|
Phospholipid Scramblase
Scramblase is a protein responsible for the translocation of phospholipids between the two monolayers of a lipid bilayer of a cell membrane. In humans, phospholipid scramblases (PLSCRs) constitute a family of five homologous proteins that are named as hPLSCR1–hPLSCR5. Scramblases are members of the general family of transmembrane lipid transporters known as flippases. Scramblases are distinct from flippases and floppases. Scramblases, flippases, and floppases are three different types of enzymatic groups of phospholipid transportation enzymes. The inner-leaflet, facing the inside of the cell, contains negatively charged amino-phospholipids and phosphatidylethanolamine. The outer-leaflet, facing the outside environment, contains phosphatidylcholine and sphingomyelin. Scramblase is an enzyme, present in the cell membrane, that can transport (''scramble'') the negatively charged phospholipids from the inner-leaflet to the outer-leaflet, and vice versa. Expression Whereas ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
PLSCR1
Phospholipid scramblase 1 (PL scramblase 1) is an enzyme that in humans is encoded by the ''PLSCR1'' gene. Interactions PLSCR1 has been shown to Protein-protein interaction, interact with: * CPSF6, * Epidermal growth factor receptor, * NEU4, * SHC1, * SLPI, and * TFG (gene), TFG. See also *Scramblase References Further reading * * * * * * * * * * * * * * * * * * {{gene-3-stub ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Beta Barrel
In protein structures, a beta barrel (β barrel) is a beta sheet (β sheet) composed of tandem repeats that twists and coils to form a closed toroidal structure in which the first strand is bonded to the last strand (hydrogen bond). Beta-strands in many beta-barrels are arranged in an antiparallel fashion. Beta barrel structures are named for resemblance to the barrels used to contain liquids. Most of them are water-soluble outer membrane proteins and frequently bind hydrophobic ligands in the barrel center, as in lipocalins. Others span cell membranes and are commonly found in porins. Porin-like barrel structures are encoded by as many as 2–3% of the genes in Gram-negative bacteria. It has been shown that more than 600 proteins with various function such as oxidase, dismutase, and amylase contain the beta barrel structure. In many cases, the strands contain alternating polar and non-polar (hydrophilic and hydrophobic) amino acids, so that the hydrophobic residues are orient ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Cell Nucleus
The cell nucleus (; : nuclei) is a membrane-bound organelle found in eukaryote, eukaryotic cell (biology), cells. Eukaryotic cells usually have a single nucleus, but a few cell types, such as mammalian red blood cells, have #Anucleated_cells, no nuclei, and a few others including osteoclasts have Multinucleate, many. The main structures making up the nucleus are the nuclear envelope, a double membrane that encloses the entire organelle and isolates its contents from the cellular cytoplasm; and the nuclear matrix, a network within the nucleus that adds mechanical support. The cell nucleus contains nearly all of the cell's genome. Nuclear DNA is often organized into multiple chromosomes – long strands of DNA dotted with various proteins, such as histones, that protect and organize the DNA. The genes within these chromosomes are Nuclear organization, structured in such a way to promote cell function. The nucleus maintains the integrity of genes and controls the activities of the ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
1Y2A
1Y or 1-Y may refer to: *UH-1Y; see H-1 upgrade program **Bell UH-1Y Venom *SSH 1Y (WA); see Washington State Route 532 *1Y-J, a model of Toyota Y engine *1Y, IATA code for Sun Air (Sudan) *1Y, IATA code for Electronic Data Systems * 1-Y classification in the U.S. Selective Service System, no longer in use See also *Year A year is a unit of time based on how long it takes the Earth to orbit the Sun. In scientific use, the tropical year (approximately 365 Synodic day, solar days, 5 hours, 48 minutes, 45 seconds) and the sidereal year (about 20 minutes longer) ... * Y1 (other) {{Letter-NumberCombDisambig ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Erythrocyte
Red blood cells (RBCs), referred to as erythrocytes (, with -''cyte'' translated as 'cell' in modern usage) in academia and medical publishing, also known as red cells, erythroid cells, and rarely haematids, are the most common type of blood cell and the vertebrate's principal means of delivering oxygen () to the body tissues—via blood flow through the circulatory system. Erythrocytes take up oxygen in the lungs, or in fish the gills, and release it into tissues while squeezing through the body's capillaries. The cytoplasm of a red blood cell is rich in hemoglobin (Hb), an iron-containing biomolecule that can bind oxygen and is responsible for the red color of the cells and the blood. Each human red blood cell contains approximately 270 million hemoglobin molecules. The cell membrane is composed of proteins and lipids, and this structure provides properties essential for physiological cell function such as deformability and stability of the blood cell while traversing ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Sickle Cell Disease
Sickle cell disease (SCD), also simply called sickle cell, is a group of inherited Hemoglobinopathy, haemoglobin-related blood disorders. The most common type is known as sickle cell anemia. Sickle cell anemia results in an abnormality in the oxygen-carrying protein haemoglobin found in red blood cells. This leads to the red blood cells adopting an abnormal sickle-like shape under certain circumstances; with this shape, they are unable to deform as they pass through Capillary, capillaries, causing blockages. Problems in sickle cell disease typically begin around 5 to 6 months of age. A number of health problems may develop, such as attacks of pain (known as a sickle cell crisis) in joints, anemia, swelling in the hands and feet, bacterial infections, dizziness and stroke. The probability of severe symptoms, including long-term pain, increases with age. Without treatment, people with SCD rarely reach adulthood but with good healthcare, median life expectancy is between 58 and 66 ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Nitrosylation
