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
Assignee:
Panacos Pharmaceuticals, Inc. - Gaithersburg MD The United States of America as represented by the Department of Health and Human Services - Washington DC
International Classification:
A61K 39/00 A61K 39/12 A61K 39/21 A61K 38/00
US Classification:
4241841, 530300, 4241861, 4241871, 4241881
Abstract:
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.
Inhibition Of Hiv-1 Replication By Disruption Of The Processing Of The Viral Capsid-Spacer Peptide 1 Protein
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
Assignee:
The United States of America, as represented by the Secretary, Department & Human Services - Washington DC Myrexis, Inc. - Salt Lake City UT
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.
Inhibition Of Hiv-1 Replication By Disruption Of The Processing Of The Viral Capsid-Spacer Peptide 1 Protein
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
International Classification:
A61K039/42
US Classification:
424/160100
Abstract:
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.
Inhibition Of Hiv-1 Replication By Disruption Of The Processing Of The Viral Capsid-Spacer Peptide 1 Protein
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
Assignee:
V.I. TECHNOLOGIES, INC. - Gaithersburg MD THE GOV. OF US AS REP. BY THE SEC. DEP. OF HEALTH - Rockville MD
International Classification:
A61K 31/557
US Classification:
514573
Abstract:
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.
Inhibition Of Hiv-1 Replication By Disruption Of The Processing Of The Viral Capsid-Spacer Peptide 1 Protein
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
International Classification:
C12Q 1/70
US Classification:
435 5
Abstract:
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.
Compositions For Use In Identification Of Strains Of E. Coli O157:H7
James C. Hannis - Vista CA, US Feng Li - San Diego CA, US Rangarajan Sampath - San Diego CA, US Lawrence B. Blyn - Mission Viejo CA, US Steven A. Hofstadler - Vista CA, US David J. Ecker - Encinitas CA, US Mark W. Eshoo - Solana Beach CA, US
The present invention relates generally to strain typing of O157:H7, and provides methods, compositions and kits useful for this purpose when combined, for example, with molecular mass or base composition analysis.
Compositions For Use In Identification Of Streptococcus Pneumoniae
Christian Massire - Carlsbad CA, US Rachael Kreft - Pittsburgh PA, US Lawrence B. Blyn - Mission Viejo CA, US David J. Ecker - Encinitas CA, US Feng Li - San Diego CA, US Rangarajan Sampath - San Diego CA, US
Assignee:
Ibis Biosciences, Inc. - Carlsbad CA
International Classification:
C12Q 1/68 H01J 49/26
US Classification:
435 612, 435 615, 250281
Abstract:
The present invention relates generally to the identification of , such as antibiotic resistant , and provides methods, compositions, kits and systems useful for this purpose when combined, for example, with molecular mass or base composition analysis.
Compositions For Use In Identification Of Enteric Bacterial Pathogens
Sherilynn Manalili Wheeler - Encinitas CA, US James C. Hannis - Vista CA, US Feng Li - San Diego CA, US Raymond Ranken - Encinitas CA, US Lawrence B. Blyn - Mission Viejo CA, US David J. Ecker - Encinitas CA, US Steven A. Hofstadler - Vista CA, US
Assignee:
IBIS Biosciences, Inc. - Carlsbad CA
International Classification:
C12Q 1/68 C12M 1/34
US Classification:
435 611, 435 61, 435 612, 4352872
Abstract:
The present invention relates generally to identification of enteric bacterial pathogens, and provides methods, compositions and kits useful for this purpose when combined, for example, with molecular mass or base composition analysis.
2014 to 2000 Assistant ProfessorThe University of Kansas Medical Center Kansas City, KS 2012 to 2013 Research Assistant ProfessorThe University of Kansas Medical Center Kansas City, KS 2009 to 2012 Postdoctoral FellowNational Institute on Drug Abuse Bethesda, MD 2007 to 2009 Visiting FellowInstitute of Organic Chemistry Stuttgart, AR 2002 to 2007 PhD studentShanghai Institute of Materia Medica Shangahi 1999 to 2002 MS Student
Education:
Stuttgart University 2002 to 2007 PhD in ChemistryChinese Academy of Sciences 1999 to 2002 MSZhengzhou University 1995 to 1999 BS in Chemistry
Accustrata, Inc. College Park, MD Apr 2012 to Dec 2012 Accounting AssociateAccustrata, Inc. College Park, MD Feb 2012 to Mar 2012 Part-time BookkeeperEGS Electrical Group Rosemont, IL Jun 2010 to Aug 2010 Finance/Accounting Summer Internship
Education:
University of Maryland College Park, MD 2010 to 2011 M.S. of Business in AccountingUniversity of Wisconsin Stevens Point, WI 2006 to 2010 B.S. of Accounting in Accounting
Apple, Inc Bethesda, MD Dec 2010 to Apr 2013 Genius TechnicianMicrosoft/ Volt Management Corp Baltimore, MD Feb 2010 to Dec 2010 Microsoft Student Partner - MarketingRSM McGladrey/ Tax Firm Bethesda, MD Sep 2006 to Jan 2007 File Room ClerkThe Gambian Embassy Washington, DC Sep 2005 to Dec 2005 International Politics InternLuxenberg, Johnson, & Dickens, P.C Washington, DC Jun 2003 to Sep 2003 Summer Law Intern
Education:
University of Maryland Baltimore, MD Sep 2004 to May 2010 B.A. in English Literature & Political Science
Skills:
Computer Software: Apple OS X - iWork, iLife, Final Cut Pro; Microsoft Office Suite - Word, Excel, PowerPoint, Access; Internet Browsers - Bing, Internet Explorer, Mozilla Firefox, Google Chrome; Adobe Suite - Lightroom and Photoshop
Medical School Tufts University School of Medicine Graduated: 2002
Description:
Dr. Li graduated from the Tufts University School of Medicine in 2002. He works in Tyler, TX and specializes in Gastroenterology. Dr. Li is affiliated with Mother Francis Hospital.
Baidu - Sofeware Development Engineer (2011) Alstom China Technology Center - Sofeware Development Engineer (2009-2011) EMC R&D Center - Sofeware Development Engineer Intern (2008-2008)
Education:
Fudan University - Master, Computer Science, National University of Singapore - Research Assistant, Sichuan University - Computer Science
Tagline:
To be or not to be
Feng Li
Lived:
Los Angeles, Ca Bethesda, MD
Work:
Louis Vuitton - Leather Goods (2013)
Feng Li
Work:
Nanyang Technological University - PhD Student
Education:
Nanyang Technological University - Computer Engineering, Shandong University - Computer Science and Technology, Shandong Normal University - Computer Science and Technology