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…
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 …
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 …
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 …
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
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 …
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, …
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 …
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, …
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 …
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 …
and bundling/gelation proteins on positively charged lipid monolayers. These arrays …