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.
Ronald Montelaro - Wexford PA, US Jodi Craigo - Allian Park PA, US Feng Li - Gaithersburg MD, US
International Classification:
A61K048/00 A61K039/12 C12N007/00
US Classification:
424/199100, 424/093200, 435/235100
Abstract:
The invention provides an equine infectious anemia (EIA) vaccine and/or construct that provides immunity to mammals, especially equines, from infection with equine infectious anemia virus (EIAV) and which, in embodiments, allows differentiation between vaccinated and non-vaccinated, but exposed, mammals or equines. In various embodiments, said vaccine encompasses at least one mutation in an EIAV which produces a non-functional gene in the vaccine virus that is always expressed in disease-producing wild-type EIA viruses. Additionally, said EIA vaccine virus cannot cause clinical disease in mammals or spread or shed to other mammals including equines.
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.
Mirror Device Structure For Power Mosfet And Method Of Manufacture
A MOSFET includes a substrate having a body region of a first conductivity type. A main field effect transistor (mainFET) and a mirror device are formed in the substrate. The mainFET includes first gate trenches, first source regions of a second conductivity type adjacent to the first gate trenches, and first body implant regions of the first conductivity type extending into the body region adjacent to and interposed between the first source regions. The mirror device includes second gate trenches, second source regions of the second conductivity type adjacent to the second gate trenches, second body implant regions of the first conductivity type extending into the body region adjacent to and interposed between the second source regions, and link elements of the first conductivity type interconnecting pairs of the second body implant regions.
Mirror Device Structure For Power Mosfet And Method Of Manufacture
A MOSFET includes a substrate having a body region of a first conductivity type. A main field effect transistor (mainFET) and a mirror device are formed in the substrate. The mainFET includes first gate trenches, first source regions of a second conductivity type adjacent to the first gate trenches, and first body implant regions of the first conductivity type extending into the body region adjacent to and interposed between the first source regions. The mirror device includes second gate trenches, second source regions of the second conductivity type adjacent to the second gate trenches, second body implant regions of the first conductivity type extending into the body region adjacent to and interposed between the second source regions, and link elements of the first conductivity type interconnecting pairs of the second body implant regions.
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
University of Texas in Austin Austin, TX 2013 to 2013 Postdoctoral FellowR&D Division
2004 to 2006 Project ManagerTianjin Nankai Hecheng S&T Co. Ltd
2000 to 2001 Research Assistant
Education:
Kansas State University Manhattan, KS 2007 to 2013 PhD in Analytical ChemistryChina Agreculture University 2001 to 2004 Master's in ChemistryNankai University China, ME 1996 to 2000 BS in Chemistry
Skills:
NMR, MS, FTIR, HPLC, GC, UV-Vis, Atomic Absorption, Wet Chemistry, Hands-on knowledge in the maintenance, repairs, calibration and qualification of all applicable laboratory instruments, computer (Word, Excel) and office-related skills.
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.
Trinity Clinic - Gastroenterology
910 E Houston St, Tyler, TX 75702 Univ. Of Md Medical Group
22 S Greene St, Baltimore, MD 21263 Univ. Of Md Medical Group
419 W Redwood St, Baltimore, MD 21201
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