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Toll-like Receptors
Toll-like receptors (TLRs) are a class of proteins that play a key role in the innate immune system. They are single-pass membrane protein, single-spanning receptor (biochemistry), receptors usually expressed on sentinel cells such as macrophages and dendritic cells, that recognize structurally conserved molecules derived from Microorganism, microbes. Once these microbes have reached physical barriers such as the skin or intestinal tract mucosa, they are recognized by TLRs, which activate immune cell responses. The TLRs include TLR1, TLR2, TLR3, TLR4, TLR5, TLR6, TLR7, TLR8, TLR9, TLR10, TLR11, TLR12, and TLR13. Humans lack genes for TLR11, TLR12 and TLR13 and mice lack a functional gene for TLR10. The receptors TLR1, TLR2, TLR4, TLR5, TLR6, and TLR10 are located on the cell membrane, whereas TLR3, TLR7, TLR8, and TLR9 are located in Intracellular receptor, intracellular Vesicle (biology and chemistry), vesicles (because they are sensors of nucleic acids). TLRs received their name ...
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Leucine-rich Repeat
A leucine-rich repeat (LRR) is a protein structural motif that forms an α/β horseshoe tertiary structure, fold. It is composed of repeating 20–30 amino acid stretches that are unusually rich in the hydrophobic amino acid leucine. These Protein tandem repeats, tandem repeats commonly fold together to form a solenoid protein domain, termed leucine-rich repeat domain. Typically, each repeat unit has beta sheet, beta strand-turn (biochemistry), turn-alpha helix structure, and the assembled structural domain, domain, composed of many such repeats, has a horseshoe shape with an interior parallel beta sheet and an exterior array of helices. One face of the beta sheet and one side of the helix array are exposed to solvent and are therefore dominated by hydrophilic residues. The region between the helices and sheets is the protein's hydrophobic core and is tightly sterically packed with leucine residues. Leucine-rich repeats are frequently involved in the formation of protein–pro ...
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TLR6
Toll-like receptor 6 is a protein that in humans is encoded by the ''TLR6'' gene. TLR6 is a transmembrane protein, member of toll-like receptor family, which belongs to the pattern recognition receptor (PRR) family. TLR6 acts in a heterodimer form with toll-like receptor 2 (TLR2). Its ligands include multiple diacyl lipopeptides derived from gram-positive bacteria and mycoplasma and several fungal cell wall saccharides. After dimerizing with TLR2, the NF-κB intracellular signalling pathway is activated, leading to a pro-inflammatory cytokine production and activation of innate immune response. TLR6 has also been designated as CD286 (cluster of differentiation 286). Function The protein encoded by this gene is a member of the toll-like receptor (TLR) family which plays a fundamental role in pathogen recognition and activation of innate immunity. TLRs are highly conserved from Drosophila to humans and share structural and functional similarities. They recognize pathogen-associ ...
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Molecule
A molecule is a group of two or more atoms that are held together by Force, attractive forces known as chemical bonds; depending on context, the term may or may not include ions that satisfy this criterion. In quantum physics, organic chemistry, and biochemistry, the distinction from ions is dropped and ''molecule'' is often used when referring to polyatomic ions. A molecule may be homonuclear, that is, it consists of atoms of one chemical element, e.g. two atoms in the oxygen molecule (O2); or it may be heteronuclear, a chemical compound composed of more than one element, e.g. water (molecule), water (two hydrogen atoms and one oxygen atom; H2O). In the kinetic theory of gases, the term ''molecule'' is often used for any gaseous particle regardless of its composition. This relaxes the requirement that a molecule contains two or more atoms, since the noble gases are individual atoms. Atoms and complexes connected by non-covalent interactions, such as hydrogen bonds or ionic ...
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Future Microbiology
''Future Microbiology'' is a peer-reviewed medical journal that was established in 2006 and is published by Future Medicine. The editors-in-chief are Richard A. Calderone (Georgetown University) and B. Brett Finlay (University of British Columbia). The journal covers all aspects of the microbiological sciences, including virology, bacteriology, parasitology, and mycology. Abstracting and indexing The journal is abstracted and indexed in BIOSIS Previews, Biotechnology Citation Index, CAB Abstracts, Chemical Abstracts, Elsevier Biobase, EMBASE/Excerpta Medica, Index Medicus/MEDLINE/PubMed, Science Citation Index Expanded, and Scopus. According to the ''Journal Citation Reports'', the journal has a 2022 impact factor The impact factor (IF) or journal impact factor (JIF) of an academic journal is a type of journal ranking. Journals with higher impact factor values are considered more prestigious or important within their field. The Impact Factor of a journa ... of 3.1. Referen ...
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Nucleic Acid
Nucleic acids are large biomolecules that are crucial in all cells and viruses. They are composed of nucleotides, which are the monomer components: a pentose, 5-carbon sugar, a phosphate group and a nitrogenous base. The two main classes of nucleic acids are deoxyribonucleic acid (DNA) and ribonucleic acid (RNA). If the sugar is ribose, the polymer is RNA; if the sugar is deoxyribose, a variant of ribose, the polymer is DNA. Nucleic acids are chemical compounds that are found in nature. They carry information in cells and make up genetic material. These acids are very common in all living things, where they create, encode, and store information in every living cell of every outline of life forms, life-form on Earth. In turn, they send and express that information inside and outside the cell nucleus. From the inner workings of the cell to the young of a living thing, they contain and provide information via the nucleic acid sequence. This gives the RNA and DNA their unmistakable 'la ...
