Từ điển y khoa
Thuật ngữ y khoa chuẩn hóa theo MeSH, ICD-11, SNOMED CT.
62,341 terms indexed
RefSeq NM_168985
GenBank Nucleotide AABR07049223
RefSeq NM_141560
A suborder of CRUSTACEA, order Diplostraca, comprising the water fleas. They are benthic filter feeders that consume PHYTOPLANKTON. The body is laterally compressed and enclosed in a bivalved carapace, from which the head extends.
A mitosporic Loculoascomycetes fungal genus including some economically important plant parasites. Teleomorphs include Mycosphaerella and Venturia.
An antineoplastic agent used in the treatment of lymphoproliferative diseases including hairy-cell leukemia.
A semisynthetic macrolide antibiotic derived from ERYTHROMYCIN that is active against a variety of microorganisms. It can inhibit PROTEIN SYNTHESIS in BACTERIA by reversibly binding to the 50S ribosomal subunits. This inhibits the translocation of aminoacyl transfer-RNA and prevents peptide chain elongation.
A plant genus, of the family ONAGRACEAE, which is the subject of genetic studies. The floral aroma is attributed to benzenoid esters and benzyl acetate.
A phosphatidylinositol 3-kinase subclass that includes enzymes with a specificity for 1-phosphatidylinositol, 1-phosphatidylinositol 4-phosphate, and 1-phosphatidylinositol 4,5-bisphosphate. Members of this enzyme subclass are activated by cell surface receptors and occur as heterodimers of enzymatic and regulatory subunits.
A subclass of phosphatidylinositol 3-kinases that have specificity for 1-phosphatidylinositol and 1-phosphatidylinositol 4-phosphate. Members of this subclass consist of a single subunit structure and are regulated by RECEPTOR TYROSINE KINASES; CYTOKINE RECEPTORS; and INTEGRINS.
A phosphatidylinositol 3-kinase subclass that includes enzymes whose specificity is limited to 1-phosphatidylinositol. Members of this class play a role in vesicular transport and in the regulation of TOR KINASES.
A phosphatidylinositol 3-kinase subclass that includes enzymes formed through the heterodimerization of a p110 catalytic and a p85, p55, or p50 regulatory subunit. This subclass of enzymes is a downstream target of TYROSINE KINASE RECEPTORS and G PROTEIN-COUPLED RECEPTORS.
A phosphatidylinositol 3-kinase subclass that includes enzymes formed through the association of a p110gamma catalytic subunit and one of the three regulatory subunits of 84, 87, and 101 kDa in size. This subclass of enzymes is a downstream target of G PROTEIN-COUPLED RECEPTORS.
Disorders comprising a spectrum of brain malformations representing the paradigm of a diffuse neuronal migration disorder. They result in cognitive impairment; SEIZURES; and HYPOTONIA or spasticity. Mutations of two genes, LIS1, the gene for the non-catalytic subunit of PLATELET-ACTIVATING FACTOR ACETYLHYDROLASE IB; and DCX or XLIS, the gene for doublecortin, have been identified as the most common causes of disorders in this spectrum. Additional variants of classical (Type I) lissencephaly have been linked to RELN, the gene for reelin, and ARX, the gene for aristaless related homeobox protein. (From Leventer, R.J., et al, Mol Med Today. 2000 Jul;6(7):277-84 and Barkovich, A.J., et al, Neurology. 2005 Dec 27;65(12):1873-87.)
An acute, highly contagious disease affecting swine of all ages and caused by the CLASSICAL SWINE FEVER VIRUS. It has a sudden onset with high morbidity and mortality.
A species of the PESTIVIRUS genus causing exceedingly contagious and fatal hemorrhagic disease of swine.
The systematic arrangement of entities in any field into categories classes based on common characteristics such as properties, morphology, subject matter, etc.
The main structural coat protein of COATED VESICLES which play a key role in the intracellular transport between membranous organelles. Each molecule of clathrin consists of three light chains (CLATHRIN LIGHT CHAINS) and three heavy chains (CLATHRIN HEAVY CHAINS) that form a structure called a triskelion. Clathrin also interacts with cytoskeletal proteins.
The heavy chain subunits of clathrin.
The light chain subunits of clathrin.
