All individuals in MeSH

Label Id Description
Protein Binding D011485 [The process in which substances, either endogenous or exogenous, bind to proteins, peptides, enzymes, protein precursors, or allied compounds. Specific protein-binding measures are often used as assays in diagnostic assessments. ]
Protein Biosynthesis D014176 [The biosynthesis of PEPTIDES and PROTEINS on RIBOSOMES, directed by MESSENGER RNA, via TRANSFER RNA that is charged with standard proteinogenic AMINO ACIDS. ]
Protein C D011486 [A vitamin-K dependent zymogen present in the blood, which, upon activation by thrombin and thrombomodulin exerts anticoagulant properties by inactivating factors Va and VIIIa at the rate-limiting steps of thrombin formation. ]
Protein C Deficiency D020151 [An absence or deficiency in PROTEIN C which leads to impaired regulation of blood coagulation. It is associated with an increased risk of severe or premature thrombosis. (Stedman's Med. Dict., 26th ed.) ]
Protein C Inhibitor D018046 [A member of the serpin family of proteins that is found in plasma and urine. It is dependent on heparin and is able to inhibit activated PROTEIN C; THROMBIN; KALLIKREIN; and other SERINE ENDOPEPTIDASES. ]
Protein Carbamylation D000077279 [Non-enzymatic addition of carbamoyl (-CONH2) on protein or amino acid functional groups from isocyanic acid or CARBAMOYL-PHOSPHATE. Carbamylation may induce a structural change that results in a functional loss and serves as a biomarker for protein aging and disease pathophysiology. ]
Protein Carbonylation D050050 [The appearance of carbonyl groups (such as aldehyde or ketone groups) in PROTEINS as the result of several oxidative modification reactions. It is a standard marker for OXIDATIVE STRESS. Carbonylated proteins tend to be more hydrophobic and resistant to proteolysis. ]
Protein Conformation D011487 [The characteristic 3-dimensional shape of a protein, including the secondary, supersecondary (motifs), tertiary (domains) and quaternary structure of the peptide chain. PROTEIN STRUCTURE, QUATERNARY describes the conformation assumed by multimeric proteins (aggregates of more than one polypeptide chain). ]
Protein Conformation, alpha-Helical D000072756 [A secondary structure of proteins that is a right-handed helix or coil, where each amino (N-H) group of the peptide backbone contributes a hydrogen bond to the carbonyl(C=O) group of the amino acid four residues N-terminal to it (n-4). It is the most common type of secondary structure. ]
Protein Conformation, beta-Strand D000072757 [A secondary structure of proteins where the amino (N-H) groups of a polypeptide backbone, three to ten amino acids in length, establish hydrogen bonds with the carbonyl (C=O) groups in the backbone of adjacent strands. These may form a beta-sheet, where the side chains of the adjacent strands point in the same direction. , A type of secondary structure that occurs between lateral beta strands connected by at least two or three backbone hydrogen bonds. Multiple beta-sheets may associate to form PROTEIN AGGREGATES. ]
Protein Corona D000066970 [A layer of protein coating adsorbed by NANOPARTICLES upon entry into PLASMA or other protein-containing biological fluids, which affects how nanoparticles are internalized by cells and cleared from the body. ]
Protein D-Aspartate-L-Isoaspartate Methyltransferase D026601 [A PROTEIN O-METHYLTRANSFERASE that recognizes and catalyzes the methyl esterification of ISOASPARTIC ACID and D-ASPARTIC ACID residues in peptides and proteins. It initiates the repair of proteins damaged by the spontaneous decomposition of normal L-aspartic acid and L-asparagine residues. ]
Protein Deficiency D011488 [A nutritional condition produced by a deficiency of proteins in the diet, characterized by adaptive enzyme changes in the liver, increase in amino acid synthetases, and diminution of urea formation, thus conserving nitrogen and reducing its loss in the urine. Growth, immune response, repair, and production of enzymes and hormones are all impaired in severe protein deficiency. Protein deficiency may also arise in the face of adequate protein intake if the protein is of poor quality (i.e., the content of one or more amino acids is inadequate and thus becomes the limiting factor in protein utilization). (From Merck Manual, 16th ed; Harrison's Principles of Internal Medicine, 12th ed, p406) ]
Protein Deglycase DJ-1 D000071617 [A protein deglycase that repairs methylglyoxal- and glyoxal-glycated amino acids and proteins, releasing repaired proteins and lactate or glycolate. It deglycates CYSTEINE, ARGININE and LYSINE residues to reactivate proteins by reversing glycation and prevent the formation of ADVANCED GLYCATION END PRODUCTS. It protects cells against OXIDATIVE STRESS and CELL DEATH by functioning as an oxidative stress sensor and redox-sensitive MOLECULAR CHAPERONE and PROTEASE. Mutations in the PARK7 gene are associated with autosomal-recessive, early-onset PARKINSON DISEASE. ]
Protein Degradation End Products D062106 [Degraded protein components that are found within TISSUES, bodily fluids, and cells under certain pathological conditions. They are largely formed through chemical reactions which occur during non-physiological conditions such as ISCHEMIA; HYPERGLYCEMIA; and PHYSIOLOGICAL STRESS. ]
Protein Denaturation D011489 [Disruption of the non-covalent bonds and/or disulfide bonds responsible for maintaining the three-dimensional shape and activity of the native protein. ]
Protein Disulfide Reductase (Glutathione) D011490 [An enzyme that catalyzes the reduction of a protein-disulfide in the presence of glutathione, forming a protein-dithiol. Insulin is one of its substrates. EC 1.8.4.2. ]
Protein Disulfide-Isomerases D019704 [Sulfur-sulfur bond isomerases that catalyze the rearrangement of disulfide bonds within proteins during folding. Specific protein disulfide-isomerase isoenzymes also occur as subunits of PROCOLLAGEN-PROLINE DIOXYGENASE. ]
Protein Domains D000072417 [Discrete protein structural units that may fold independently of the rest of the protein and have their own functions. ]
Protein Engineering D015202 [Procedures by which protein structure and function are changed or created in vitro by altering existing or synthesizing new structural genes that direct the synthesis of proteins with sought-after properties. Such procedures may include the design of MOLECULAR MODELS of proteins using COMPUTER GRAPHICS or other molecular modeling techniques; site-specific mutagenesis (MUTAGENESIS, SITE-SPECIFIC) of existing genes; and DIRECTED MOLECULAR EVOLUTION techniques to create new genes. ]