Nitrosation and nitrosylation are two names for the process of converting organic compounds or metal complexes into nitroso derivatives, i.e., compounds containing the functionality. The synonymy arises because the R-NO functionality can be interpreted two different ways, depending on the physico-chemical environment: * Nitrosylation interprets the process as adding a nitrosyl radical NO•. Nitrosylation commonly occurs in the context of a metal (e.g. iron) or a thiol, leading to nitrosyl iron (e.g., in nitrosylated heme = nitrosylheme) or ''S''-nitrosothiols (RSNOs). * Nitrosation interprets the process as adding a nitrosonium ion . Nitrosation commonly occurs with amines (–), leading to a nitrosamine. There are multiple chemical mechanisms by which this can be achieved, including enzymes and chemical synthesis. In biochemistry The biological functions of nitric oxide include S-nitrosylation, the conjugation of NO to cysteine thiols in proteins, which is an imp ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Redox
Redox ( , , reduction–oxidation or oxidation–reduction) is a type of chemical reaction in which the oxidation states of the reactants change. Oxidation is the loss of electrons or an increase in the oxidation state, while reduction is the gain of electrons or a decrease in the oxidation state. The oxidation and reduction processes occur simultaneously in the chemical reaction. There are two classes of redox reactions: * Electron transfer, Electron-transfer – Only one (usually) electron flows from the atom, ion, or molecule being oxidized to the atom, ion, or molecule that is reduced. This type of redox reaction is often discussed in terms of redox couples and electrode potentials. * Atom transfer – An atom transfers from one Substrate (chemistry), substrate to another. For example, in the rusting of iron, the oxidation state of iron atoms increases as the iron converts to an oxide, and simultaneously, the oxidation state of oxygen decreases as it accepts electrons r ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Proline
Proline (symbol Pro or P) is an organic acid classed as a proteinogenic amino acid (used in the biosynthesis of proteins), although it does not contain the amino group but is rather a secondary amine. The secondary amine nitrogen is in the protonated form (NH2+) under biological conditions, while the carboxyl group is in the deprotonated −COO− form. The "side chain" from the α carbon connects to the nitrogen forming a pyrrolidine loop, classifying it as a aliphatic amino acid. It is non-essential in humans, meaning the body can synthesize it from the non-essential amino acid L-glutamate. It is encoded by all the codons starting with CC (CCU, CCC, CCA, and CCG). Proline is the only proteinogenic amino acid which is a secondary amine, as the nitrogen atom is attached both to the α-carbon and to a chain of three carbons that together form a five-membered ring. History and etymology Proline was first isolated in 1900 by Richard Willstätter who obtained the amino a ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Adenosine Triphosphate
Adenosine triphosphate (ATP) is a nucleoside triphosphate that provides energy to drive and support many processes in living cell (biology), cells, such as muscle contraction, nerve impulse propagation, and chemical synthesis. Found in all known forms of life, it is often referred to as the "molecular unit of currency" for intracellular energy transfer. When consumed in a Metabolism, metabolic process, ATP converts either to adenosine diphosphate (ADP) or to adenosine monophosphate (AMP). Other processes regenerate ATP. It is also a Precursor (chemistry), precursor to DNA and RNA, and is used as a coenzyme. An average adult human processes around 50 kilograms (about 100 mole (unit), moles) daily. From the perspective of biochemistry, ATP is classified as a nucleoside triphosphate, which indicates that it consists of three components: a nitrogenous base (adenine), the sugar ribose, and the Polyphosphate, triphosphate. Structure ATP consists of three parts: a sugar, an amine base ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Protein Domain
In molecular biology, a protein domain is a region of a protein's Peptide, polypeptide chain that is self-stabilizing and that Protein folding, folds independently from the rest. Each domain forms a compact folded Protein tertiary structure, three-dimensional structure. Many proteins consist of several domains, and a domain may appear in a variety of different proteins. Molecular evolution uses domains as building blocks and these may be recombined in different arrangements to create proteins with different functions. In general, domains vary in length from between about 50 amino acids up to 250 amino acids in length. The shortest domains, such as zinc fingers, are stabilized by metal ions or Disulfide bond, disulfide bridges. Domains often form functional units, such as the calcium-binding EF-hand, EF hand domain of calmodulin. Because they are independently stable, domains can be "swapped" by genetic engineering between one protein and another to make chimera (protein), chimeric ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
EF Hand
The EF hand is a helix–loop–helix structural domain or ''motif'' found in a large family of calcium-binding proteins. The EF-hand motif contains a helix–loop–helix topology, much like the spread thumb and forefinger of the human hand, in which the Ca2+ ions are coordinated by ligands within the loop. The motif takes its name from traditional nomenclature used in describing the protein parvalbumin, which contains three such motifs and is probably involved in muscle relaxation via its calcium-binding activity. The EF-hand consists of two alpha helices linked by a short loop region (usually about 12 amino acids) that usually binds calcium ions. EF-hands also appear in each structural domain of the signaling protein calmodulin and in the muscle protein troponin-C. Calcium ion binding site The calcium ion is coordinated in a pentagonal bipyramidal configuration. The six residues involved in the binding are in positions 1, 3, 5, 7, 9 and 12; these residues are denoted ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