Vesicles formed when cell-membrane coated pits (COATED PITS, CELL-MEMBRANE) invaginate and pinch off. The outer surface of these vesicles is covered with a lattice-like network of the protein CLATHRIN. Shortly after formation, however, the clathrin coat is removed and the vesicles are referred to as ENDOSOMES.
An integral membrane protein that is localized to TIGHT JUNCTIONS, where it plays a role in controlling the paracellular permeability of polarized cells. Mutations in the gene for claudin-1 are associated with Neonatal Ichthyosis-Sclerosing Cholangitis (NISCH) Syndrome.
A claudin subtype that is associated with the formation of cation-selective channels and increased epithelial permeability. It is localized to the TIGHT JUNCTIONS of the PROXIMAL KIDNEY TUBULE and INTESTINAL EPITHELIUM.
A ubiquitously-expressed claudin subtype that acts as a general barrier-forming protein in TIGHT JUNCTIONS. Elevated expression of claudin-3 is found in a variety of tumor cell types, suggesting its role as a therapeutic target for specific ANTINEOPLASTIC AGENTS.
A claudin subtype that takes part in maintaining the barrier-forming property of TIGHT JUNCTIONS. Claudin-4 is found associated with CLAUDIN-8 in the KIDNEY COLLECTING DUCT where it may play a role in paracellular chloride ion reabsorption.
A claudin subtype that is found localized to TIGHT JUNCTIONS in VASCULAR ENDOTHELIAL CELLS. The protein was initially identified as one of several proteins which are deleted in VELOCARDIOFACIAL SYNDROME and may play an important role in maintaining the integrity of the BLOOD-BRAIN BARRIER.
A large family of transmembrane proteins found in TIGHT JUNCTIONS. They take part in the formation of paracellular barriers and pores that regulate paracellular permeability.
A plant genus of the family RUTACEAE. Members contain anethole and CARBAZOLES.
A genus of ascomycetous fungi, family Clavicipitaceae, order Hypocreales, parasitic on various grasses (POACEAE). The sclerotia contain several toxic alkaloids. Claviceps purpurea on rye causes ERGOTISM.
A bone on the ventral side of the shoulder girdle, which in humans is commonly called the collar bone.
A beta-lactam antibiotic produced by the actinobacterium Streptomyces clavuligerus. It is a suicide inhibitor of bacterial beta-lactamase enzymes. Administered alone, it has only weak antibacterial activity against most organisms, but given in combination with other beta-lactam antibiotics it prevents antibiotic inactivation by microbial lactamase.
Acids, salts, and derivatives of clavulanic acid (C8H9O5N). They consist of those beta-lactam compounds that differ from penicillin in having the sulfur of the thiazolidine ring replaced by an oxygen. They have limited antibacterial action, but block bacterial beta-lactamase irreversibly, so that similar antibiotics are not broken down by the bacterial enzymes and therefore can exert their antibacterial effects.
a colibactin maturating enzyme
RefSeq NM_001021650
RefSeq NM_016674
RefSeq NM_031699
RefSeq NM_001014096
RefSeq NM_001306
RefSeq NM_031700
RefSeq NM_009903
An RNA-binding protein that recognizes the AAUAAA RNA SEQUENCE at the 3' end of MRNA. It contains four subunits of 30, 73, 100 and 160 kDa molecular size and combines with CLEAVAGE STIMULATION FACTOR to form a stable complex with mRNA that directs the 3' cleavage and polyadenylation reaction.
The earliest developmental stage of a fertilized ovum (ZYGOTE) during which there are several mitotic divisions within the ZONA PELLUCIDA. Each cleavage or segmentation yields two BLASTOMERES of about half size of the parent cell. This cleavage stage generally covers the period up to 16-cell MORULA.
A RNA-binding protein that stimulates the cleavage of the 3' end of MRNA near the POLYADENYLATION site. It is a heterotrimer of 55-, 64- and 77-kDa subunits and combines with CLEAVAGE STIMULATION FACTOR to form a stable complex with mRNA that directs the 3' cleavage and polyadenylation reaction.
RefSeq NM_001163161
Congenital defect in the upper lip where the maxillary prominence fails to merge with the merged medial nasal prominences. It is thought to be caused by faulty migration of the mesoderm in the head region.