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Innexin
Innexins are transmembrane proteins that form gap junctions in invertebrates. Gap junctions are composed of membrane proteins that form a channel permeable to ions and small molecules connecting the cytoplasm of adjacent cells. Although gap junctions provide similar functions in all multicellular organisms, it was not known what proteins invertebrates used for this purpose until the late 1990s. While the connexin family of gap junction proteins was well-characterized in vertebrates, no homologues were found in non-chordates. Innexins or related proteins are widespread among Eumetazoa, with the exception of echinoderms. Discovery Gap junction proteins with no sequence homology to connexins were initially identified in fruit flies. It was suggested that these proteins are specific invertebrate gap junctions, and they were thus named "innexins" (invertebrate analog of connexins). They were later identified in diverse invertebrates. Invertebrate genomes may contain more than a d ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Vinnexin
Vinnexin is a transmembrane protein whose DNA code is held in a virus genome. When the virus genome is expressed in a cell the vinnexin gene from the virus is made into a functioning protein by the infected cell. The vinnexin protein is then incorporated into the host's cell membranes to alter the way the hosts cells communicate with each other. The altered communication aids the transmission and replication of the virus in complex ways. The communication structure that the vinnexin is involved in is the gap junction and vinnexin forms part of a wider family of proteins that are innexin homologues referred to as pannexins. So far Vinnexins have only been found in Adenovirus and the way they affect the functioning of innexins is being studied in great detail. Discovery Vinnexin was first described in 2005 in an adenovirus as a gene homologue of an insect gap protein called innexin. Vinnexins were shown to be used by the adenovirus to help Incheon wasps successfully inject their eg ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Gap Junction
Gap junctions are membrane channels between adjacent cells that allow the direct exchange of cytoplasmic substances, such small molecules, substrates, and metabolites. Gap junctions were first described as ''close appositions'' alongside tight junctions, however, electron microscopy studies in 1967 led to gap junctions being named as such to be distinguished from tight junctions. They bridge a 2-4 nm gap between cell membranes. Gap junctions use protein complexes known as connexons, composed of connexin proteins to connect one cell to another. Gap junction proteins include the more than 26 types of connexin, as well as at least 12 non-connexin components that make up the gap junction complex or ''nexus,'' including the tight junction protein ZO-1—a protein that holds membrane content together and adds structural clarity to a cell, sodium channels, and aquaporin. More gap junction proteins have become known due to the development of next-generation sequencing. Connexins ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Connexin
Connexins (Cx)TC# 1.A.24, or gap junction proteins, are structurally related transmembrane proteins that assemble to form vertebrate gap junctions. An entirely different family of proteins, the innexins, forms gap junctions in invertebrates. Each gap junction is composed of two hemichannels, or connexons, which consist of homo- or heterohexameric arrays of connexins, and the connexon in one plasma membrane docks end-to-end with a connexon in the membrane of a closely opposed cell. The hemichannel is made of six connexin subunits, each of which consist of four transmembrane segments. Gap junctions are essential for many physiological processes, such as the coordinated depolarization of cardiac muscle, proper embryonic development, and the conducted response in microvasculature. Connexins also have non-channel dependant functions relating to cytoskeleton and cell migration. For these reasons, mutations in connexin-encoding genes can lead to functional and developmental abnormalitie ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Polydnavirus
''Polydnaviriformidae'' ( PDV) is a family of insect viriforms; members are known as polydnaviruses. There are two genera in the family: '' Bracoform'' and '' Ichnoviriform''. Polydnaviruses form a symbiotic relationship with parasitoid wasps. Ichnoviriforms (IV) occur in Ichneumonid wasps and Bracoviriforms (BV) in Braconid wasps. The larvae of wasps in both of those groups are themselves parasitic on Lepidoptera (moths and butterflies), and the polydnaviruses are important in circumventing the immune response of their parasitized hosts. Little or no sequence homology exists between BV and IV, suggesting that the two genera have been evolving independently for a long time. Taxonomy Bracoviriform * Bracoviriform altitudinis * Bracoviriform argentifrontis * Bracoviriform blackburni * Bracoviriform canadense * Bracoviriform congregatae * Bracoviriform crassicornis * Bracoviriform croceipedis * Bracoviriform curvimaculati * Bracoviriform demolitoris * Bracoviriform ectdytolop ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Pannexin
Pannexins (from Greek 'παν' — all, and from Latin 'nexus' — connection) are a family of vertebrate proteins identified by their homology to the invertebrate innexins. While innexins are responsible for forming gap junctions in invertebrates, the pannexins have been shown to predominantly exist as large transmembrane channels connecting the intracellular and extracellular space, allowing the passage of ions and small molecules between these compartments (such as ATP and sulforhodamine B). Three pannexins have been described in Chordates: Panx1, Panx2 and Panx3. Function Pannexins can form nonjunctional transmembrane channels for transport of molecules of less than 1000 Da. These hemichannels can be present in plasma, endoplasmic resticulum (ER) and Golgi membranes. They transport Ca2+, ATP, inositol triphosphate and other small molecules and can form hemichannels with greater ease than connexin subunits. Pannexin 1 and pannexin 2 underlie channel function in neurons ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Transmembrane Proteins
