12-fold difference between the critical monomer concentrations of the two ends of actin filaments in physiological salt conditions
about
The control of actin nucleotide exchange by thymosin beta 4 and profilin. A potential regulatory mechanism for actin polymerization in cellsTropomodulin-3 is essential in asymmetric division during mouse oocyte maturation.Characterization of the biochemical properties and biological function of the formin homology domains of Drosophila DAAM.Synchrotron x-ray diffraction studies of actin structure during polymerization.Chemotactic signaling pathways in neutrophils: from receptor to actin assembly.Reconstitution of a prokaryotic minus end-tracking system using TubRC centromeric complexes and tubulin-like protein TubZ filaments.FtsZ filament capping by MciZ, a developmental regulator of bacterial division.Ultrastructure of unit fragments of the skeleton of the human erythrocyte membrane.Polymerization of ADP-actinBinding and assembly of actin filaments by plasma membranes from Dictyostelium discoideum.How actin binds and assembles onto plasma membranes from Dictyostelium discoideum.Actin structure and function.ADP-ribosylation of actin by clostridial toxins.Interaction of a Dictyostelium member of the plastin/fimbrin family with actin filaments and actin-myosin complexes.Role of actin polymerization in cell locomotion: molecules and models.Does actin bind to the ends of thin filaments in skeletal muscle?Domain structure in actin-binding proteins: expression and functional characterization of truncated severin.'Cap 90', a 90-kDa Ca2+-dependent F-actin-capping protein from vertebrate brain.
P2860
Q24657873-B424AE83-57B1-4192-AF15-F444D50BDFE6Q27333117-8D508055-EDC5-47D2-8960-8F3998457615Q30494160-2E437BEA-7948-4FFF-AAF2-9F7D6C849E4EQ34622163-08C09A7A-29D5-4348-92FD-3067B438AEA5Q34713881-F313C79F-ECC0-4E22-A963-22AC4A3E325FQ35484814-057A3801-77F2-4FCB-9E5A-6BCE8D861546Q35567122-0FFC4B1D-D277-498E-8887-9720D8DF1AE1Q36211263-D3CF4B03-D072-4F44-A175-7B2BE1327441Q36211356-F4D84E39-E922-421F-B424-CE3C20DE9921Q36215193-56C5B655-73C1-449F-8872-BD0849459B6FQ36219038-DFCA8730-6AE3-4CCD-B9AD-31F1B7D67154Q37840146-4BF04DAD-A75A-4936-B2FC-06A0090FE88EQ38697508-BB36D282-2E9C-4B2E-861E-F822649F168EQ40243219-B8F27196-EC72-4BDA-AA4B-D40CE21AA2CCQ40821929-A2F72A97-5AE9-4D3B-85C0-D82D32EBDEFBQ41470021-455214F4-7E5B-43F5-87A1-361994CCD683Q43107722-86C5C311-375B-4184-85AA-A8FAE5EDEA65Q48714889-FC987B9A-EB21-4D7A-8D33-96E3D549E1F3
P2860
12-fold difference between the critical monomer concentrations of the two ends of actin filaments in physiological salt conditions
description
article científic
@ca
article scientifique
@fr
articolo scientifico
@it
artigo científico
@pt
bilimsel makale
@tr
scientific article published on August 1983
@en
vedecký článok
@sk
vetenskaplig artikel
@sv
videnskabelig artikel
@da
vědecký článek
@cs
name
12-fold difference between the ...... physiological salt conditions
@en
12-fold difference between the ...... physiological salt conditions.
@nl
type
label
12-fold difference between the ...... physiological salt conditions
@en
12-fold difference between the ...... physiological salt conditions.
@nl
prefLabel
12-fold difference between the ...... physiological salt conditions
@en
12-fold difference between the ...... physiological salt conditions.
@nl
P2860
P356
P1476
12-fold difference between the ...... physiological salt conditions
@en
P2093
P2860
P304
P356
10.1073/PNAS.80.16.4922
P407
P577
1983-08-01T00:00:00Z