All terms in GO
| Label | Id | Description |
|---|---|---|
| clathrin-coated endocytic vesicle lumen | GO_0106176 |
The volume enclosed by the membrane of a clathrin-coated endocytic vesicle.
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| reservosome lumen | GO_0106124 |
The volume enclosed by the membranes of a reservosome.
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| reservosome | GO_0106123 |
A large membrane-bound endocytic organelle present only in members of the Schizotrypanum subgenus of the Trypanosoma genus and is defined as the site of storage of endocytosed macromolecules and lysosomal enzymes. It is found at the posterior end of epimastigote forms of Trypanosoma cruzi, but absent in amastigotes and trypomastigotes.
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| reservosome membrane | GO_0106126 |
The lipid bilayer surrounding a reservosome.
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| reservosome matrix | GO_0106125 |
A matrix composed of planar membranes, vesicles and lipid inclusions within the reservosome.
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| negative regulation of cobalamin metabolic process | GO_0106122 |
Any process that stops, prevents or reduces the frequency, rate or extent of a cobalamin metabolic process.
|
| regulation of cobalamin metabolic process | GO_0106064 |
Any process that modulates the frequency, rate or extent of the chemical reactions and pathways involving cobalamin (vitamin B12), a water-soluble vitamin characterized by possession of a corrin nucleus containing a cobalt atom.
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| positive regulation of cobalamin metabolic process | GO_0106121 |
Any process that activates or increases the frequency, rate or extent of a cobalamin metabolic process.
|
| negative regulation of store-operated calcium entry | GO_0106128 |
Any process that stops, prevents or reduces the frequency, rate or extent of store-operated calcium entry.
|
| regulation of store-operated calcium entry | GO_2001256 |
Any process that modulates the frequency, rate or extent of store-operated calcium entry.
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| positive regulation of store-operated calcium entry | GO_0106129 |
Any process that activates or increases the frequency, rate or extent of store-operated calcium entry.
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| positive regulation of mitotic cohesin ssDNA (lagging strand) loading | GO_0106113 |
Any process that activates or increases the frequency, rate or extent of mitotic cohesin ssDNA (lagging strand) loading.
|
| regulation of mitotic cohesin ssDNA (lagging strand) loading | GO_0106111 |
Any process that modulates the frequency, rate or extent of mitotic cohesin ssDNA (lagging strand) loading.
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| negative regulation of mitotic cohesin ssDNA (lagging strand) loading | GO_0106112 |
Any process that stops, prevents or reduces the frequency, rate or extent of mitotic cohesin ssDNA (lagging strand) loading.
|
| negative regulation of mitotic cohesin dsDNA (leading strand) loading | GO_0106115 |
Any process that stops, prevents or reduces the frequency, rate or extent of mitotic cohesin dsDNA (leading strand) loading.
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| regulation of mitotic cohesin dsDNA (leading strand) loading | GO_0106114 |
Any process that modulates the frequency, rate or extent of mitotic cohesin dsDNA (leading strand) loading.
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| vomitoxin biosynthetic process | GO_0106110 |
The chemical reactions and pathways resulting in the formation of type B trichothecene vomitoxin, also known as deoxynivalenol, a poisonous substance produced by some species of fungi and predominantly occurs in grains such as wheat, barley and oats.
|
| acidocalcisome organization | GO_0106117 |
A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of an acidocalcisome. An acidocalcisome is an electron-dense acidic membrane-bounded organelle which contains a matrix of pyrophosphate and polyphosphates with bound calcium and other cations.
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| positive regulation of mitotic cohesin dsDNA (leading strand) loading | GO_0106116 |
Any process that activates or increases the frequency, rate or extent of mitotic cohesin dsDNA (leading strand) loading.
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| CNBH domain intrinsic ligand binding | GO_0106151 |
Interacting selectivity and noncovalently with a cyclic nucleotide mimicking protein motif that is part of the same protein. The CNBHD is a domain on KCNH channels that creates a binding pocket on the KCNH channel that resembles the cyclic nucleotide- binding domain on other ion channels. It binds to a peptide motif that is part of the same protein rather than a cyclic nucleotide.
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