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Entebbe Bat Virus
''Entebbe bat virus'' is an infectious disease caused by a ''Flavivirus'' that is closely related to yellow fever. Little is known about the symptoms caused by the Entebbe bat virus, and it is unknown if the virus can infect humans. Entebbe bat virus was initially a mosquito-borne pathogen that was able to infect bats and use them as reservoirs for the virus. However, the virus does not seem to have any existing adverse side effects on its host. Entebbe bat virus was first isolated from a little free-tailed bat ('' Chaerephon pumilus'') in Uganda in 1957, but was not detectable after initial isolation. In 2011, Entebbe bat virus was isolated from a free-tailed bat captured from the attic of a house where it had been originally found. Infectious virus was recovered from the spleen and lung. The viral RNA was sequenced and compared with that of the original isolate (Kading et al. 2015). Entebbe bat virus is a (+) single-stranded RNA (ssRNA) genome virus. It is an enveloped v ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Flavivirus
''Flavivirus'' is a genus of positive-strand RNA viruses in the family ''Flaviviridae''. The genus includes the West Nile virus, dengue virus, tick-borne encephalitis virus, yellow fever virus, Zika virus and several other viruses which may cause encephalitis, as well as insect-specific flaviviruses (ISFs) such as cell fusing agent virus (CFAV), Palm Creek virus (PCV), and Parramatta River virus (PaRV). While dual-host flaviviruses can infect vertebrates as well as arthropods, insect-specific flaviviruses are restricted to their competent arthropods. The means by which flaviviruses establish persistent infection in their competent vectors and cause disease in humans depends upon several virus-host interactions, including the intricate interplay between flavivirus-encoded immune antagonists and the host antiviral innate immune effector molecules. Flaviviruses are named for the yellow fever virus; the word ''flavus'' means 'yellow' in Latin, and yellow fever in turn is named from i ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Endocytosis
Endocytosis is a cellular process in which substances are brought into the cell. The material to be internalized is surrounded by an area of cell membrane, which then buds off inside the cell to form a vesicle containing the ingested material. Endocytosis includes pinocytosis (cell drinking) and phagocytosis (cell eating). It is a form of active transport. History The term was proposed by De Duve in 1963. Phagocytosis was discovered by Élie Metchnikoff in 1882. Pathways Endocytosis pathways can be subdivided into four categories: namely, receptor-mediated endocytosis (also known as clathrin-mediated endocytosis), caveolae, pinocytosis, and phagocytosis Phagocytosis () is the process by which a cell uses its plasma membrane to engulf a large particle (≥ 0.5 μm), giving rise to an internal compartment called the phagosome. It is one type of endocytosis. A cell that performs phagocytosis is .... *Clathrin-mediated endocytosis is mediated by the production of smal ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Polymerase
A polymerase is an enzyme ( EC 2.7.7.6/7/19/48/49) that synthesizes long chains of polymers or nucleic acids. DNA polymerase and RNA polymerase are used to assemble DNA and RNA molecules, respectively, by copying a DNA template strand using base-pairing interactions or RNA by half ladder replication. A DNA polymerase from the thermophilic bacterium, ''Thermus aquaticus'' (''Taq'') ( PDBbr>1BGX EC 2.7.7.7) is used in the polymerase chain reaction, an important technique of molecular biology. A polymerase may be template dependent or template independent. Poly-A-polymerase is an example of template independent polymerase. Terminal deoxynucleotidyl transferase also known to have template independent and template dependent activities. Types By function *DNA polymerase (DNA-directed DNA polymerase, DdDP) **Family A: DNA polymerase I; Pol γ, θ, ν **Family B: DNA polymerase II; Pol α, δ, ε, ζ **Family C: DNA polymerase III holoenzyme **Family X: Pol β, λ, μ * ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Autocatalysis
