Feng Li

7537765, May 26, 2009

May 24, 2004

10/851637

Karl Salzwedel - Olney MD, US
Feng Li - Gaithersburg MD, US
Carl T. Wild - Gaithersburg MD, US
Graham P. Allaway - Darnestown MD, US
Eric O. Freed - Frederick MD, US

Panacos Pharmaceuticals, Inc. - Gaithersburg MD
The United States of America as represented by the Department of Health and Human Services - Washington DC

A61K 39/00
A61K 39/12
A61K 39/21
A61K 38/00

4241841, 530300, 4241861, 4241871, 4241881

Inhibition of HIV-1 replication by disrupting the processing of the viral Gag capsid (CA) protein (p24) from the CA-spacer peptide 1 (SP1) protein precursor (p25) is disclosed. Amino acid sequences containing a mutation in the Gag p25 protein, with the mutation resulting in a decrease in the inhibition of processing of p25 to p24 by dimethylsuccinyl betulinic acid or dimethylsuccinyl betulin, polynucleotides encoding such mutated sequences and antibodies that selectively bind such mutated sequences are also included. Methods of inhibiting, inhibitory compounds and methods of discovering inhibitory compounds that target proteolytic processing of the HIV Gag protein are included. In one embodiment, such compounds inhibit the interaction of the HIV protease enzyme with Gag by binding to Gag rather than to the protease enzyme. In another embodiment, viruses or recombinant proteins that contain mutations in the region of the Gag proteolytic cleavage site can be used in screening assays to identify compounds that target proteolytic processing.

8318425, Nov 27, 2012

Jul 6, 2009

12/498157

Karl Salzwedel - Olney MD, US
Feng Li - Brookings SD, US
Carl T. Wild - Gaithersburg MD, US
Graham P. Allaway - Darnestown MD, US
Eric O. Freed - Frederick MD, US

The United States of America, as represented by the Secretary, Department & Human Services - Washington DC
Myrexis, Inc. - Salt Lake City UT

C12Q 1/70
C12Q 1/68
A01N 61/00
A01N 57/00
A61K 31/00
A61K 31/66

435 61, 435 5, 435 611, 435 612, 514 1, 514120, 514510

Inhibition of HIV-1 replication by disrupting the processing of the viral Gag capsid (CA) protein (p24) from the CA-spacer peptide 1 (SP1) protein precursor (p25) is disclosed. Amino acid sequences containing a mutation in the Gag p25 protein, with the mutation resulting in a decrease in the inhibition of processing of p25 to p24 by dimethylsuccinyl betulinic acid or dimethylsuccinyl betulin, polynucleotides encoding such mutated sequences and antibodies that selectively bind such mutated sequences are also included. Methods of inhibiting, inhibitory compounds and methods of discovering inhibitory compounds that target proteolytic processing of the HIV Gag protein are included. In one embodiment, such compounds inhibit the interaction of the HIV protease enzyme with Gag by binding to the Gag proteolytic cleavage site rather than to the protease enzyme. In another embodiment, viruses or recombinant proteins that contain mutations in the region of the Gag proteolytic cleavage site can be used in screening assays to identify compounds that target proteolytic processing.

20040265320, Dec 30, 2004

Jan 29, 2004

10/766528

Karl Salzwedel - Olney MD, US
Feng Li - Gaithersburg MD, US
Carl Wild - Gaithersburg MD, US
Graham Allaway - Darnestown MD, US
Eric Freed - Frederick MD, US

A61K039/42

424/160100

Inhibition of HIV-1 replication by disrupting the processing of the viral Gag capsid (CA) protein (p24) from the CA-spacer peptide 1 (SP1) protein precursor (p25) is disclosed. Amino acid sequences containing a mutation in the Gag p25 protein, with the mutation resulting in a decrease in the inhibition of processing of p25 to p24 by dimethylsuccinyl betulinic acid or dimethylsuccinyl betulin, polynucleotides encoding such mutated sequences and antibodies that selectively bind such mutated sequences are also included. Methods of inhibiting, inhibitory compounds and methods of discovering inhibitory compounds that target proteolytic processing of the HIV Gag protein are included. In one embodiment, such compounds inhibit the interaction of the HIV protease enzyme with Gag by binding to the Gag proteolytic cleavage site rather than to the protease enzyme. In another embodiment, viruses or recombinant proteins that contain mutations in the region of the Gag proteolytic cleavage site can be used in screening assays to identify compounds that target proteolytic processing.

