نتایج جستجو برای: beta toxin

تعداد نتایج: 236856  

Journal: :Journal of molecular biology 2010
Mark A Blenner Oren Shur Géza R Szilvay Donald M Cropek Scott Banta

Beta roll motifs are associated with several proteins secreted by the type 1 secretion system (T1SS). Located just upstream of the C-terminal T1SS secretion signal, they are believed to act as calcium-induced switches that prevent folding before secretion. Bordetella pertussis adenylate cyclase (CyaA) toxin has five blocks of beta roll motifs (or repeats-in-toxin motifs) separated by linkers. T...

Journal: :Rinsho Biseibutsu Jinsoku Shindan Kenkyukai shi = JARMAM : Journal of the Association for Rapid Method and Automation in Microbiology 2009
Hitoshi Saito Masaharu Inoue Masayoshi Tomiki Hiroshi Nemoto Tomoe Komoriya Junko Kimata Kunitomo Watanabe Hideki Kohno

Only a few methods exist for simple, sensitive and rapid detection of alpha-toxin in clinical and biological samples. The aim of our study was to establish a procedure for the production of an antibody against a recombinant antigen with confirmed sequence identity. We applied a noble approach based on proteomics using a mass spectrometer for the conclusive identification of the recombinant alph...

Journal: :Arquivo Brasileiro de Medicina Veterinária e Zootecnia 2006

Journal: :Proceedings of the National Academy of Sciences of the United States of America 2001
T Scherf R Kasher M Balass M Fridkin S Fuchs E Katchalski-Katzir

Snake-venom alpha-bungarotoxin is a member of the alpha-neurotoxin family that binds with very high affinity to the nicotinic acetylcholine receptor (AChR) at the neuromuscular junction. The structure of the complex between alpha-bungarotoxin and a 13-mer peptide (WRYYESSLEPYPD) that binds the toxin with high affinity, thus inhibiting its interactions with AChR with an IC(50) of 2 nM, has been ...

Journal: :The Journal of neuroscience : the official journal of the Society for Neuroscience 1987
R H Loring R E Zigmond

Although alpha-bungarotoxin (BGT), a common probe for nicotinic ACh receptors from vertebrate skeletal muscle, binds tightly to many autonomic ganglia, it fails to block nicotinic transmission in most of these ganglia. Recently, we have isolated a second toxin, toxin F, that blocks transmission in several autonomic ganglia, including the chick ciliary ganglion. 125I-Toxin F binds to 2 sites in ...

Journal: :Infection and immunity 1989
M H Witvliet D L Burns M J Brennan J T Poolman C R Manclark

The binding of pertussis toxin and its subunits to cell surface receptors and purified glycoproteins was examined. The interaction of pertussis toxin with components of two variant Chinese hamster ovary (CHO) cell lines was studied. These cell lines are deficient in either sialic acid residues (LEC 2) or sialic acid and galactose residues (LEC 8) on cell surface macromolecules. The binding of p...

Journal: :The Journal of Experimental Medicine 1986
M Jacewicz H Clausen E Nudelman A Donohue-Rolfe G T Keusch

A glycolipid that specifically binds shigella toxin was isolated from both HeLa cells and rabbit jejunal mucosa and identified as globotriaosylceramide (Gb3) by its identical mobility on HPTLC to authentic erythrocyte Gb3. Toxin also bound to a band tentatively identified as alpha-hydroxylated Gb3. In addition, toxin bound to P1 antigen present in group B human erythrocyte glycolipid extracts. ...

Journal: :Proceedings of the National Academy of Sciences of the United States of America 1989
F A Ribeiro-Neto M Rodbell

Pertussis toxin catalyzes ADP-ribosylation of a family of GTP-binding proteins (G alpha proteins) involved in signal transduction. It is thought that this activity is responsible for the attenuating effects of the toxin on the actions of a number of hormones and neurotransmitters. By utilizing specific antisera for detecting on electrophoretic transfer blots (Western blots) alpha proteins that ...

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