Surfeit
surfeit (n.) early 14c., "excess quantity;" late 14c., "overindulgence," from Old French sorfet "excess; arrogance" (Modern French surfait), noun use of past participle of surfaire "overdo," from sur- "over" (see sur- (1)) + faire "do," from Latin facere "to make, do" (from PIE root *dhe- "to set, put"). surfeit (v.) late 14c., intransitive, "indulge or feed to excess," from surfeit (n.). Related: Surfeited; surfeiting.
Cell surface receptor deficiencies
Cell surface receptors (membrane receptors, transmembrane receptors) are receptors that are embedded in the plasma membrane of cells. They act in cell signaling by receiving (binding to) extracellular molecules. They are specialized integral membrane proteins that allow communication between the cell and the extracellular space. The extracellular molecules may be hormones, neurotransmitters, cytokines, growth factors, cell adhesion molecules,
Integrin ÎąIIbβ3 – Glycoprotein IIb/IIIa
In medicine, glycoprotein IIb/IIIa (GPIIb/IIIa, also known as integrin ιIIbβ3) is an integrin complex found on platelets. It is a receptor for fibrinogen[1] and von Willebrand factor and aids platelet activation. The complex is formed via calcium-dependent association of gpIIb and gpIIIa, a required step in normal platelet aggregation and endothelial adherence.[2][3] Platelet
Tetraspanin
Tetraspanins are a family of membrane proteins found in all multicellular eukaryotes. Tetraspanins, also referred to as the transmembrane 4 superfamily (TM4SF) proteins, have four transmembrane alpha-helices and two extracellular domains, one short (called the small extracellular domain or loop, SED/SEL or EC1) and one longer, typically 100 amino acid residues (the large extracellular domain/loop,
Orotidine 5′-phosphate decarboxylase
Orotidine 5'-phosphate decarboxylase (OMP decarboxylase) or orotidylate decarboxylase is an enzyme involved in pyrimidine biosynthesis. It catalyzes the decarboxylation of orotidine monophosphate (OMP) to form uridine monophosphate (UMP). The function of this enzyme is essential to the de novo biosynthesis of the pyrimidine nucleotides uridine triphosphate, cytidine triphosphate, and thymidine triphosphate. OMP decarboxylase has been a frequent
Carbonâcarbon lyases
4.1.1: Carboxy-lyasesAcetoacetate decarboxylase Adenosylmethionine decarboxylase Arginine decarboxylase Aromatic L-amino acid decarboxylase Glutamate decarboxylase Histidine decarboxylase Lysine decarboxylase Malonyl-CoA decarboxylase Ornithine decarboxylase Oxaloacetate decarboxylase Phosphoenolpyruvate carboxykinase Phosphoenolpyruvate carboxylase Phosphoribosylaminoimidazole carboxylase Pyrophosphomevalonate decarboxylase Pyruvate decarboxylase RuBisCO Uridine monophosphate synthetase/Orotidine 5'-phosphate decarboxylase Uroporphyrinogen III
Metabolism amino acid metabolism nucleotide  enzymes
Purine metabolismAnabolism R5PâIMP: Ribose-phosphate diphosphokinase Amidophosphoribosyltransferase Phosphoribosylglycinamide formyl transferase AIR synthetase (FGAM cyclase) Phosphoribosylaminoimidazole carboxylase Phosphoribosylaminoimidazolesuccinocarboxamide synthase IMP synthase IMPâAMP: Adenylosuccinate synthase Adenylosuccinate lyase reverse AMP deaminase IMPâGMP: IMP dehydrogenase GMP synthase reverse GMP reductase Nucleotide salvage Hypoxanthine-guanine phosphoribosyltransferase Adenine phosphoribosyltransferase Catabolism
Inborn errors of carbohydrate metabolism
Sucrose, transport(extracellular)Disaccharide catabolism - Congenital alactasia Sucrose intolerance Monosaccharide transport - Glucose-galactose malabsorption Inborn errors of renal tubular transport (Renal glycosuria) Fructose malabsorptionHexose â glucoseMonosaccharide catabolism - Fructose: Essential fructosuria Fructose intolerance Galactose/galactosemia: GALK deficiency GALT deficiency/GALE deficiencyGlucose â glycogenGlycogenesis GSD type 0Â (glycogen synthase
Pompe Disease
Glycogen storage disease type II, also called Pompe disease, is an autosomal recessive metabolic disorder[1] which damages muscle and nerve cells throughout the body. It is caused by an accumulation of glycogen in the lysosome due to deficiency of the lysosomal acid alpha-glucosidase enzyme. It is the only glycogen storage disease with
Amiodarone
Amiodarone is an antiarrhythmic medication used to treat and prevent a number of types of cardiac dysrhythmias.[4] This includes ventricular tachycardia (VT), ventricular fibrillation (VF), and wide complex tachycardia, as well as atrial fibrillation and paroxysmal supraventricular tachycardia.[4] Evidence in cardiac arrest, however, is poor.[5] It can be given by mouth, intravenously, or intraosseously.[4] When used by mouth, it
mdia1
mDia1 (also known as Dia1, Drf1 for Diaphanous-related formin-1, Diaph1, KIAA4062, p140mDia, mKIAA4062, or D18Wsu154e) is a member of the protein family called the formins and is a Rho effector. It is the mouse version of the diaphanous homolog 1 of Drosophila. mDia1 localizes to cells' mitotic spindle and midbody,[1] plays a role
Hippo signaling pathway
The Hippo signaling pathway, also known as the Salvador-Warts-Hippo (SWH) pathway, is a signaling pathway that controls organ size in animals through the regulation of cell proliferation and apoptosis. The pathway takes its name from one of its key signaling componentsâthe protein kinase Hippo (Hpo). Mutations in this gene lead to tissue overgrowth, or a "hippopotamus"-like phenotype. A fundamental
WW domain
The WW domain,[2] (also known as the rsp5-domain[3] or WWP repeating motif[4]) is a modular protein domain that mediates specific interactions with protein ligands. This domain is found in a number of unrelated signaling and structural proteins and may be repeated up to four times in some proteins.[2][3][4][5] Apart
Dystrophin
Dystrophin is a rod-shaped cytoplasmic protein, and a vital part of a protein complex that connects the cytoskeleton of a muscle fiber to the surrounding extracellular matrix through the cell membrane. This complex is variously known as the costamere or the dystrophin-associated protein complex (DAPC). Many muscle proteins, such as Îą-dystrobrevin, syncoilin, synemin, sarcoglycan, dystroglycan, and sarcospan, colocalize with dystrophin at
Spastic Quadriplegia
Spastic quadriplegia, also known as spastic tetraplegia, is a subset of spastic cerebral palsy that affects all four limbs (both arms and legs). Compared to quadriplegia, spastic tetraplegia is defined by spasticity of the limbs as opposed to strict paralysis. It is distinguishable from other forms of cerebral
Filopodia
Filopodia (singular filopodium) are slender cytoplasmic projections that extend beyond the leading edge of lamellipodia in migrating cells.[1] Within the lamellipodium, actin ribs are known as microspikes, and when they extend beyond the lamellipodia, they're known as filopodia.[2] They contain microfilaments (also called actin filaments) cross-linked into bundles by actin-bundling proteins,[3] such as fascin and fimbrin.[4] Filopodia