20080200550, Aug 21, 2008

May 24, 2005

11/597431

Karl Salzwedel - Olney MD, US
Feng Li - Gaithersburg MD, US
Carl T. Wild - Gaithersburg MD, US
Graham P. Allaway - Darnestown MD, US
Eric O. Freed - Frederick MD, US

V.I. TECHNOLOGIES, INC. - Gaithersburg MD
THE GOV. OF US AS REP. BY THE SEC. DEP. OF HEALTH - Rockville MD

A61K 31/557

514573

Inhibition of HIV-1 replication by disrupting the processing of the viral Gag capsid (CA) protein (p24) from the CA-spacer peptide 1 (SP1) protein precursor (p25) is disclosed. Amino acid sequences containing a mutation in the Gag p25 protein, with the mutation resulting in a decrease in the inhibition of processing of p25 to p24 by dimethylsuccinyl betulinic acid or dimethylsuccinyl betulin, polynucleotides encoding such mutated sequences and antibodies that selectively bind such mutated sequences are also included. Methods of inhibiting, inhibitory compounds and methods of discovering inhibitory compounds that target proteolytic processing of the HIV Gag protein are included. In one embodiment, such compounds inhibit the interaction of the HIV protease enzyme with Gag by binding to Gag rather than to the protease enzyme. In another embodiment, viruses or recombinant proteins that contain mutations in the region of the Gag proteolytic cleavage site can be used in screening assays to identify compounds that target proteolytic processing.

20080233559, Sep 25, 2008

Dec 21, 2007

11/962315

Karl SALZWEDEL - Olney MD, US
Feng Li - Gaithersburg MD, US
Carl T. Wild - Gaithersburg MD, US
Graham P. Allaway - Darnestown MD, US
Eric O. Freed - Frederick MD, US

C12Q 1/70

435 5

Inhibition of HIV-1 replication by disrupting the processing of the viral Gag capsid (CA) protein (p24) from the CA-spacer peptide 1 (SP1) protein precursor (p25) is disclosed. Amino acid sequences containing a mutation in the Gag p25 protein, with the mutation resulting in a decrease in the inhibition of processing of p25 to p24 by dimethylsuccinyl betulinic acid or dimethylsuccinyl betulin, polynucleotides encoding such mutated sequences and antibodies that selectively bind such mutated sequences are also included. Methods of inhibiting, inhibitory compounds and methods of discovering inhibitory compounds that target proteolytic processing of the HIV Gag protein are included. In one embodiment, such compounds inhibit the interaction of the HIV protease enzyme with Gag by binding to Gag rather than to the protease enzyme. In another embodiment, viruses or recombinant proteins that contain mutations in the region of the Gag proteolytic cleavage site can be used in screening assays to identify compounds that target proteolytic processing.

20120280435, Nov 8, 2012

Nov 1, 2010

13/505739

Ou Mao - Mequon WI, US
Feng Li - Troy MI, US
On Chang - San Jose CA, US
Dania Ghantous - Walnut Creek CA, US
George Blomgren - Lakewood OH, US

Basvah, LLC - Menlo Park CA

H01B 1/08
H01M 4/04

264681, 25251915

Methods for forming a cathode active material comprise sintering flakes formed from a nickel, manganese, cobalt and lithium-containing slurry to form the cathode material having the formula LiNiMnCoO, wherein ‘x’ is a number between about 0 and 1, ‘y’ is a number between about 0 and 1, and ‘z’ is a number greater than or equal to about 0.8 and less than 1. Lithium-ion batteries having cathode active materials formed according to methods of embodiments of the invention are provided.