A single chemical reaction is said to be autocatalytic if one of the reaction products is also a catalyst for the same or a coupled reaction.Steinfeld J.I., Francisco J.S. and Hase W.L. ''Chemical Kinetics and Dynamics'' (2nd ed., Prentice-Hall 1999) p.151-2 Such a reaction is called an autocatalytic reaction. A ''set'' of chemical reactions can be said to be "collectively autocatalytic" if a number of those reactions produce, as reaction products, catalysts for enough of the other reactions that the entire set of chemical reactions is self-sustaining given an input of energy and food molecules (see autocatalytic set). Chemical reactions A chemical reaction of two reactants and two products can be written as : \alpha A + \beta B \rightleftharpoons \sigma S + \tau T where the Greek letters are stoichiometric coefficients and the capital Latin letters represent chemical species. The chemical reaction proceeds in both the forward and reverse direction. This equation is easily g ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Polyprotein
Proteolysis is the breakdown of proteins into smaller polypeptides or amino acids. Uncatalysed, the hydrolysis of peptide bonds is extremely slow, taking hundreds of years. Proteolysis is typically catalysed by cellular enzymes called proteases, but may also occur by intra-molecular digestion. Proteolysis in organisms serves many purposes; for example, digestive enzymes break down proteins in food to provide amino acids for the organism, while proteolytic processing of a polypeptide chain after its synthesis may be necessary for the production of an active protein. It is also important in the regulation of some physiological and cellular processes including apoptosis, as well as preventing the accumulation of unwanted or misfolded proteins in cells. Consequently, abnormality in the regulation of proteolysis can cause disease. Proteolysis can also be used as an analytical tool for studying proteins in the laboratory, and it may also be used in industry, for example in food proc ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
MRNAs
In molecular biology, messenger ribonucleic acid (mRNA) is a single-stranded molecule of RNA that corresponds to the genetic sequence of a gene, and is read by a ribosome in the process of synthesizing a protein. mRNA is created during the process of transcription, where an enzyme (RNA polymerase) converts the gene into primary transcript mRNA (also known as pre-mRNA). This pre-mRNA usually still contains introns, regions that will not go on to code for the final amino acid sequence. These are removed in the process of RNA splicing, leaving only exons, regions that will encode the protein. This exon sequence constitutes mature mRNA. Mature mRNA is then read by the ribosome, and, utilising amino acids carried by transfer RNA (tRNA), the ribosome creates the protein. This process is known as translation. All of these processes form part of the central dogma of molecular biology, which describes the flow of genetic information in a biological system. As in DNA, genetic informa ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Polypeptides
Peptides (, ) are short chains of amino acids linked by peptide bonds. Long chains of amino acids are called proteins. Chains of fewer than twenty amino acids are called oligopeptides, and include dipeptides, tripeptides, and tetrapeptides. A polypeptide is a longer, continuous, unbranched peptide chain. Hence, peptides fall under the broad chemical classes of biological polymers and oligomers, alongside nucleic acids, oligosaccharides, polysaccharides, and others. A polypeptide that contains more than approximately 50 amino acids is known as a protein. Proteins consist of one or more polypeptides arranged in a biologically functional way, often bound to ligands such as coenzymes and cofactors, or to another protein or other macromolecule such as DNA or RNA, or to complex macromolecular assemblies. Amino acids that have been incorporated into peptides are termed residues. A water molecule is released during formation of each amide bond.. All peptides except cyclic peptides ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
N-terminus
The N-terminus (also known as the amino-terminus, NH2-terminus, N-terminal end or amine-terminus) is the start of a protein or polypeptide, referring to the free amine group (-NH2) located at the end of a polypeptide. Within a peptide, the amine group is bonded to the carboxylic group of another amino acid, making it a chain. That leaves a free carboxylic group at one end of the peptide, called the C-terminus, and a free amine group on the other end called the N-terminus. By convention, peptide sequences are written N-terminus to C-terminus, left to right (in LTR writing systems). This correlates the translation direction to the text direction, because when a protein is translated from messenger RNA, it is created from the N-terminus to the C-terminus, as amino acids are added to the carboxyl end of the protein. Chemistry Each amino acid has an amine group and a carboxylic group. Amino acids link to one another by peptide bonds which form through a dehydration reaction that ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Hydrolysis