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Vesicle (biology And Chemistry)
In cell biology, a vesicle is a structure within or outside a cell, consisting of liquid or cytoplasm enclosed by a lipid bilayer. Vesicles form naturally during the processes of secretion ( exocytosis), uptake (endocytosis), and the transport of materials within the plasma membrane. Alternatively, they may be prepared artificially, in which case they are called liposomes (not to be confused with lysosomes). If there is only one phospholipid bilayer, the vesicles are called ''unilamellar liposomes''; otherwise they are called ''multilamellar liposomes''. The membrane enclosing the vesicle is also a lamellar phase, similar to that of the plasma membrane, and intracellular vesicles can fuse with the plasma membrane to release their contents outside the cell. Vesicles can also fuse with other organelles within the cell. A vesicle released from the cell is known as an extracellular vesicle. Vesicles perform a variety of functions. Because it is separated from the cytosol, the ...
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Intracellular Receptor
Intracellular receptors are globular protein receptors located inside the cell rather than on its cell membrane. The word ''intracellular'' means "within or inside a cell." Molecules that cross a cell membrane to bind with a receptor are generally nonpolar and may be relatively small. These molecules are also known as ligands, these trigger how genes are turned on or off which are essential for processes like growth metabolism etc. Hormones that use intracellular receptors include thyroid, aldosterone, and steroid hormones. Mechanism of Intracellular Receptors The process starts when a signaling molecule like hormones and binds to a specific receptor. # Binding: the molecule(hormone) bind to the intracellular receptor which changes its shape (induced-fit mechanism) and activates it. # Activation: the intracellular receptor moves to the nucleus if it wasn’t already in the nucleus. # DNA binding: the activated intracellular receptor binds to a specific part of the DNA calle ...
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Cell Membrane
The cell membrane (also known as the plasma membrane or cytoplasmic membrane, and historically referred to as the plasmalemma) is a biological membrane that separates and protects the interior of a cell from the outside environment (the extracellular space). The cell membrane consists of a lipid bilayer, made up of two layers of phospholipids with cholesterols (a lipid component) interspersed between them, maintaining appropriate membrane fluidity at various temperatures. The membrane also contains membrane proteins, including integral proteins that span the membrane and serve as membrane transporters, and peripheral proteins that loosely attach to the outer (peripheral) side of the cell membrane, acting as enzymes to facilitate interaction with the cell's environment. Glycolipids embedded in the outer lipid layer serve a similar purpose. The cell membrane controls the movement of substances in and out of a cell, being selectively permeable to ions and organic mole ...
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TLR12
Toll-like receptor 1 (TLR1) is a member of the toll-like receptor (TLR) family of pattern recognition receptors (PRRs) that form the cornerstone of the innate immune system. TLR1 recognizes bacterial lipoproteins and glycolipids in complex with TLR2. TLR1 is a cell surface receptor. In humans, TLR1 is encoded by the ''TLR1'' gene, which is located on chromosome 4. Function The binding of ligands to TLR1 activates intracellular signaling cascades leading to an inflammatory response and initiation of immune processes. TLR1 cooperates with TLR2 in the recognition of bacterial triacyl lipoproteins. TLR1 has been shown to recognize the outer surface lipoprotein of ''Borrelia burgdorferi''. The important role of TLR1 in recognizing triacyl lipopeptides has been shown in TLR1-deficient mice. Toll-like receptors, including TLR-1, found on the epithelial cell layer that lines the small and large intestine are important players in the management of the gut microbiota and detection of ...
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TLR11
Toll-like receptor 11 (TLR11) is a protein that in mice and rats is encoded by the gene ''TLR11'', whereas in humans it is represented by a pseudogene. TLR11 belongs to the toll-like receptor (TLR) family and the interleukin-1 receptor/toll-like receptor superfamily and is found in the endosomes. In mice, TLR11 has been shown to recognise (bacterial) flagellin and (eukaryotic) profilin present on certain microbes on, it helps propagate a host immune response. TLR11 plays a fundamental role in both the innate and adaptive immune responses, through the activation of tumor necrosis factor-alpha, the interleukin 12 (IL-12) response, and interferon-gamma (IFN-gamma) secretion. TLR11 mounts an immune response to multiple microbes, including ''Toxoplasma gondii'' (''T. gondii''), ''Salmonella'' species, and uropathogenic ''E. coli'', and likely many other species due to the highly conserved nature of flagellin and profilin. Structure and localization Proteins in the TLR family are pa ...
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TLR10
Toll-like receptor 10 is a protein that in humans is encoded by the ''TLR10'' gene. TLR10 has also been designated as CD290 (cluster of differentiation 290). TLR10 has not been extensively studied because it is a pseudogene in mice, though all other mammalian species contain an intact copy of the TLR10 gene. Unlike other TLRs, TLR10 does not activate the immune system and has instead been shown to suppress inflammatory signaling on primary human cells. This makes TLR10 unique among the TLR family. TLR10 was thought to be an "orphan" receptor, however, recent studies have identified ligands for TLR10 and these include HIV- gp41. Ligands for TLR2 are potential ligands for TLR10. Function The protein encoded by this gene is a member of the toll-like receptor (TLR) family which play a fundamental role in pathogen recognition and activation of innate immunity. TLRs are highly conserved from ''Drosophila'' to humans and share structural and functional similarities. They recognize p ...
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