Antibacterial nanomaterials: mechanisms, impacts on antimicrobial resistance and design principles
M Xie, M Gao, Y Yun, M Malmsten… - Angewandte Chemie …, 2023 - Wiley Online Library
Antimicrobial resistance (AMR) is one of the biggest threats to the environment and health.
AMR rapidly invalidates conventional antibiotics, and antimicrobial nanomaterials have …
AMR rapidly invalidates conventional antibiotics, and antimicrobial nanomaterials have …
Insights into the structure, function, and dynamics of the bacterial cytokinetic FtsZ-ring
R McQuillen, J Xiao - Annual Review of Biophysics, 2020 - annualreviews.org
The FtsZ protein is a highly conserved bacterial tubulin homolog. In vivo, the functional form
of FtsZ is the polymeric, ring-like structure (Z-ring) assembled at the future division site …
of FtsZ is the polymeric, ring-like structure (Z-ring) assembled at the future division site …
Stress-induced mutagenesis, gambler cells, and stealth targeting antibiotic-induced evolution
Mechanisms of evolution and evolution of antibiotic resistance are both fundamental and
world health problems. Stress-induced mutagenesis defines mechanisms of mutagenesis …
world health problems. Stress-induced mutagenesis defines mechanisms of mutagenesis …
Molecular dissection of a yeast septin: distinct domains are required for septin interaction, localization, and function
A Casamayor, M Snyder - Molecular and cellular biology, 2003 - Am Soc Microbiol
The septins are a family of cytoskeletal proteins present in animal and fungal cells. They
were first identified for their essential role in cytokinesis, but more recently, they have been …
were first identified for their essential role in cytokinesis, but more recently, they have been …
FtsZ protofilaments use a hinge-opening mechanism for constrictive force generation
The essential bacterial protein FtsZ is a guanosine triphosphatase that self-assembles into a
structure at the division site termed the “Z ring”. During cytokinesis, the Z ring exerts a …
structure at the division site termed the “Z ring”. During cytokinesis, the Z ring exerts a …
GTP hydrolysis of cell division protein FtsZ: evidence that the active site is formed by the association of monomers
DJ Scheffers, JG de Wit, T den Blaauwen… - Biochemistry, 2002 - ACS Publications
The essential prokaryotic cell division protein FtsZ is a tubulin homologue that forms a ring at
the division site. FtsZ forms polymers in a GTP-dependent manner. Recent biochemical …
the division site. FtsZ forms polymers in a GTP-dependent manner. Recent biochemical …
New (and not so new) antibacterial targets–from where and when will the novel drugs come?
SJ Projan - Current opinion in pharmacology, 2002 - Elsevier
Although the need for new antibacterial therapies and strategies is greater than it has been
in a quarter of a century and despite considerable effort, little progress has been observed in …
in a quarter of a century and despite considerable effort, little progress has been observed in …
[HTML][HTML] Structure prediction of magnetosome-associated proteins
H Nudelman, R Zarivach - Frontiers in microbiology, 2014 - frontiersin.org
Magnetotactic bacteria (MTB) are Gram-negative bacteria that can navigate along
geomagnetic fields. This ability is a result of a unique intracellular organelle, the …
geomagnetic fields. This ability is a result of a unique intracellular organelle, the …
The tubulin ancester, FtsZ, draughtsman, designer and driving force for bacterial cytokinesis
SG Addinall, B Holland - Journal of molecular biology, 2002 - Elsevier
We discuss in this review the regulation of synthesis and action of FtsZ, its structure in
relation to tubulin and microtubules, and the mechanism of polymerization and disassembly …
relation to tubulin and microtubules, and the mechanism of polymerization and disassembly …
The GTPase Activity of Escherichia coli FtsZ Determines the Magnitude of the FtsZ Polymer Bundling by ZapA in Vitro
T Mohammadi, GEJ Ploeger, J Verheul… - Biochemistry, 2009 - ACS Publications
FtsZ polymerizes in a ring-like structure at mid cell to initiate cell division in Escherichia coli.
The ring is stabilized by a number of proteins among which the widely conserved ZapA …
The ring is stabilized by a number of proteins among which the widely conserved ZapA …