Hydrolysis (; ) is any chemical reaction in which a molecule of water breaks one or more chemical bonds. The term is used broadly for substitution reaction, substitution, elimination reaction, elimination, and solvation reactions in which water is the nucleophile. Biological hydrolysis is the cleavage of biomolecules where a water molecule is consumed to effect the separation of a larger molecule into component parts. When a carbohydrate is broken into its component sugar molecules by hydrolysis (e.g., sucrose being broken down into glucose and fructose), this is recognized as saccharification. Hydrolysis reactions can be the reverse of a condensation reaction in which two molecules join into a larger one and eject a water molecule. Thus hydrolysis adds water to break down, whereas condensation builds up by removing water. Types Usually hydrolysis is a chemical process in which a molecule of water is added to a substance. Sometimes this addition causes both the substance and w ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Helicase
Helicases are a class of enzymes thought to be vital to all organisms. Their main function is to unpack an organism's genetic material. Helicases are motor proteins that move directionally along a nucleic acid phosphodiester backbone, separating two hybridized nucleic acid strands (hence '' helic- + -ase''), using energy from ATP hydrolysis. There are many helicases, representing the great variety of processes in which strand separation must be catalyzed. Approximately 1% of eukaryotic genes code for helicases. The human genome codes for 95 non-redundant helicases: 64 RNA helicases and 31 DNA helicases. Many cellular processes, such as DNA replication, transcription, translation, recombination, DNA repair, and ribosome biogenesis involve the separation of nucleic acid strands that necessitates the use of helicases. Some specialized helicases are also involved in sensing of viral nucleic acids during infection and fulfill a immunological function. Function Helicases are o ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
N-methyltransferase
N-methyltransferase may refer to: *(RS)-1-benzyl-1,2,3,4-tetrahydroisoquinoline N-methyltransferase * 3-hydroxy-16-methoxy-2,3-dihydrotabersonine N-methyltransferase * Amine N-methyltransferase * Anthranilate N-methyltransferase * (cytochrome c)-arginine N-methyltransferase * (myelin basic protein)-arginine N-methyltransferase * Calmodulin-lysine N-methyltransferase *Carnosine N-methyltransferase * (S)-coclaurine-N-methyltransferase * Dimethylhistidine N-methyltransferase *Glycine N-methyltransferase *Guanidinoacetate N-methyltransferase *Histamine N-methyltransferase *Histone methyltransferase * (cytochrome c)-lysine N-methyltransferase *(ribulose-bisphosphate carboxylase)-lysine N-methyltransferase *Methylamine—glutamate N-methyltransferase * Nicotinamide N-methyltransferase *Nicotinate N-methyltransferase *Phenylethanolamine N-methyltransferase *Phosphatidylethanolamine N-methyltransferase *Phosphatidyl-N-methylethanolamine N-methyltransferase *Phosphoethanolamine N-methyltransf ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Guanylyltransferase
Guanylyl transferases are enzymes that transfer a guanosine mono phosphate group, usually from GTP to another molecule, releasing pyrophosphate. Many eukaryotic guanylyl transferases are capping enzymes that catalyze the formation of the 5' cap in the co-transcriptional modification of messenger RNA. Because the 5' end of the RNA molecule ends in a phosphate group, the bond formed between the RNA and the GTP molecule is an unusual 5'-5' triphosphate linkage, instead of the 3'-5' linkages between the other nucleotides that form an RNA strand. In capping enzymes, a highly conserved lysine residue serves as the catalytic residue that forms a covalent enzyme-GMP complex.Fresco LD, Buratowski S. (1994). Active site of the mRNA-capping enzyme guanylyltransferase from Saccharomyces cerevisiae: similarity to the nucleotidyl attachment motif of DNA and RNA ligases. ''Proc Natl Acad Sci USA'' 91(14): 6624–6628. The transfer RNA (tRNA) for histidine is unique among eukaryotic tRNAs in ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
