All individuals in MeSH

Label Id Description
Protein Phosphatase 1 D054645 [A eukayrotic protein serine-threonine phosphatase subtype that dephosphorylates a wide variety of cellular proteins. The enzyme is comprised of a catalytic subunit and regulatory subunit. Several isoforms of the protein phosphatase catalytic subunit exist due to the presence of multiple genes and the alternative splicing of their mRNAs. A large number of proteins have been shown to act as regulatory subunits for this enzyme. Many of the regulatory subunits have additional cellular functions. ]
Protein Phosphatase 2 D054648 [A phosphoprotein phosphatase subtype that is comprised of a catalytic subunit and two different regulatory subunits. At least two genes encode isoforms of the protein phosphatase catalytic subunit, while several isoforms of regulatory subunits exist due to the presence of multiple genes and the alternative splicing of their mRNAs. Protein phosphatase 2 acts on a broad variety of cellular proteins and may play a role as a regulator of intracellular signaling processes. ]
Protein Phosphatase 2C D000071636 [One of four major classes of mammalian serine/threonine specific protein phosphatases. Protein phosphatase 2C is a monomeric enzyme about 42 kDa in size. It shows broad substrate specificity dependent on divalent cations (mainly manganese and magnesium). Three isozymes are known in mammals: PP2C -alpha, -beta and -gamma. In yeast, there are four PP2C homologues: phosphatase PTC1 that have weak tyrosine phosphatase activity, phosphatase PTC2, phosphatase PTC3, and PTC4. Isozymes of PP2C also occur in Arabidopsis thaliana where the kinase-associated protein phosphatase (KAPP) containing a C-terminal PP2C domain, dephosphorylates Ser/Thr receptor-like kinase RLK5. ]
Protein Precursors D011498
Protein Prenylation D017368 [A post-translational modification of proteins by the attachment of an isoprenoid to the C-terminal cysteine residue. The isoprenoids used, farnesyl diphosphate or geranylgeranyl diphosphate, are derived from the same biochemical pathway that produces cholesterol. ]
Protein Processing, Post-Translational D011499 [Any of various enzymatically catalyzed post-translational modifications of PEPTIDES or PROTEINS in the cell of origin. These modifications include carboxylation; HYDROXYLATION; ACETYLATION; PHOSPHORYLATION; METHYLATION; GLYCOSYLATION; ubiquitination; oxidation; proteolysis; and crosslinking and result in changes in molecular weight and electrophoretic motility. ]
Protein Refolding D058849 [Conformational transitions of a protein from unfolded states (after PROTEIN UNFOLDING) to a more folded state. ]
Protein Renaturation D020673 [The reconstitution of a protein's activity following denaturation. ]
Protein S D017293 [The vitamin K-dependent cofactor of activated PROTEIN C. Together with protein C, it inhibits the action of factors VIIIa and Va. A deficiency in protein S; (PROTEIN S DEFICIENCY); can lead to recurrent venous and arterial thrombosis. ]
Protein S Deficiency D018455 [An autosomal dominant disorder showing decreased levels of plasma protein S antigen or activity, associated with venous thrombosis and pulmonary embolism. PROTEIN S is a vitamin K-dependent plasma protein that inhibits blood clotting by serving as a cofactor for activated PROTEIN C (also a vitamin K-dependent protein), and the clinical manifestations of its deficiency are virtually identical to those of protein C deficiency. Treatment with heparin for acute thrombotic processes is usually followed by maintenance administration of coumarin drugs for the prevention of recurrent thrombosis. (From Harrison's Principles of Internal Medicine, 12th ed, p1511; Wintrobe's Clinical Hematology, 9th ed, p1523) ]
Protein Sorting Signals D021382 [Highly hydrophobic amino acid sequences of proteins that must cross through membranes to arrive at their functioning cellular location (such as secreted and membrane proteins). They are 15 to 60 amino acids long and reside at the amino-terminus (leader signal peptides) or internally. By binding to signal recognition particles, these sequences direct nascent protein-ribosome complexes to a membrane where the protein is inserted during translation. Signal peptides direct translational uptake of the protein by various membranes -endoplamic reticulum, mitochondrial, chloroplast, peroxisomal, etc. Leader signal sequences on non-membrane proteins are ultimately removed by specific peptidases. , Amino acid sequences found in transported proteins that selectively guide the distribution of the proteins to specific cellular compartments. ]
Protein Splicing D019154 [The excision of in-frame internal protein sequences (INTEINS) of a precursor protein, coupled with ligation of the flanking sequences (EXTEINS). Protein splicing is an autocatalytic reaction and results in the production of two proteins from a single primary translation product: the intein and the mature protein. ]
Protein Stability D055550 [The ability of a protein to retain its structural conformation or its activity when subjected to physical or chemical manipulations. ]
Protein Structural Elements D000072416 [Distinguishing three-dimensional structures characteristically formed by homologous protein sequences. ]
Protein Structure, Quaternary D020836 [The characteristic 3-dimensional shape and arrangement of multimeric proteins (aggregates of more than one polypeptide chain). ]
Protein Structure, Secondary D017433 [The level of protein structure in which regular hydrogen-bond interactions within contiguous stretches of polypeptide chain give rise to ALPHA-HELICES; BETA-STRANDS (which align to form BETA-SHEETS), or other types of coils. This is the first folding level of protein conformation. ]
Protein Structure, Tertiary D017434 [The level of protein structure in which combinations of secondary protein structures (ALPHA HELICES; BETA SHEETS; loop regions, and AMINO ACID MOTIFS) pack together to form folded shapes. Disulfide bridges between cysteines in two different parts of the polypeptide chain along with other interactions between the chains play a role in the formation and stabilization of tertiary structure. ]
Protein Subunits D021122 [Single chains of amino acids that are the units of multimeric PROTEINS. Multimeric proteins can be composed of identical or non-identical subunits. One or more monomeric subunits may compose a protomer which itself is a subunit structure of a larger assembly. , Substructures of multimeric PROTEINS. They may be monomeric or heterodimeric substructures. ]
Protein Synthesis Inhibitors D011500 [Compounds which inhibit the synthesis of proteins. They are usually ANTI-BACTERIAL AGENTS or toxins. Mechanism of the action of inhibition includes the interruption of peptide-chain elongation, the blocking the A site of ribosomes, the misreading of the genetic code or the prevention of the attachment of oligosaccharide side chains to glycoproteins. ]
Protein Translocation Systems D000069284 [Multiprotein complexes that carry out protein SECRETION PROCESSES. , Multiprotein complexes that carry out PROTEIN TRANSPORT across CELL MEMBRANES. ]