F-actin capping protein - significado y definición. Qué es F-actin capping protein
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Qué (quién) es F-actin capping protein - definición


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.
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.
Beta-actin         
PROTEIN-CODING GENE IN THE SPECIES HOMO SAPIENS
ACTB; Beta actin; Β-actin; ACTB (gene)
Beta-actin (human gene and protein abbreviation ACTB/ACTB) is one of six different actin isoforms which have been identified in humans. This is one of the two nonmuscle cytoskeletal actins.

Wikipedia

F-actin capping protein
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.