Bacterial cell division protein FtsZ assembles into protofilament sheets and minirings, structural homologs of tubulin polymers.

HP Erickson, DW Taylor, KA Taylor… - Proceedings of the …, 1996 - National Acad Sciences
The bacterial cell division protein FtsZ is a homolog of tubulin, but it has not been determined
whether FtsZ polymers are structurally related to the microtubule lattice. In the present study…

Three-dimensional structure of the myosin V inhibited state by cryoelectron tomography

…, DW Taylor, EB Krementsova, KM Trybus, KA Taylor - Nature, 2006 - nature.com
Unconventional myosin V (myoV) is an actin-based molecular motor that has a key function
in organelle and mRNA transport, as well as in membrane trafficking 1 . MyoV was the first …

Novel structures for α-actinin: F-actin interactions and their implications for actin–membrane attachment and tension sensing in the cytoskeleton

CM Hampton, DW Taylor, KA Taylor - Journal of molecular biology, 2007 - Elsevier
We have applied correspondence analysis to electron micrographs of 2-D rafts of F-actin
cross-linked with α-actinin on a lipid monolayer to investigate α-actinin:F-actin binding and …

Structure of myosin filaments from relaxed Lethocerus flight muscle by cryo-EM at 6 Å resolution

…, DW Taylor, MK Reedy, RJ Edwards, KA Taylor - Science advances, 2016 - science.org
We describe a cryo–electron microscopy three-dimensional image reconstruction of relaxed
myosin II–containing thick filaments from the flight muscle of the giant water bug Lethocerus …

A 3-D reconstruction of smooth muscle α-actinin by CryoEm reveals two different conformations at the actin-binding region

J Liu, DW Taylor, KA Taylor - Journal of molecular biology, 2004 - Elsevier
Cryoelectron microscopy was used to obtain a 3-D image at 2.0 nm resolution of 2-D arrays
of smooth muscle α-actinin. The reconstruction reveals a well-resolved long central domain …

The myosin II coiled-coil domain atomic structure in its native environment

…, Z Hu, N Daneshparvar, DW Taylor… - Proceedings of the …, 2021 - National Acad Sciences
The atomic structure of the complete myosin tail within thick filaments isolated from Lethocerus
indicus flight muscle is described and compared to crystal structures of recombinant, …

The three-dimensional structure of α-actinin obtained by cryoelectron microscopy suggests a model for Ca2+-dependent actin binding

J Tang, DW Taylor, KA Taylor - Journal of molecular biology, 2001 - Elsevier
The three-dimensional structure of α-actinin from rabbit skeletal muscle was determined by
cryoelectron microscopy in combination with homology modeling of the separate domain …

CryoEM structure of Drosophila flight muscle thick filaments at 7 Å resolution

N Daneshparvar, DW Taylor, TS O'Leary… - Life Science …, 2020 - life-science-alliance.org
Striated muscle thick filaments are composed of myosin II and several non-myosin proteins.
Myosin II’s long α-helical coiled-coil tail forms the dense protein backbone of filaments, …

Isoforms of α-actinin from cardiac, smooth, and skeletal muscle form polar arrays of actin filaments

KA Taylor, DW Taylor, F Schachat - The Journal of cell biology, 2000 - rupress.org
We have used a positively charged lipid monolayer to form two-dimensional bundles of F-actin
cross-linked by α-actinin to investigate the relative orientation of the actin filaments within …

[PDF][PDF] Formation of two-dimensional complexes of F-actin and crosslinking proteins on lipid monolayers: demonstration of unipolar alpha-actinin-F-actin crosslinking

KA Taylor, DW Taylor - Biophysical journal, 1994 - cell.com
A method is described for forming two-dimensional (2-D) paracrystalline complexes of F-actin
and bundling/gelation proteins on positively charged lipid monolayers. These arrays …