Results 251 to 260 of about 209,245 (296)

Endogenous inhibitor of the ADP-ribosylation of (a) G-protein(s) as catalyzed by pertussis toxin is present in rat liver

open access: yesFEBS Letters, 1988
The inhibitor activity of the ADP-ribosylation of (a) G-protein(s) as catalyzed by pertussis toxin was found in the membrane extract of rat liver. The inhibitor activity was found in the fractions of DEAE-Sephacel column chromatography at 50–120 mM NaCl.
Miki Hara-Yokoyama   +2 more
exaly   +2 more sources

Fusion protein of Δ27LFn and EFn has the potential as a novel anthrax toxin inhibitor

open access: yesFEBS Letters, 2009
PA-binding domain of LF (LFn) or PA-binding domain of EF (EFn) is the anthrax protective antigen (PA) binding domain of anthrax lethal factor (LF) or edema factor (EF).
Dayong Dong, Chenguang Cai
exaly   +2 more sources
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Designing a polyvalent inhibitor of anthrax toxin

Nature Biotechnology, 2001
Screening peptide libraries is a proven strategy for identifying inhibitors of protein-ligand interactions. Compounds identified in these screens often bind to their targets with low affinities. When the target protein is present at a high density on the surface of cells or other biological surfaces, it is sometimes possible to increase the biological ...
M, Mourez   +7 more
openaire   +2 more sources

Metallopeptidase Inhibitors of Tetanus Toxin:  A Combinatorial Approach

Journal of Medicinal Chemistry, 1999
The bacterial protein tetanus toxin (TeNt), which belongs to the family of zinc endopeptidases, cleaves synaptobrevin, an essential synaptic protein component of the neurotransmitter exocytosis apparatus, at a single peptide bond (Gln76-Phe77). This protease activity is a particularly attractive target for designing potent and selective synthetic ...
Martin, Loïc   +5 more
openaire   +3 more sources

AB5 toxins: structures and inhibitor design

Current Opinion in Structural Biology, 2000
High-resolution crystal structures of AB(5) toxins in their native form or in complex with a variety of ligands have led to the structure-based design and discovery of inhibitors targeting different areas of the toxins. The most significant progress is the development of highly potent multivalent ligands that block binding of the toxins to their ...
E, Fan   +3 more
openaire   +2 more sources

Diacetyl—A growth and toxin inhibitor of Aspergilli

Journal of Stored Products Research, 1985
Abstract Diacetyl (2,3-butanedione) a food additive, was found to be very effective in inhibiting growth and toxin production of Aspergillus flavus, A. versicolor and A. ochraceus when grown on synthetic liquid media and on natural substrates of maize and maize flour. Total growth inhibition of A. flavus and A. versicolor was observed at 250 ppm when
Rama Devi, G, Polasa, H
openaire   +1 more source

Small-Molecule Inhibitors of Ricin and Shiga Toxins

2011
This review summarizes the successes and continuing challenges associated with the identification of small-molecule inhibitors of ricin and Shiga toxins, members of the RNA N-glycosidase family of toxins that irreversibly inactivate eukaryotic ribosomes through the depurination of a conserved adenosine residue within the sarcin-ricin loop (SRL) of 28S ...
Paul G, Wahome   +2 more
openaire   +2 more sources

The Rational Design of Bacterial Toxin Inhibitors

Current Computer Aided-Drug Design, 2007
Protein toxins play key roles in many infectious diseases of humans which are caused by bacteria. In some cases the toxin alone is directly responsible for the majority of the symptoms of the disease (e.g. tetanus, anthrax, diphtheria). In others the toxin is one of an arsenal of virulence factors which allow the bacterium to cause disease. Antibiotics
Graeme Clark   +2 more
openaire   +1 more source

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