The bulk of unpolymerized actin in Xenopus egg extracts is ATP-bound.
about
Regulatory interaction of phosducin-like protein with the cytosolic chaperonin complexIn vivo importance of actin nucleotide exchange catalyzed by profilin.The majority of the Saccharomyces cerevisiae septin complexes do not exchange guanine nucleotides.The polymerization motor.Nuclear actin and protein 4.1: essential interactions during nuclear assembly in vitro.Xenopus laevis actin-depolymerizing factor/cofilin: a phosphorylation-regulated protein essential for development.A purified Drosophila septin complex forms filaments and exhibits GTPase activity.Xenopus actin depolymerizing factor/cofilin (XAC) is responsible for the turnover of actin filaments in Listeria monocytogenes tails.Characterization of two related Drosophila gamma-tubulin complexes that differ in their ability to nucleate microtubules.Actin-based movement of Listeria monocytogenes: actin assembly results from the local maintenance of uncapped filament barbed ends at the bacterium surface.ATP-dependent membrane assembly of F-actin facilitates membrane fusion.Actin and Actin-Binding Proteins.Actin: Structure, Function, Dynamics, and Interactions with Bacterial Toxins.Mutant actins that stabilise F-actin use distinct mechanisms to activate the SRF coactivator MAL.Actin Turnover in Lamellipodial Fragments.Beta-thymosins from marine invertebrates: primary structure and interaction with actin.Cofilin reduces the mechanical properties of actin filaments: approach with coarse-grained methods.
P2860
Q24534363-F874AAFB-CB82-4099-815C-2B24E76612CEQ27939378-9B1E28A6-112C-4474-B1C0-9D81859E50EBQ27939520-CA71B004-CBF1-408F-8281-E8AA03E5AED9Q34156477-2B9DC879-E6CA-46FB-A36B-4B8C913593EDQ35977914-D7BA20A1-7F6F-4BC3-AF21-D4DACBE01F53Q36236511-E42BE340-255A-4E32-AA7D-1F084D5DDD2CQ36236841-6F232E2A-FE70-4C37-BDA7-3CDCB6912CC0Q36254640-96FFEB7D-70B5-4FA6-985A-C44FABE17B81Q36255800-33B12E6A-C56E-42E1-B140-9AD27E63855DQ36382607-A006E3D5-31A6-4853-9CE8-A0EC63D34CF6Q38670988-9C2F80BA-41B6-476D-9599-4F0F14602C16Q38779192-610DFA9B-1567-4A3D-8453-D8EC1322C70BQ39009746-5E1C6333-FC2C-450F-9C4B-F374BF0B255BQ40251456-B7F8D1B2-212A-4CDB-ACCB-5ABA25FD2A3FQ46168953-5A09994E-1B3C-47EF-92F3-B1AE889881F5Q52197209-4E9E7D14-021C-4365-8F14-659BB5A6E21DQ53302609-ED726826-22DC-4718-80A7-B1A4485036E8
P2860
The bulk of unpolymerized actin in Xenopus egg extracts is ATP-bound.
description
article científic
@ca
article scientifique
@fr
articolo scientifico
@it
artigo científico
@pt
bilimsel makale
@tr
scientific article published on February 1995
@en
vedecký článok
@sk
vetenskaplig artikel
@sv
videnskabelig artikel
@da
vědecký článek
@cs
name
The bulk of unpolymerized actin in Xenopus egg extracts is ATP-bound.
@en
The bulk of unpolymerized actin in Xenopus egg extracts is ATP-bound.
@nl
type
label
The bulk of unpolymerized actin in Xenopus egg extracts is ATP-bound.
@en
The bulk of unpolymerized actin in Xenopus egg extracts is ATP-bound.
@nl
prefLabel
The bulk of unpolymerized actin in Xenopus egg extracts is ATP-bound.
@en
The bulk of unpolymerized actin in Xenopus egg extracts is ATP-bound.
@nl
P2093
P2860
P356
P1476
The bulk of unpolymerized actin in Xenopus egg extracts is ATP-bound.
@en
P2093
J Rosenblatt
T J Mitchison
P2860
P304
P356
10.1091/MBC.6.2.227
P577
1995-02-01T00:00:00Z