Structure, Subunit Topology, and Actin-binding Activity of the Arp2/3 Complex from Acanthamoeba

RD Mullins, WF Stafford, TD Pollard - The Journal of cell biology, 1997 - rupress.org
The Arp2/3 complex, first isolated from Acanthamoeba castellani by affinity chromatography
on profilin, consists of seven polypeptides; two actinrelated proteins, Arp2 and Arp3; and five …

Structure, subunit topology, and actin-binding activity of the Arp2/3 complex from Acanthamoeba.

RD Mullins, WF Stafford, TD Pollard - The Journal of Cell Biology, 1997 - europepmc.org
Abstract The Arp2/3 complex, first isolated from Acanthamoeba castellani by affinity
chromatography on profilin, consists of seven polypeptides; two actinrelated proteins, Arp2 …

Structure, subunit topology, and actin-binding activity of the Arp2/3 complex from Acanthamoeba

RD Mullins, WF Stafford… - The Journal of cell …, 1997 - pubmed.ncbi.nlm.nih.gov
The Arp2/3 complex, first isolated from Acanthamoeba castellani by affinity chromatography
on profilin, consists of seven polypeptides; two actin-related proteins, Arp2 and Arp3; and …

[PDF][PDF] Structure, Subunit Topology, and Actin-binding Activity of the Arp2/3 Complex from Acanthamoeba

RD Mullins, WF Stafford, TD Pollard - The Journal of Cell Biology, 1997 - Citeseer
The Arp2/3 complex, first isolated from Acanthamoeba castellani by affinity chromatography
on profilin, consists of seven polypeptides; two actinrelated proteins, Arp2 and Arp3; and five …

[PDF][PDF] Structure, Subunit Topology, and Actin-binding Activity of the Arp2/3 Complex from Acanthamoeba

RD Mullins, WF Stafford… - The Journal of Cell …, 1997 - pdfs.semanticscholar.org
The Arp2/3 complex, first isolated from Acanthamoeba castellani by affinity chromatography
on profilin, consists of seven polypeptides; two actinrelated proteins, Arp2 and Arp3; and five …

Structure, subunit topology, and actin-binding activity of the Arp2/3 complex from Acanthamoeba.

RD Mullins, WF Stafford, TD Pollard - 1997 - cabidigitallibrary.org
The actin related protein (Arp) 2/3 complex, isolated from Acanthamoeba castellanii, was
shown to be homogeneous by hydrodynamic criteria, with a Stokes' radius of 5.3 nm by gel …

[HTML][HTML] Structure, Subunit Topology, and Actin-binding Activity of the Arp2/3 Complex from Acanthamoeba

RD Mullins, WF Stafford, TD Pollard - The Journal of Cell Biology, 1997 - ncbi.nlm.nih.gov
Abstract The Arp2/3 complex, first isolated from Acanthamoeba castellani by affinity
chromatography on profilin, consists of seven polypeptides; two actinrelated proteins, Arp2 …

[PDF][PDF] Structure, Subunit Topology, and Actin-binding Activity of the Arp2/3 Complex from Acanthamoeba

RD Mullins, WF Stafford, TD Pollard - The Journal of Cell Biology, 1997 - researchgate.net
The Arp2/3 complex, first isolated from Acanthamoeba castellani by affinity chromatography
on profilin, consists of seven polypeptides; two actinrelated proteins, Arp2 and Arp3; and five …

[PDF][PDF] Structure, Subunit Topology, and Actin-binding Activity of the Arp2/3 Complex from Acanthamoeba

RD Mullins, WF Stafford, TD Pollard - The Journal of Cell Biology, 1997 - academia.edu
The Arp2/3 complex, first isolated from Acanthamoeba castellani by affinity chromatography
on profilin, consists of seven polypeptides; two actinrelated proteins, Arp2 and Arp3; and five …