Results 161 to 170 of about 121,700,018 (217)

Design and evaluation of mRNA encoding recombinant neutralizing antibodies for botulinum neurotoxin type B intoxication prophylaxis. [PDF]

Hum Vaccin Immunother
Qiaerxie G, Jiang Y, Li G, Yang Z, Long F, Yu Y, Lu JS, Du P, Cui Y.   +8 more
europepmc   +1 more source

Isolation and characterization of Hc-targeting chimeric heavy chain antibodies neutralizing botulinum neurotoxin type B. [PDF]

Front Immunol
Jiang Y, Wang R, Guo J, Cheng K, Chen L, Wang X, Li Y, Du P, Gao C, Lu J, Yu Y, Yang Z.   +11 more
europepmc   +1 more source

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Studies on the Dissociation of Botulinum Neurotoxin Type A Complexes

Toxicon, 2011
The neurotoxins produced by the various strains of the anaerobic bacterium Clostridium botulinum naturally occur associated with complexing proteins which serve to protect the neurotoxins from the harsh environment of the mammalian gastrointestinal tract during bacterial invasion of the host. Three different complex species with the discrete sizes 19S (
Klaus Fink
exaly   +3 more sources

Cosmetic Uses of Botulinum Neurotoxin Type A

Archives of Facial Plastic Surgery, 2002
C lostridium botulinum produces 7 serologically distinct toxins that are designated A, B, C, D, E, and F. They all have similar structure (a dichain with a disulfide bond) and a molecular weight of about 150 d. The light chain is a zinc-dependent metalloprotease, in which the substrate is one of the fusion proteins responsible for docking and ...
Andrew, Blitzer, William J, Binder
openaire   +2 more sources

The evolution of botulinum neurotoxin type A for cosmetic applications

Journal of Cosmetic and Laser Therapy, 2007
Very few pharmaceutical preparations share an evolutionary history as remarkable as that of botulinum neurotoxin (BoNT). The exotoxin of the organism Clostridium botulinum, once feared as a terrible poison, has been reborn as a highly regarded and widely used therapeutic and aesthetic agent.
Jean, Carruthers, Alastair, Carruthers
openaire   +2 more sources

Proteolysis of synthetic peptides by type A botulinum neurotoxin

Journal of Protein Chemistry, 1995
Type A botulinum neurotoxin catalyzed the hydrolysis of synthetic peptides based on the sequence of the 25-kD synaptosomal protein SNAP-25. In each peptide, the toxin cleaved at a single glutaminyl-arginine bond corresponding to residues 197 and 198 of SNAP-25, confirming earlier reports on the enzymatic specificity of the toxin in synaptosomal ...
J J, Schmidt, K A, Bostian
openaire   +2 more sources

Effects of purification on the bioavailability of botulinum neurotoxin type A

Toxicology, 2008
Botulinum neurotoxins (BoNTs) are among the most potent biological toxins for humans. They are primarily produced by the gram-positive, anaerobic spore-forming bacterium, Clostridium botulinum. In bacterial cultures, secreted BoNTs are associated with non-toxic accessory proteins forming large complexes.
Luisa W, Cheng, Bruce, Onisko, Eric A, Johnson, J Rachel, Reader, Stephen M, Griffey, Ann E, Larson, William H, Tepp, Larry H, Stanker, David L, Brandon, J Mark, Carter   +9 more
openaire   +2 more sources

The use of botulinum neurotoxin type A (BoNTA) in urology

Journal of Neural Transmission, 2008
The use of Botulinum neurotoxin type A (BoNT/A) in the lower urinary tract was pioneered as early as 20 years ago with injections into the urethral sphincter reducing bladder voiding pressures, urethral pressures, and post-void residual urine. Over the past 9 years, the use of BoNT/A has revolutionised the treatment of intractable symptoms associated ...
A, Apostolidis, C J, Fowler
openaire   +2 more sources