A transmembrane protein is a type of integral membrane protein that spans the entirety of the cell membrane. Many transmembrane proteins function as gateways to permit the transport of specific substances across the membrane. They frequently undergo significant conformational changes to move a substance through the membrane. They are usually highly hydrophobic and aggregate and precipitate in water. They require detergents or nonpolar solvents for extraction, although some of them ( beta-barrels) can be also extracted using denaturing agents. The peptide sequence that spans the membrane, or the transmembrane segment, is largely hydrophobic and can be visualized using the hydropathy plot. Depending on the number of transmembrane segments, transmembrane proteins can be classified as single-pass membrane proteins, or as multipass membrane proteins. Some other integral membrane proteins are called monotopic, meaning that they are also permanently attached to the membrane, bu ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Transmembrane Transporters
A transmembrane protein is a type of integral membrane protein that spans the entirety of the cell membrane. Many transmembrane proteins function as gateways to permit the transport of specific substances across the membrane. They frequently undergo significant conformational changes to move a substance through the membrane. They are usually highly hydrophobic and aggregate and precipitate in water. They require detergents or nonpolar solvents for extraction, although some of them (beta-barrels) can be also extracted using denaturing agents. The peptide sequence that spans the membrane, or the transmembrane segment, is largely hydrophobic and can be visualized using the hydropathy plot. Depending on the number of transmembrane segments, transmembrane proteins can be classified as single-pass membrane proteins, or as multipass membrane proteins. Some other integral membrane proteins are called monotopic, meaning that they are also permanently attached to the membrane, but do ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Transmembrane Proteins
A transmembrane protein is a type of integral membrane protein that spans the entirety of the cell membrane. Many transmembrane proteins function as gateways to permit the transport of specific substances across the membrane. They frequently undergo significant conformational changes to move a substance through the membrane. They are usually highly hydrophobic and aggregate and precipitate in water. They require detergents or nonpolar solvents for extraction, although some of them ( beta-barrels) can be also extracted using denaturing agents. The peptide sequence that spans the membrane, or the transmembrane segment, is largely hydrophobic and can be visualized using the hydropathy plot. Depending on the number of transmembrane segments, transmembrane proteins can be classified as single-pass membrane proteins, or as multipass membrane proteins. Some other integral membrane proteins are called monotopic, meaning that they are also permanently attached to the membrane, bu ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Membrane Proteins
Membrane proteins are common proteins that are part of, or interact with, biological membranes. Membrane proteins fall into several broad categories depending on their location. Integral membrane proteins are a permanent part of a cell membrane and can either penetrate the membrane (Transmembrane protein, transmembrane) or associate with one or the other side of a membrane (Integral monotopic protein, integral monotopic). Peripheral membrane proteins are transiently associated with the cell membrane. Membrane proteins are common, and medically important—about a third of all human proteins are membrane proteins, and these are targets for more than half of all drugs. Nonetheless, compared to other classes of proteins, determining membrane protein structures remains a challenge in large part due to the difficulty in establishing experimental conditions that can preserve the correct (Native state, native) Protein structure, conformation of the protein in isolation from its native ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Protein Families
A protein family is a group of evolutionarily related proteins. In many cases, a protein family has a corresponding gene family, in which each gene encodes a corresponding protein with a 1:1 relationship. The term "protein family" should not be confused with family as it is used in taxonomy. Proteins in a family descend from a common ancestor and typically have similar three-dimensional structures, functions, and significant sequence similarity. Sequence similarity (usually amino-acid sequence) is one of the most common indicators of homology, or common evolutionary ancestry. Some frameworks for evaluating the significance of similarity between sequences use sequence alignment methods. Proteins that do not share a common ancestor are unlikely to show statistically significant sequence similarity, making sequence alignment a powerful tool for identifying the members of protein families. Families are sometimes grouped together into larger clades called superfamilies based on stru ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Hirudo Medicinalis
''Hirudo medicinalis'', or the European medicinal leech, is one of several species of leeches used as medicinal leeches. Other species of ''Hirudo'' sometimes also used as medicinal leeches include ''Hirudo orientalis, H. orientalis'', ''Hirudo troctina, H. troctina'', and ''Hirudo verbana, H. verbana''. The Asian medicinal leech includes ''Hirudinaria manillensis'', and the North American medicinal leech is Macrobdella decora, ''Macrobdella decora''. Medicinal leech populations were reduced significantly in many countries during the 19th century due to the high demand in medical contexts, and remain endangered in many countries today. Morphology The general morphology (biology), morphology of medicinal leeches follows that of most other leeches. Fully mature adults can be up to 20 centimeters in length, and are green, brown, or greenish-brown with a darker tone on the Dorsum (biology), dorsal side and a lighter ventral side. The dorsal side also has a thin red stripe. These or ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Caenorhabditis Elegans
''Caenorhabditis elegans'' () is a free-living transparent nematode about 1 mm in length that lives in temperate soil environments. It is the type species of its genus. The name is a Hybrid word, blend of the Greek ''caeno-'' (recent), ''rhabditis'' (rod-like) and Latin ''elegans'' (elegant). In 1900, Émile Maupas, Maupas initially named it ''Rhabditidae, Rhabditides elegans.'' Günther Osche, Osche placed it in the subgenus ''Caenorhabditis'' in 1952, and in 1955, Ellsworth Dougherty, Dougherty raised ''Caenorhabditis'' to the status of genus. ''C. elegans'' is an unsegmented pseudocoelomate and lacks respiratory or circulatory systems. Most of these nematodes are hermaphrodites and a few are males. Males have specialised tails for mating that include spicule (nematode), spicules. In 1963, Sydney Brenner proposed research into ''C. elegans,'' primarily in the area of neuronal development. In 1974, he began research into the molecular biology, molecular and developmental ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
