G-actin - translation to Αγγλικά
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G-actin - translation to Αγγλικά

MOTOR PROTEIN INVOLVED IN MUSCLE CONTRACTION
G-actin; Alpha-actin; F-actin; Actins; Microfilament proteins; Microfilament protein; Actinous; F actin; G actin; Actin tail; Actin polymerization
  • [[Ribbon diagram]] of an actin monomer from rabbit skeletal muscle, with the molecule's surface shown semi-transparent. The four subdomains as well as the bound ATP and calcium ion are annotated.
  •  s2cid = 4317981 }}</ref>
  • Principal interactions of structural proteins are at [[cadherin]]-based adherens junction. Actin filaments are linked to α-[[actinin]] and to the membrane through [[vinculin]]. The head domain of vinculin associates to E-cadherin via [[α-catenin]], [[β-catenin]], and [[γ-catenin]]. The tail domain of vinculin binds to membrane lipids and to actin filaments.
  •  bibcode = 2001Sci...294.1679R }}</ref> Each colour corresponds to a subunit: Arp3, orange; Arp2, sea blue (subunits 1 and 2 are not shown); p40, green; p34, light blue; p20, dark blue; p21, magenta; p16, yellow.
  • chaperonin]] CCT
  • Cardiac sarcomere structure featuring actin and myosin
  • Diagram of a ''[[zonula occludens]]'' or tight junction, a structure that joins the [[epithelium]] of two cells. Actin is one of the anchoring elements shown in green.
  • asymmetric cell division]]. Then, at 10 s, formation of the contractile actin ring can be observed.
  • The protein [[gelsolin]], which is a key regulator in the assembly and disassembly of actin.
  • Albert von Szent-Györgyi Nagyrápolt]], co-discoverer of actin with [[Brunó Ferenc Straub]]
  • Fluorescence]] micrograph showing F-actin (in green) in rat [[fibroblast]]s
  • Structure of [[MreB]], a bacterial protein whose three-dimensional structure resembles that of G-actin
  •  doi = 10.1186/1471-2121-8-2 }}</ref>
  •  doi = 10.1371/journal.pgen.0020010 }}</ref>
  • nemaline rods]] produced by the [[transfection]] of a [[DNA sequence]] of ''[[ACTA1]]'', which is the carrier of a [[mutation]] responsible for nemaline myopathy<ref name="Bathe_2007"/>
  •  doi = 10.1186/1471-2202-6-24 }}</ref>
  •  doi = 10.1110/ps.03518104 }}</ref>
  • eukariotic]] prefoldin has a similar structure.<ref name="Simons_2004"/>
  •  s2cid = 4359724 }}</ref> The profilin shown belongs to group II, normally present in the [[kidney]]s and the [[brain]].
  • A merged stack of confocal images showing actin filaments within a cell. The image has been colour coded in the z axis to show in a 2D image which heights filaments can be found at within cells.
  • 291x291px
  • Chemical structure of [[phalloidin]]
  • Microfilament formation showing the polymerization mechanism for converting G-actin to F-actin; note the hydrolysis of the ATP.
  • Western blot for cytoplasmic actin from rat lung and epididymis

G-actin         

общая лексика

G-актин

глобулярный актин

actin         

общая лексика

актин

Смотрите также

globular actin

g         
  • Pictogram of a Camel
  • Early Etruscan C
  • Early Greek Gamma
  • 10px
  • Typographic variants]] include a double-storey and single-storey '''g'''.
  • 8px
  • Gimel
LETTER OF THE LATIN ALPHABET
G; G (letter); ℊ; Script g; Double-story g; Single-story g; Single-storey g; Openptail g; Looptail g; Double-storey g; Open-tail g; Loop-tail g; ASCII 71; ASCII 103; U+0047; U+0067; Letter G; Opentail g
g I specific gravity noun удельный вес II G - gauss noun гаусс (единица магнитной индукции) III G - giga noun гига- (10 в 9-й степени)

Ορισμός

АКСЕЛЕРОМЕТР
(от лат. accelero - ускоряю и ...метр), прибор для измерения ускорений (перегрузок) летательных аппаратов и др.

Βικιπαίδεια

Actin

Actin is a family of globular multi-functional proteins that form microfilaments in the cytoskeleton, and the thin filaments in muscle fibrils. It is found in essentially all eukaryotic cells, where it may be present at a concentration of over 100 μM; its mass is roughly 42 kDa, with a diameter of 4 to 7 nm.

An actin protein is the monomeric subunit of two types of filaments in cells: microfilaments, one of the three major components of the cytoskeleton, and thin filaments, part of the contractile apparatus in muscle cells. It can be present as either a free monomer called G-actin (globular) or as part of a linear polymer microfilament called F-actin (filamentous), both of which are essential for such important cellular functions as the mobility and contraction of cells during cell division.

Actin participates in many important cellular processes, including muscle contraction, cell motility, cell division and cytokinesis, vesicle and organelle movement, cell signaling, and the establishment and maintenance of cell junctions and cell shape. Many of these processes are mediated by extensive and intimate interactions of actin with cellular membranes. In vertebrates, three main groups of actin isoforms, alpha, beta, and gamma have been identified. The alpha actins, found in muscle tissues, are a major constituent of the contractile apparatus. The beta and gamma actins coexist in most cell types as components of the cytoskeleton, and as mediators of internal cell motility. It is believed that the diverse range of structures formed by actin enabling it to fulfill such a large range of functions is regulated through the binding of tropomyosin along the filaments.

A cell's ability to dynamically form microfilaments provides the scaffolding that allows it to rapidly remodel itself in response to its environment or to the organism's internal signals, for example, to increase cell membrane absorption or increase cell adhesion in order to form cell tissue. Other enzymes or organelles such as cilia can be anchored to this scaffolding in order to control the deformation of the external cell membrane, which allows endocytosis and cytokinesis. It can also produce movement either by itself or with the help of molecular motors. Actin therefore contributes to processes such as the intracellular transport of vesicles and organelles as well as muscular contraction and cellular migration. It therefore plays an important role in embryogenesis, the healing of wounds, and the invasivity of cancer cells. The evolutionary origin of actin can be traced to prokaryotic cells, which have equivalent proteins. Actin homologs from prokaryotes and archaea polymerize into different helical or linear filaments consisting of one or multiple strands. However the in-strand contacts and nucleotide binding sites are preserved in prokaryotes and in archaea. Lastly, actin plays an important role in the control of gene expression.

A large number of illnesses and diseases are caused by mutations in alleles of the genes that regulate the production of actin or of its associated proteins. The production of actin is also key to the process of infection by some pathogenic microorganisms. Mutations in the different genes that regulate actin production in humans can cause muscular diseases, variations in the size and function of the heart as well as deafness. The make-up of the cytoskeleton is also related to the pathogenicity of intracellular bacteria and viruses, particularly in the processes related to evading the actions of the immune system.

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