of peptidyl-aspartic acid to form peptidyl-cis-14-hydroxy-10,13-dioxo-7-heptadecenoic acid aspartate ester, typical of the barley lipid transfer protein 1.] |
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obsolete protein-chromophore linkage via peptidyl-N6-3-dehydroretinal-L-lysine
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GO_0019931 |
[OBSOLETE. The modification of peptidyl-lysine to form N6-3,4-didehydroretinylidene-L-lysine.] |
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obsolete second-messenger-mediated signaling
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GO_0019932 |
[OBSOLETE. Any intracellular signal transduction in which the signal is passed on within the cell via a second messenger; a small molecule or ion that can be quickly generated or released from intracellular stores, and can diffuse within the cell. Second-messenger signaling includes production or release of the second messenger, and effectors downstream of the second messenger that further transmit the signal within the cell.] |
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cAMP-mediated signaling
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GO_0019933 |
[An intracellular signaling cassette that starts with production of cyclic AMP (cAMP), and ends with activation of downstream effectors that further transmit the signal within the cell.] |
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obsolete cyclic-nucleotide-mediated signaling
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GO_0019935 |
[OBSOLETE. An intracellular signaling cassette that starts with production or release of the cyclic nucleotide, and ends with the activation of downstream effectors that further transmit the signal within the cell.] |
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obsolete inositol phospholipid-mediated signaling
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GO_0019936 |
[OBSOLETE. (Was not defined before being made obsolete).] |
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obsolete protein catenane formation via N6-(L-isoaspartyl)-L-lysine, autocatalytic
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GO_0019937 |
[OBSOLETE. The autocatalytic formation of isopeptide bonds by ligation of peptidyl-lysine and peptidyl-asparagine residues; known to occur in the capsid of some bacteriophage, such as HK97, where it is thought to provide a mechanism for stabilizing the capsid.] |
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obsolete peptide cross-linking via N6-(L-isoaspartyl)-L-lysine, presumed catalytic
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GO_0019938 |
[OBSOLETE. The formation of isopeptide bonds by ligation of peptidyl-lysine and peptidyl-asparagine residues; occurs in mammals in proteins as yet unidentified by a mechanism probably analogous to that of transglutaminase reactions.] |