Results 221 to 230 of about 89,499 (267)
Some of the next articles are maybe not open access.

Diphtheria Toxin

The Journal of Immunology, 1929
Abstract The preparation of diphtheria toxins from the time of its discovery by Behring has been repeatedly investigated with the development of many changes in its preparation, but it still presents many difficulties. The urgent need of strong potent toxins for the Ramon flocculation tests for titration of diphtheria antitoxins, and ...
openaire   +1 more source

The crystal structure of diphtheria toxin

Nature, 1992
The crystal structure of the diphtheria toxin dimer at 2.5 A resolution reveals a Y-shaped molecule of three domains. The catalytic domain, called fragment A, is of the alpha + beta type. Fragment B actually consists of two domains. The transmembrane domain consists of nine alpha-helices, two pairs of which are unusually apolar and may participate in ...
S, Choe   +6 more
openaire   +2 more sources

Diphtheria toxin (Corynebacterium diphtheriae)

1997
Abstract Diphtheria toxin is the primary virulence factor of toxigenic C. diphtheriae the etiologic agent of clinical diphtheria (Pappenheimer 1977). The structural gene for diphtheria toxin, tox, is carried by a closely related family of corynebacteriophages of which the β-phage has been the best studied (Buck et al.
openaire   +1 more source

Diphtheria Toxin Fusion Proteins

1998
Two different approaches have been undertaken to develop targeted biomolecules for therapeutics. The first was the construction of immunotoxins consisting of monoclonal antibodies chemically linked through a disulfide bond to a plant or bacterial toxin or radionuclide.
F M, Foss   +4 more
openaire   +2 more sources

Diphtheria toxin-receptor interaction: A polyphosphate-insensitive diphtheria toxin-binding domain

Biochemical and Biophysical Research Communications, 1982
Abstract Inositol hexaphosphate, and other polyphosphates, inhibit diphtheria toxin-mediated cytotoxicity by binding to the toxin at a highly cationic site called the P site and preventing toxin binding to cell surface receptors. The binding of diphtheria toxin to a solubilized cell surface glycoprotein (150,000 daltons) is also inhibited by these ...
L, Eidels, L L, Ross, D A, Hart
openaire   +2 more sources

The Effects of Inhibitors Upon Pore Formation by Diphtheria Toxin and Diphtheria Toxin T Domain

Journal of Membrane Biology, 1999
The formation of pores by membrane-inserted diphtheria toxin is closely linked to the translocation of its catalytic chain across membranes. In this report a number of aromatic polyanionic molecules were identified that inhibit toxin-induced leakage of molecules from model membrane vesicles. One inhibitor, Cibacron blue, totally blocked pore formation.
J C, Sharpe, K, Kachel, E, London
openaire   +2 more sources

Iron and Diphtheria Toxin Production

1975
The extreme sensitivity of diphtheria toxin production to the iron concentration of the medium was clearly shown by Pappenheimer and Johnson [1]. Iron level of the medium, therefore, has to be carefully controlled whether diphtheria toxin is produced using a surface or a submerged culture.
S V, Gadre, S S, Rao
openaire   +2 more sources

New Form of Diphtheria Toxin

Nature, 1968
ULTRACENTRIFUGAL studies have shown that purified diphtheria toxin is a single protein with a molecular weight of 64,500 and an S20, w of 4.2 (ref. 1). In this communication, I report experiments with a sample of toxin that contains the 4.2 S molecule, and an unusual species with a higher sedimentation constant.
openaire   +2 more sources

Diphtheria toxin

Cold Spring Harbor Protocols, 2006
Diana Marra Oram, Randall K. Holmes
  +4 more sources

The Diphtheria Toxin Structural Gene

1985
While there was considerable indirect evidence that toxinogenesis in Corynebacterium diphtheria was related to lysogeny (FREEMAN 1951; FREEMAN AND MORSE 1952; GROMAN 1953 a, b, 1955; GROMAN and EATON 1955; HOLMES and BARKSDALE 1969), it was not until the report of UCHIDA et al.
openaire   +2 more sources

Home - About - Disclaimer - Privacy