Cell-targeted lytic pore-forming agents

Bayley, Hagen; Walker, Barbara J

Cell-targeted lytic pore-forming agents

Patent · Thu Jan 01 04:00:00 EST 1998

OSTI ID:871917

Bayley, Hagen ^[1]; Walker, Barbara J ^[2]

Grafton, MA
Auburn, MA

A chimeric compound that contains a cell-specific ligand linked to a pore-forming agent capable of lysing a cell.

View Patent

Research Organization:: Worcester Foundation

DOE Contract Number:: FG02-90ER20018

Assignee:: Worcester Foundation for Experimental Biology (Shrewsbury, MA)

Patent Number(s):: US 5824776

OSTI ID:: 871917

Country of Publication:: United States

Language:: English

References (19)

Engineered metalloregulation in enzymes Higaki, Jeffrey N.; Fletterick, Robert J.; Craik, Charles S. Trends in Biochemical Sciences, Vol. 17, Issue 3 https://doi.org/10.1016/0968-0004(92)90245-5	journal	March 1992
Primary sequence of the alpha-toxin gene from Staphylococcus aureus wood 46. Gray, G. S.; Kehoe, M. Infection and Immunity, Vol. 46, Issue 2 https://doi.org/10.1128/IAI.46.2.615-618.1984	journal	January 1984
Introduction of a Metal-dependent Regulatory Switch into an Enzyme Corey, D. R.; Schultz, P. G. Journal of Biological Chemistry, Vol. 264, Issue 7 https://doi.org/10.1016/S0021-9258(19)84902-5	journal	March 1989
Functional complementation of staphylococcal alpha-hemolysin fragments. Overlaps, nicks, and gaps in the glycine-rich loop. Walker, B.; Krishnasastry, M.; Bayley, H. Journal of Biological Chemistry, Vol. 268, Issue 7 https://doi.org/10.1016/S0021-9258(18)53531-6	journal	March 1993
Staphylococcal alpha toxin — recent advances Thelestam, Monica; Blomqvist, Lennart Toxicon, Vol. 26, Issue 1 https://doi.org/10.1016/0041-0101(88)90137-7	journal	January 1988
Functional expression of the alpha-hemolysin of Staphylococcus aureus in intact Escherichia coli and in cell lysates. Deletion of five C-terminal amino acids selectively impairs hemolytic activity. Walker, B.; Krishnasastry, M.; Zorn, L. Journal of Biological Chemistry, Vol. 267, Issue 15 https://doi.org/10.1016/S0021-9258(19)50103-X	journal	May 1992
Site-specific incorporation of novel backbone structures into proteins Ellman, J.; Mendel, D.; Schultz, P. Science, Vol. 255, Issue 5041 https://doi.org/10.1126/science.1553546	journal	January 1992
The Activation of Human Type IV Collagenase Proenzyme Stetler-Stevenson, W. G.; Krutzsch, H. C.; Wacher, M. P. Journal of Biological Chemistry, Vol. 264, Issue 3 https://doi.org/10.1016/S0021-9258(18)94193-1	journal	January 1989
Problems in the investigational study and clinical use of cancer immunotherapy Osband, Michael E.; Ross, Susan Immunology Today, Vol. 11 https://doi.org/10.1016/0167-5699(90)90080-S	journal	January 1990
Tolerogenic conjugates of xenogeneic monoclonal antibodies with monomethoxypolyethylene glycol. I. Induction of long-lasting tolerance to xenogeneic monoclonal antibodies Maiti, Pradip K.; Lang, Glen M.; Sehon, A. H. International Journal of Cancer, Vol. 41, Issue S3 https://doi.org/10.1002/ijc.2910410805	journal	January 1988
Supramolecular surfactants: Amphiphilic polymers designed to disrupt lipid membranes Regen, Steven L.; Jayasuriya, Nimal; Fabianowski, Wojciech Biochemical and Biophysical Research Communications, Vol. 159, Issue 2 https://doi.org/10.1016/0006-291X(89)90031-4	journal	March 1989
Therapeutic antibodies — the coming of age Harris, William J.; Emery, Steven Trends in Biotechnology, Vol. 11, Issue 2 https://doi.org/10.1016/0167-7799(93)90120-X	journal	February 1993
[3] Protein engineering of single-chain Fv analogs and fusion proteins Huston, James S.; Mudgett-Hunter, Meredith; Tai, Mei-Sheng Methods in Enzymology https://doi.org/10.1016/0076-6879(91)03005-2	book	January 1991
A general method for site-specific incorporation of unnatural amino acids into proteins Noren, C.; Anthony-Cahill, S.; Griffith, M. Science, Vol. 244, Issue 4901 https://doi.org/10.1126/science.2649980	journal	April 1989
Molecular design gets into a hole Amato, I. Science, Vol. 255, Issue 5045 https://doi.org/10.1126/science.1738841	journal	February 1992
Assembly of the oligomeric membrane pore formed by Staphylococcal alpha-hemolysin examined by truncation mutagenesis. Walker, B.; Krishnasastry, M.; Zorn, L. Journal of Biological Chemistry, Vol. 267, Issue 30 https://doi.org/10.1016/S0021-9258(19)36680-3	journal	October 1992
A Pore-forming protein with a protease-activated trigger Walker, Barbara; Bayley, Hagan "Protein Engineering, Design and Selection", Vol. 7, Issue 1 https://doi.org/10.1093/protein/7.1.91	journal	January 1994
Immunotoxins Pastan, Ira; Willingham, Mark C.; FitzGerald, David J. P. Cell, Vol. 47, Issue 5 https://doi.org/10.1016/0092-8674(86)90506-4	journal	December 1986
Secondary structure and assembly mechanism of an oligomeric channel protein Tobkes, Nancy; Wallace, B. A.; Bayley, Hagan Biochemistry, Vol. 24, Issue 8 https://doi.org/10.1021/bi00329a017	journal	April 1985

Similar Records

Cell-targeted lytic pore-forming agents

Patent · Wed Dec 31 23:00:00 EST 1997 · OSTI ID:871879

Cell-targeted lytic pore-forming agents

Patent · Tue Oct 20 00:00:00 EDT 1998 · OSTI ID:675830

Cell-targeted lytic pore-forming agents

Patent · Tue Oct 06 00:00:00 EDT 1998 · OSTI ID:675836

Related Subjects

/530/
agent
agent capable
agents
capable
cell
cell-specific
cell-specific ligand
cell-targeted
cell-targeted lytic
chimeric
chimeric compound
compound
contains
forming agent
ligand
ligand linked
linked
lysing
lytic
lytic pore-forming
pore-forming
pore-forming agent
pore-forming agents

Cell-targeted lytic pore-forming agents

Citation Formats

References (19)

Similar Records

Related Subjects