DR. STANLEY B. PRUSINER, M.D.
Psychiatric in San Francisco, CA

6517855, Feb 11, 2003

Sep 19, 2001

09/956705

Stanley B. Prusiner - San Francisco CA
Surachai Supattapone - San Francisco CA
Michael R. Scott - San Francisco CA

The Regents of the University of California - Oakland CA

A01N 2508

424408, 424 7808, 424 7818, 424 7827, 424 7835, 424456, 424DIG 16, 514578, 523105, 523122, 525410, 525419, 528363

A method of sterilizing objects as well as the sterilized objects obtained from the method are disclosed. The method involves contacting an object such as a medical device to be reused with polycationic dendrimer under conditions which result in rendering a conformationally altered protein (e. g. a prion) non-infectious. A disinfecting agent or surgical scrub composition which comprises the dendrimers is also disclosed as are gelatin capsules treated with polycationic dendrimers.

6767712, Jul 27, 2004

Jun 28, 2001

09/895963

Stanley B. Prusiner - San Francisco CA
Carsten Korth - San Francisco CA

The Regents of the University of California - Oakland CA

G01N 33574

435 723, 435325, 435455, 4353201

The present invention provides a novel PrP protein, and nucleic acids encoding this protein, where the PrP protein is characterized in vivo by 1) incomplete glycosylation relative to glycosylation of wild-type PrP and 2) proper cellular localization, i. e. an ability to be transported to the cell surface. This novel, under-glycosylated PrP, unlike its normal cellular counterpart, can easily be converted into a protease-resistant isoform by incubation with infectious prions. The invention further provides systems for the study of prion disorders and methods of using these systems, e. g. the study of the mechanical processes in progression of prion-mediated disease or the identification of new therapeutic agents for treatment of prion-mediated disorders. In such systems, protease-resistant under-glycosylated PrP is generated de novo and can be detected by standard immunoblot techniques.

6214565, Apr 10, 2001

Oct 9, 1998

9/169574

Stanley B. Prusiner - San Francisco CA
Jiri G. Safar - Concord CA

The Regents of the University of California - Oakland CA

G01N 3353, G01N 33567, C12P 2104, A61K 4900, C07K 1600

435 71

An assay method is disclosed which isolates and detects the presence of a disease related conformation of a protein (e. g. , PrP. sup. Sc) present in a sample also containing the non-disease related conformation of the protein (e. g. , PrP. sup. C). The sample is treated (e. g. , contacted with protease) in a manner which hydrolyzes the disease related conformation and not the non-disease related conformation. The treated sample is contacted with a binding partner (e. g. , a labeled antibody which binds PrP. sup. Sc) and the occurrence of binding provides and indication that PrP. sup. Sc is present. Alternatively the PrP. sup. Sc of the treated sample is denatured (e. g. , contacted with guanadine) or unfolded. The unfolded PrP. sup. Sc is contacted with a binding partner and the occurrence of binding indicates the presence of PrP. sup.

2006000, Jan 12, 2006

Jun 20, 2005

11/157488

Stanley Prusiner - San Francisco CA, US

A01N 25/00, A01N 37/00

424405000, 514553000

The invention comprises a formulation and a method which uses the formulation. The formulation is comprised of an aqueous or alcohol solvent having therein (1) a detergent such as SDS; (2) a weak acid such as acetic acid; and (3) a chemical modification reagent such as hydrogen peroxide. The formulation can be modified to substitute other detergents for the SDS, other acids for the acetic acid and other oxidants for the peroxide provided the substitute results in a total formulation which completely inactivates the infectivity of infectious proteins such as prions in a relatively short period of time (e.g. less than two hours) and under relatively mild temperatures (e.g. 60° C. or less).

5789655, Aug 4, 1998

Jun 6, 1996

8/660626

Stanley B. Prusiner - San Francisco CA
Glenn C. Telling - San Francisco CA
Fred E. Cohen - San Francisco CA
Michael R. Scott - San Francisco CA

The Regents of the University of California - Alameda CA

C12N 1500, A61K 4900

800 2

DNA constructs are provided of epitope-tagged proteins or protein fragments which are conveniently purified with immunoaffinity chromatography such as epitope-tagged prion proteins (PrP). Transgenic animals expressing an epitope-tagged protein are provided, including transgenic animals expressing epitope-tagged PrP. Methods for distinguishing between the conformational shapes of a protein and a convenient method for isolating a tagged protein by immunoaffinity chromatographic methods are provided.

2004005, Mar 18, 2004

Aug 14, 2003

10/641663

Stanley Prusiner - San Francisco CA, US
Jiri Safar - Walnut Creek CA, US

The Regents of the University of California

G01N033/53

435/007100

The present invention provides assays for identifying the levels of both protease sensitive and protease resistant conformers of PrPin a sample. In a preferred embodiment, the assay comprises determining levels of total PrPin a sample, subjecting the PrPfraction to treatment with a protease that selectively hydrolyzes the protease sensitive PrP(sPrP) conformers, and quantifying the levels of sPrPin the sample. The ability to detect sPrPallows early detection of prions, since the PrPin easily accessible biological samples such as blood is predominantly sPrP. The ratio of sPrPto rPrPalso allows the identification of a particular prion strain in an infected sample.

7151000, Dec 19, 2006

Apr 28, 2003

10/425129

Stanley B. Prusiner - San Francisco CA, US
Jiri G. Safar - Walnut Creek CA, US

The Regents of the University of California - Oakland CA

G01N 33/539

436539, 435 71, 4351739, 4352872, 435962, 436971, 436518, 436524, 436528, 436536, 436538, 436166, 436174, 436177, 436 16, 436 17

A sample is prepared from blood in a manner which makes it possible to further analyze proteins in the sample, e. g. to detect prions in the sample. Blood is extracted, allowed to clot and subjected to separation processing (e. g. centrifugation) to obtain serum. The serum is treated with a complexing agent which agent binds prions in the sample forming an agent/protein complex which makes it possible to concentrate the complex. Concentration of the complex results in a sample which can be successfully analyzed, e. g. assayed using a range of different types of assay methodologies for detecting prions.

2006023, Oct 26, 2006

May 22, 2006

11/419688

Stanley Prusiner - San Francisco CA, US
Jiri Safar - Walnut Creek CA, US
R. Williamson - San Diego CA, US
Dennis Burton - La Jolla CA, US

A61K 39/395, A61K 39/12

424130100, 424204100

The present invention provides antibodies that specifically bind with a high degree of binding affinity to a native ungulate PrPand/or a denatured ungulate PrP, but not to a native ungulate PrP. Preferred antibodies find native bovine PrPand treated PrPbut not native bovine PrPand can be used in an assay to determine if a sample is infected with infectious prions, i.e. PrP.

6221614, Apr 24, 2001

Jan 20, 1999

9/235372

Stanley B. Prusiner - San Francisco CA
Jiri G. Safar - Concord CA

The Regents of the University of California - Oakland CA

G01N 3353

435 71

Devices such as flow through columns, substrates such as spherical polymer beads, and methods of using such to remove prions from any liquid sample are disclosed. A surface of a substrate is coated with a prion complexing agent, such as a salt of phosphotungstic acid. Blood or plasma passing through a column containing beads coated with prion complexing agent are rendered prion free.