Anthrax toxin: receptor binding, internalization, pore formation, and translocation

JAT Young, RJ Collier - Annu. Rev. Biochem., 2007 - annualreviews.org
Anthrax toxin consists of three nontoxic proteins that self-assemble at the surface of receptor-
bearing mammalian cells or in solution, yielding a series of toxic complexes. Two of the …

Membrane translocation by anthrax toxin

RJ Collier - Molecular aspects of medicine, 2009 - Elsevier
Much attention has been focused on anthrax toxin recently, both because of its central role
in the pathogenesis of Bacillus anthracis and because it has proven to be one of the most …

α2δ expression sets presynaptic calcium channel abundance and release probability

MB Hoppa, B Lana, W Margas, AC Dolphin, TA Ryan - Nature, 2012 - nature.com
Synaptic neurotransmitter release is driven by Ca2+ influx through active zone voltage-
gated calcium channels (VGCCs),. Control of active zone VGCC abundance and function …

The metal-ion-dependent adhesion site in the Von Willebrand factor-A domain of α2δ subunits is key to trafficking voltage-gated Ca2+ channels

C Canti, M Nieto-Rostro, I Foucault… - Proceedings of the …, 2005 - National Acad Sciences
All auxiliary α2δ subunits of voltage-gated Ca2+ (CaV) channels contain an extracellular
Von Willebrand factor-A (VWA) domain that, in α2δ-1 and-2, has a perfect metal-ion …

Crystal structure of a complex between anthrax toxin and its host cell receptor

E Santelli, LA Bankston, SH Leppla, RC Liddington - Nature, 2004 - nature.com
Anthrax toxin consists of the proteins protective antigen (PA), lethal factor (LF) and oedema
factor (EF). The first step of toxin entry into host cells is the recognition by PA of a receptor on …

Cell cycle regulation of central spindle assembly

M Mishima, V Pavicic, U Grüneberg, EA Nigg… - Nature, 2004 - nature.com
The bipolar mitotic spindle is responsible for segregating sister chromatids at anaphase.
Microtubule motor proteins generate spindle bipolarity and enable the spindle to perform …

Structure of heptameric protective antigen bound to an anthrax toxin receptor: a role for receptor in pH-dependent pore formation

DB Lacy, DJ Wigelsworth, RA Melnyk… - Proceedings of the …, 2004 - National Acad Sciences
After binding to cellular receptors and proteolytic activation, the protective antigen
component of anthrax toxin forms a heptameric prepore. The prepore later undergoes pH …

Anthrax toxin: the long and winding road that leads to the kill

L Abrami, N Reig, FG van der Goot - Trends in microbiology, 2005 - cell.com
The past five years have led to a tremendous increase in our molecular understanding of the
mode of action of the anthrax toxin, one of the two main virulence factors produced by …

[HTML][HTML] Shear‐induced unfolding activates von Willebrand factor A2 domain for proteolysis

C Baldauf, R Schneppenheim, W Stacklies… - Journal of Thrombosis …, 2009 - Elsevier
Background: To avoid pathological platelet aggregation by von Willebrand factor (VWF),
VWF multimers are regulated in size and reactivity for adhesion by ADAMTS13‐mediated …

Anthrax toxins: a weapon to systematically dismantle the host immune defenses

JN Tournier, SR Paccani, A Quesnel-Hellmann… - Molecular aspects of …, 2009 - Elsevier
Successful colonization of the host by bacterial pathogens relies on their capacity to evade
the complex and powerful defenses opposed by the host immune system, at least in the …