Results 81 to 90 of about 14,243 (169)

Surfactant-free purification of membrane protein complexes from bacteria: application to the staphylococcal penicillin-binding protein complex PBP2/PBP2a. [PDF]

open access: yes, 2014
Surfactant-mediated removal of proteins from biomembranes invariably results in partial or complete loss of function and disassembly of multi-protein complexes. We determined the capacity of styrene-co-maleic acid (SMA) co-polymer to remove components of
Taylor, Peter W   +22 more
core   +1 more source

Nanoparticle‐Based Strategies to Combat Multidrug‐Resistant Bacteria: Mechanisms, Applications, and Future Perspectives

open access: yesMicrobiologyOpen, Volume 15, Issue 3, June 2026.
Nanobiotics offer a promising strategy to combat antimicrobial resistance (AMR) and multidrug‐resistant (MDR) bacteria. Nanoparticles overcome traditional resistance mechanisms through unique physicochemical properties and multivalent interactions.
Akmal Zubair   +3 more
wiley   +1 more source

The conserved C-terminal tail of FtsZ is necessary for SlmA to bind to FtsZ and to antagonize FtsZ polymerization.

open access: yes, 2014
A) Biosensor assay to monitor the binding of FtsZ C-terminal truncations to SlmA bound to biotinylated SBS17-30mer immobilized on a streptavidin biosensor. Reactions were performed as in Fig. 4B. B) SBS bound SlmA does not co-sediment with stable FtsZ360
Shishen Du (606940)   +1 more
core   +1 more source

ZipA and FtsA* stabilize FtsZ-GDP miniring structures

open access: yesScientific Reports, 2017
The cytokinetic division ring of Escherichia coli comprises filaments of FtsZ tethered to the membrane by FtsA and ZipA. Previous results suggested that ZipA is a Z-ring stabilizer, since in vitro experiments it is shown that ZipA enhanced FtsZ assembly ...
Yaodong Chen   +3 more
doaj   +1 more source

The structure and fragmentation of FtsZ.

open access: yes, 2015
A. The crystal structure of the S. aureus FtsZ monomer bound to GTP-γS (Protein Data Bank: 3WGN). B. FtsZ polymerizes into tubulin-like protofilaments by head-to-tail association with GTP. C. FtsZ is shown schematically. The black arrowhead indicates the
Hideki Maki (316193)   +7 more
core   +1 more source

Antibacterial activity of alkyl gallates is a combination of direct targeting of FtsZ and permeabilization of bacterial membranes

open access: yesFrontiers in Microbiology, 2015
Alkyl gallates are compounds with reported antibacterial activity. One of the modes of action is binding of the alkyl gallates to the bacterial membrane and interference with membrane integrity.
Ewa eKról   +6 more
doaj   +1 more source

Immediate GTP hydrolysis upon FtsZ polymerization [PDF]

open access: yes, 2002
To understand the polymerization dynamics of FtsZ, a bacterial cell division protein similar to tubulin, insight is required into the nature of the nucleotide bound to the polymerized protein. In a previous study, we showed that the FtsZ polymers contain
Driessen, A.J.M.   +3 more
core   +2 more sources

Phosphorylation of FtsZ and FtsA by a DNA Damage-Responsive Ser/Thr Protein Kinase Affects Their Functional Interactions in Deinococcus radiodurans

open access: yesmSphere, 2018
Deinococcus radiodurans, a highly radioresistant bacterium, does not show LexA-dependent regulation of recA expression in response to DNA damage. On the other hand, phosphorylation of DNA repair proteins such as PprA and RecA by a DNA damage-responsive ...
Ganesh K. Maurya   +5 more
doaj   +1 more source

A membrane protein, EzrA, regulates assembly dynamics of FtsZ by interacting with the C-terminal tail of FtsZ

open access: yes, 2007
FtsZ polymerizes to form a dynamic ring structure called the Z-ring at the midcell of bacteria. EzrA, a membrane protein, has been shown to prevent the formation of aberrant Z-rings in the low GC Gram-positive bacteria by inhibiting FtsZ assembly.
SINGH, JK   +7 more
core   +1 more source

Synthetic inhibitors of bacterial cell division targeting the GTP-binding site of FtsZ

open access: yes, 2013
Cell division protein FtsZ is the organizer of the cytokinetic Z-ring in most bacteria and a target for new antibiotics. FtsZ assembles with GTP into filaments that hydrolyze the nucleotide at the association interface between monomers and then ...
Chacón, Pablo   +11 more
core   +1 more source

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