| D008958 |
Models, Molecular |
Models used experimentally or theoretically to study molecular shape, electronic properties, or interactions; includes analogous molecules, computer-generated graphics, and mechanical structures. |
Molecular Models,Model, Molecular,Molecular Model |
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| D011487 |
Protein Conformation |
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). |
Conformation, Protein,Conformations, Protein,Protein Conformations |
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| D011950 |
Receptors, Cholinergic |
Cell surface proteins that bind acetylcholine with high affinity and trigger intracellular changes influencing the behavior of cells. Cholinergic receptors are divided into two major classes, muscarinic and nicotinic, based originally on their affinity for nicotine and muscarine. Each group is further subdivided based on pharmacology, location, mode of action, and/or molecular biology. |
ACh Receptor,Acetylcholine Receptor,Acetylcholine Receptors,Cholinergic Receptor,Cholinergic Receptors,Cholinoceptive Sites,Cholinoceptor,Cholinoceptors,Receptors, Acetylcholine,ACh Receptors,Receptors, ACh,Receptor, ACh,Receptor, Acetylcholine,Receptor, Cholinergic,Sites, Cholinoceptive |
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| D011956 |
Receptors, Cell Surface |
Cell surface proteins that bind signalling molecules external to the cell with high affinity and convert this extracellular event into one or more intracellular signals that alter the behavior of the target cell (From Alberts, Molecular Biology of the Cell, 2nd ed, pp693-5). Cell surface receptors, unlike enzymes, do not chemically alter their ligands. |
Cell Surface Receptor,Cell Surface Receptors,Hormone Receptors, Cell Surface,Receptors, Endogenous Substances,Cell Surface Hormone Receptors,Endogenous Substances Receptors,Receptor, Cell Surface,Surface Receptor, Cell |
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| D002352 |
Carrier Proteins |
Proteins that bind or transport specific substances in the blood, within the cell, or across cell membranes. |
Binding Proteins,Carrier Protein,Transport Protein,Transport Proteins,Binding Protein,Protein, Carrier,Proteins, Carrier |
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| D004167 |
Diphtheria Toxin |
An ADP-ribosylating polypeptide produced by CORYNEBACTERIUM DIPHTHERIAE that causes the signs and symptoms of DIPHTHERIA. It can be broken into two unequal domains: the smaller, catalytic A domain is the lethal moiety and contains MONO(ADP-RIBOSE) TRANSFERASES which transfers ADP RIBOSE to PEPTIDE ELONGATION FACTOR 2 thereby inhibiting protein synthesis; and the larger B domain that is needed for entry into cells. |
Corynebacterium Diphtheriae Toxin,Toxin, Corynebacterium Diphtheriae |
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| D004705 |
Endocytosis |
Cellular uptake of extracellular materials within membrane-limited vacuoles or microvesicles. ENDOSOMES play a central role in endocytosis. |
Endocytoses |
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| D005098 |
Exotoxins |
Toxins produced, especially by bacterial or fungal cells, and released into the culture medium or environment. |
Exotoxin |
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| D000097668 |
Pseudomonas aeruginosa Exotoxin A |
An NAD-dependent ADP-ribosyltransferase that catalyzes the transfer of the ADP ribosyl moiety of oxidized NAD onto elongation factor 2 (EF-2) thus arresting protein synthesis. Commonly used as the toxin in immunotoxins. |
Exotoxin A, Pseudomonas,Exotoxin A, Pseudomonas aeruginosa,Recombinant Truncated Pseudomonas Exotoxin A, Form PE38QQR,Recombinant Truncated Pseudomonas Exotoxin A, Form PE40,ToxA protein, Pseudomonas aeruginosa,ETA, Pseudomonas,PE38QQR,PE40 toxin |
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| D001427 |
Bacterial Toxins |
Toxic substances formed in or elaborated by bacteria; they are usually proteins with high molecular weight and antigenicity; some are used as antibiotics and some to skin test for the presence of or susceptibility to certain diseases. |
Bacterial Toxin,Toxins, Bacterial,Toxin, Bacterial |
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