Zobrazeno 1 - 6
of 6
pro vyhledávání: '"Françoise Levinthal"'
Publikováno v:
Science. 259:960-963
To investigate the mechanism of interaction of the toxin colicin E1 with membranes, three cysteine substitution mutants and the wild type of the channel-forming fragment were spin labeled at the unique thiol. Time-resolved interaction of these labele
Publikováno v:
Proteins: Structure, Function, and Bioinformatics. 11:254-262
The molecularity of the ion channel formed by peptide fragments of colicin has taken on particular significance since the length of the active peptide has been shown to be less than 90 amino acids and the lumen size at least 8 A. Cell survival experi
Publikováno v:
Neuron. 1:367-376
To search for genes involved in determining the morphology of individual neuronal types, a cDNA library was constructed from postnatal day 13 mouse cerebellum. From this library, 2 clones, L7 and L19, were isolated by a differential hybridization pro
Publikováno v:
Proteins: Structure, Function, and Genetics. 6:294-305
Colicin E1 is an E. coli plasmid-encoded water-soluble protein that spontaneously inserts into lipid membranes to form a voltage-gated ion channel. We have employed a novel approach in which site-directed mutagenesis is used to provide highly specifi
Publikováno v:
Cold Spring Harbor symposia on quantitative biology. 40
Autor:
Qian Liu, Cyrus Levinthal, Françoise Levinthal, Stephen L. Slatin, V. Crozel, Alan Finkelstein
Publikováno v:
Proteins. 1(3)
Cleavage of colicin E1 molecules with a variety of proteases or with cyanogen bromide (CNBr) generates COOH-terminal fragments which have channel-forming activity similar to that of intact colicin in planar lipid bilayer membranes. The smallest chann