Warning: The NCBI web site requires JavaScript to function. more...
An official website of the United States government
The .gov means it's official. Federal government websites often end in .gov or .mil. Before sharing sensitive information, make sure you're on a federal government site.
The site is secure. The https:// ensures that you are connecting to the official website and that any information you provide is encrypted and transmitted securely.
Phosphorylation
The introduction of a phosphoryl group into a compound through the formation of an ester bond between the compound and a phosphorus moiety.
Year introduced: 1991(1979)
Oxidative Phosphorylation Coupling Factors
Year introduced: 1974(1972)
Oxidative Phosphorylation
Electron transfer through the cytochrome system liberating free energy which is transformed into high-energy phosphate bonds.
Year introduced: 1966
Dyrk Kinases
PROTEIN KINASES that can phosphorylate aromatic amino acid residue TYROSINE as well as aliphatic amino acid residues SERINE and THREONINE.
Year introduced: 2024 (1996)
P-type ATPases
A highly conserved family of ATPases that facilitate the transport of lipids and cations across the plasma membrane. Structurally, they are elongated ALPHA-HELICES constituting five functionally distinct domains: three cytoplasmic domains A, N, and P which contain the catalytic sites, and two transmembrane domains. The N domain phosphorylates the P-domain at an invariant ASPARTATE residue, which, in turn, is dephosphorylated by the A domain. The phosphorylation and dephosphorylation cycles drive conformational changes in the protein between two states (E1 and E2), which allow the substrate to access the other side of the membrane.
Year introduced: 2018
Antibodies, Phospho-Specific
Antibodies directed against immunogen-coupled phosphorylated PEPTIDES corresponding to amino acids surrounding the PHOSPHORYLATION site. They are used to study proteins involved in SIGNAL TRANSDUCTION pathways. (From Methods Mol Biol 2000; 99:177-89)
Year introduced: 2004
Mitochondrial Diseases
Diseases caused by abnormal function of the MITOCHONDRIA. They may be caused by mutations, acquired or inherited, in mitochondrial DNA or in nuclear genes that code for mitochondrial components. They may also be the result of acquired mitochondria dysfunction due to adverse effects of drugs, infections, or other environmental causes.
Year introduced: 2002
Photophosphorylation
The use of light to convert ADP to ATP without the concomitant reduction of dioxygen to water as occurs during OXIDATIVE PHOSPHORYLATION in MITOCHONDRIA.
DYRK3 protein, mouse [Supplementary Concept]
RefSeq NM_145508
Date introduced: April 17, 2013
Combined Oxidative Phosphorylation Deficiency 5 [Supplementary Concept]
mutation in MRPS22
Date introduced: November 5, 2012
Combined Oxidative Phosphorylation Deficiency 2 [Supplementary Concept]
Combined Oxidative Phosphorylation Deficiency 3 [Supplementary Concept]
mutation in TSFM
Combined Oxidative Phosphorylation Deficiency 4 [Supplementary Concept]
Combined Oxidative Phosphorylation Deficiency 1 [Supplementary Concept]
Ccdc88a protein, mouse [Supplementary Concept]
RefSeq NM_176841
Date introduced: August 31, 2005
CCDC88A protein, human [Supplementary Concept]
RefSeq NM_017571
Date introduced: July 31, 2005
PHAX protein, human [Supplementary Concept]
RefSeq NM_032177
Date introduced: July 29, 2005
Cabyr protein, mouse [Supplementary Concept]
RefSeq NM_181731
Date introduced: August 6, 2004
CABYR protein, human [Supplementary Concept]
RefSeq NM_153770
Date introduced: March 8, 2002
DYRK3 protein, human [Supplementary Concept]
RefSeq NM_003582
Date introduced: May 22, 2000