F-actin capping protein - significado y definición. Qué es F-actin capping protein
Diclib.com
Diccionario ChatGPT
Búsqueda en el diccionario Soluciones personalizadas
Ingrese una palabra o frase en cualquier idioma 👆
Idioma:

Traducción y análisis de palabras por inteligencia artificial ChatGPT

En esta página puede obtener un análisis detallado de una palabra o frase, producido utilizando la mejor tecnología de inteligencia artificial hasta la fecha:

  • cómo se usa la palabra
  • frecuencia de uso
  • se utiliza con más frecuencia en el habla oral o escrita
  • opciones de traducción
  • ejemplos de uso (varias frases con traducción)
  • etimología
  1. Diccionarios
  2. Diccionario inglés
  3. F-actin capping protein

Qué (quién) es F-actin capping protein - definición


F-actin capping protein         
A HETERODIMER CONSISTING OF ALPHA AND BETA SUBUNITS THAT BINDS TO AND CAPS THE BARBED ENDS OF ACTIN FILAMENTS, THEREBY REGULATING THE POLYMERIZATION OF ACTIN MONOMERS BUT NOT SEVERING ACTIN FILAMENTS.
In molecular biology, the F-actin capping protein is a protein complex which binds in a calcium-independent manner to the fast-growing ends of actin filaments (barbed end), thereby blocking the exchange of subunits at these ends. Unlike gelsolin and severin this protein does not sever actin filaments.
https://en.wikipedia.org/wiki/F-actin_capping_protein
Actin         
  • [[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
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
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.
https://en.wikipedia.org/wiki/Actin
actin         
  • [[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
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
['akt?n]
¦ noun Biochemistry a protein which forms (together with myosin) the contractile filaments of muscle cells.
Origin
1940: from Gk aktis, aktin- 'ray' + -in1.
Búsqueda en el diccionario
Todos los diccionarios Diccionario alemán Diccionario español Diccionario francés Diccionario francés-ruso Diccionario griego Diccionario holandés Diccionario inglés Diccionario inglés-alemán Diccionario inglés-español Diccionario inglés-francés Diccionario inglés-griego Diccionario inglés-holandés Diccionario inglés-italiano Diccionario inglés-ruso Diccionario inglés-árabe Diccionario italiano Diccionario italiano-ruso Diccionario latín-español Diccionario latín-portugués Diccionario portugués Diccionario portugués-ruso Diccionario ruso Diccionario árabe
Creado por IA
Inglés Ruso Español Portugués Alemán Francés Griego Holandés Italiano Árabe
Idioma de la interfaz
Русский English Español Português Deutsch Français Ελληνικά Nederlands Italiano عربي
Contactos
Contáctenos



Privacidad
Política de privacidad