Any process involved in the maintenance of an internal steady state of phosphate ions at the level of a cell.

Any process involved in the maintenance of an internal steady state of trivalent inorganic anions at the level of a cell.

Any process involved in the maintenance of an internal steady state of chloride ions at the level of a cell.

The anaerobic chemical reactions and pathways resulting in the breakdown of glucose, with the production of acetic acid, butyric acid, carbon dioxide (CO2), and dihydrogen; effected by some saccharolytic species of Clostridium, e.g. C. butyricum.

The chemical reactions and pathways resulting in the breakdown of hexose to butyrate.

A collagen homotrimer of alpha1(VII) chains; type VII collagen triple helices form antiparallel dimer, which in turn associate laterally to form anchoring fibrils that connect type IV collagen in the basal lamina to plaques in the underlying connective tissue. It binds laminin.

A collagen heterotrimer containing type VIII alpha chains; [alpha1(VIII)2]alpha2(VIII) and alpha1(VIII)[alpha2(VIII)]2 trimers have been observed; type VIII collagen triple helices associate to form regular hexagonal nets.

Any collagen trimer that does not form fibrils and that is relatively short compared to the collagen trimers that do form fibrils.

A collagen heterotrimer containing type XI alpha chains in alpha1(XI)alpha2(XI)alpha3(XI) trimers; type XI collagen triple helices associate to form fibrils.

A collagen heterotrimer containing type IX alpha chains in alpha1(IX)alpha2(IX)alpha3(IX) trimers; type IX collagen triple helices associate to form a structure that links glycosaminoglycans to type II collagen fibrils.

Binds to and stops, prevents or reduces the activity of an acetylcholine receptor.

Interacting (directly or indirectly) with acetylcholine receptors such that the proportion of receptors in the active form is changed.

A collagen homotrimer of alpha1(XII) chains; type XII collagen triple helices may link sheet-forming or fibrillar collagens to other structures.

A collagen homotrimer of alpha1(XIV) chains; type XIV collagen triple helices may link sheet-forming or fibrillar collagens to other structures.

Binding to cAMP, the nucleotide cyclic AMP (adenosine 3',5'-cyclophosphate).

A collagen trimer containing alpha(XVI) chains; type XVI trimers can associate with microfibrils.

Binding to cGMP, the nucleotide cyclic GMP (guanosine 3',5'-cyclophosphate).

A collagen homotrimer of alpha1(X) chains; type X collagen triple helices form hexagonal networks (sheets).

Specifies the site of a posttranscriptional modification in an RNA molecule by base pairing with a short sequence around the target residue.