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.
Jiwei Qi - West Roxbury MA, US Yihan Wang - Newton MA, US Feng Li - Winchester MA, US William C. Shakespeare - Southborough MA, US Anna Kohlmann - Winchster MA, US David C. Dalgarno - Brookline MA, US Xiaotian Zhu - Newton MA, US
Yihan Wang - Newton MA, US Wei-Sheng Huang - Acton MA, US Shuangying Liu - Wellesley MA, US William C. Shakespeare - Southborough MA, US R. Mathew Thomas - Sharon MA, US Jiwei Qi - West Roxbury MA, US Feng Li - Winchester MA, US Xiaotian Zhu - Newton MA, US Anna Kohlmann - Winchester MA, US David C. Dalgarno - Brookline MA, US Jan Antoinette C. Romero - Somerville MA, US Dong Zou - Concord MA, US
The present invention provides a method of generating megakaryocytes and platelets. In various embodiments, method involves the use of human embryonic stem cell derived hemangioblasts for differentiation into megakaryocytes and platelets under serum and stromal-free condition. In this system, hESCs are directed towards megakaryocytes through embryoid body formation and hemangioblast differentiation. Further provided is a method of treating a subject in need of platelet transfusion.
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
Jun 2013 to 2000 Senior Algorithm EngineerMitsubishi Electric Research Labs Cambridge, MA Nov 2011 to Jun 2013 Adjunct Member Research ScientistUniversity of Delaware Newark, DE Aug 2006 to Oct 2011 Research AssistantMitsubishi Electric Research Labs Cambridge, MA Jun 2011 to Aug 2011 Research InternThomson Corporate Research Princeton, NJ Feb 2009 to May 2009 Research Intern, TechnicolorMicrosoft Research Asia
Jul 2008 to Oct 2008 Research InternPacific Research & Development Ltd
Apr 2006 to Jul 2006 Technical Marketing Engineer, Intel AsiaIntel China Software Center
Sep 2005 to Mar 2006 Software Engineering Intern
Education:
University of Delaware Newark, DE Sep 2011 Ph.D. in Computer ScienceShanghai Jiao Tong University Mar 2006 M.EFuzhou University Jul 2003 B.E. in Electrical Engineering
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
Feng Li
Lived:
Cambridge, MA Jiaozuo,China Fuzhou,China Shanghai, China Beijing, China Newark, DE