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Items: 32


Sequence-conserved and antibody-accessible sites in the V1V2 domain of HIV-1 gp120 envelope protein.

Shmelkov E, Grigoryan A, Krachmarov C, Abagyan R, Cardozo T.

AIDS Res Hum Retroviruses. 2014 Sep;30(9):927-31. doi: 10.1089/AID.2014.0034. Epub 2014 Aug 14.


Vaccine focusing to cross-subtype HIV-1 gp120 variable loop epitopes.

Cardozo T, Wang S, Jiang X, Kong XP, Hioe C, Krachmarov C.

Vaccine. 2014 Sep 3;32(39):4916-24. doi: 10.1016/j.vaccine.2014.07.026. Epub 2014 Jul 18.


Computational prediction of neutralization epitopes targeted by human anti-V3 HIV monoclonal antibodies.

Shmelkov E, Krachmarov C, Grigoryan AV, Pinter A, Statnikov A, Cardozo T.

PLoS One. 2014 Feb 25;9(2):e89987. doi: 10.1371/journal.pone.0089987. eCollection 2014.


Specific sequences commonly found in the V3 domain of HIV-1 subtype C isolates affect the overall conformation of native Env and induce a neutralization-resistant phenotype independent of V1/V2 masking.

Salomon A, Krachmarov C, Lai Z, Honnen W, Zingman BS, Sarlo J, Gorny MK, Zolla-Pazner S, Robinson JE, Pinter A.

Virology. 2014 Jan 5;448:363-74. doi: 10.1016/j.virol.2013.10.007. Epub 2013 Nov 12.


Resistance of Subtype C HIV-1 Strains to Anti-V3 Loop Antibodies.

Almond D, Krachmarov C, Swetnam J, Zolla-Pazner S, Cardozo T.

Adv Virol. 2012;2012:803535. doi: 10.1155/2012/803535. Epub 2012 Apr 2.


Characterization of structural features and diversity of variable-region determinants of related quaternary epitopes recognized by human and rhesus macaque monoclonal antibodies possessing unusually potent neutralizing activities.

Krachmarov C, Lai Z, Honnen WJ, Salomon A, Gorny MK, Zolla-Pazner S, Robinson J, Pinter A.

J Virol. 2011 Oct;85(20):10730-40. doi: 10.1128/JVI.00365-11. Epub 2011 Aug 10.


Structure-guided design and immunological characterization of immunogens presenting the HIV-1 gp120 V3 loop on a CTB scaffold.

Totrov M, Jiang X, Kong XP, Cohen S, Krachmarov C, Salomon A, Williams C, Seaman MS, Abagyan R, Cardozo T, Gorny MK, Wang S, Lu S, Pinter A, Zolla-Pazner S.

Virology. 2010 Sep 30;405(2):513-23. doi: 10.1016/j.virol.2010.06.027. Epub 2010 Jul 21. Erratum in: Virology. 2011 Jan 20;409(2):360. Abagyan, Ruben [added].


Cross-clade neutralizing antibodies against HIV-1 induced in rabbits by focusing the immune response on a neutralizing epitope.

Zolla-Pazner S, Cohen S, Pinter A, Krachmarov C, Wrin T, Wang S, Lu S.

Virology. 2009 Sep 15;392(1):82-93. doi: 10.1016/j.virol.2009.05.039. Epub 2009 Jul 26.


Worldwide distribution of HIV type 1 epitopes recognized by human anti-V3 monoclonal antibodies.

Cardozo T, Swetnam J, Pinter A, Krachmarov C, Nadas A, Almond D, Zolla-Pazner S.

AIDS Res Hum Retroviruses. 2009 Apr;25(4):441-50. doi: 10.1089/aid.2008.0188.


Preferential use of the VH5-51 gene segment by the human immune response to code for antibodies against the V3 domain of HIV-1.

Gorny MK, Wang XH, Williams C, Volsky B, Revesz K, Witover B, Burda S, Urbanski M, Nyambi P, Krachmarov C, Pinter A, Zolla-Pazner S, Nadas A.

Mol Immunol. 2009 Feb;46(5):917-26. doi: 10.1016/j.molimm.2008.09.005. Epub 2008 Oct 25.


Focusing the immune response on the V3 loop, a neutralizing epitope of the HIV-1 gp120 envelope.

Zolla-Pazner S, Cohen SS, Krachmarov C, Wang S, Pinter A, Lu S.

Virology. 2008 Mar 15;372(2):233-46. Epub 2007 Dec 3.


Cross-clade neutralizing activity of human anti-V3 monoclonal antibodies derived from the cells of individuals infected with non-B clades of human immunodeficiency virus type 1.

Gorny MK, Williams C, Volsky B, Revesz K, Wang XH, Burda S, Kimura T, Konings FA, NĂ¡das A, Anyangwe CA, Nyambi P, Krachmarov C, Pinter A, Zolla-Pazner S.

J Virol. 2006 Jul;80(14):6865-72.


The v3 loop is accessible on the surface of most human immunodeficiency virus type 1 primary isolates and serves as a neutralization epitope.

Gorny MK, Revesz K, Williams C, Volsky B, Louder MK, Anyangwe CA, Krachmarov C, Kayman SC, Pinter A, Nadas A, Nyambi PN, Mascola JR, Zolla-Pazner S.

J Virol. 2004 Mar;78(5):2394-404.


Human monoclonal antibodies specific for conformation-sensitive epitopes of V3 neutralize human immunodeficiency virus type 1 primary isolates from various clades.

Gorny MK, Williams C, Volsky B, Revesz K, Cohen S, Polonis VR, Honnen WJ, Kayman SC, Krachmarov C, Pinter A, Zolla-Pazner S.

J Virol. 2002 Sep;76(18):9035-45.


Efficient isolation of novel human monoclonal antibodies with neutralizing activity against HIV-1 from transgenic mice expressing human Ig loci.

He Y, Honnen WJ, Krachmarov CP, Burkhart M, Kayman SC, Corvalan J, Pinter A.

J Immunol. 2002 Jul 1;169(1):595-605.


V3-specific polyclonal antibodies affinity purified from sera of infected humans effectively neutralize primary isolates of human immunodeficiency virus type 1.

Krachmarov CP, Kayman SC, Honnen WJ, Trochev O, Pinter A.

AIDS Res Hum Retroviruses. 2001 Dec 10;17(18):1737-48.


Interaction of HIV-1 Tat with Puralpha in nuclei of human glial cells: characterization of RNA-mediated protein-protein binding.

Wortman MJ, Krachmarov CP, Kim JH, Gordon RG, Chepenik LG, Brady JN, Gallia GL, Khalili K, Johnson EM.

J Cell Biochem. 2000 Feb;77(1):65-74.


Peptide inhibitors of HIV-1 protease and viral infection of peripheral blood lymphocytes based on HIV-1 Vif.

Potash MJ, Bentsman G, Muir T, Krachmarov C, Sova P, Volsky DJ.

Proc Natl Acad Sci U S A. 1998 Nov 10;95(23):13865-8.


The single-stranded DNA binding protein, Pur-alpha, binds HIV-1 TAR RNA and activates HIV-1 transcription.

Chepenik LG, Tretiakova AP, Krachmarov CP, Johnson EM, Khalili K.

Gene. 1998 Mar 27;210(1):37-44.


Human immunodeficiency virus type 1 (HIV-1) protein Vif inhibits the activity of HIV-1 protease in bacteria and in vitro.

Kotler M, Simm M, Zhao YS, Sova P, Chao W, Ohnona SF, Roller R, Krachmarov C, Potash MJ, Volsky DJ.

J Virol. 1997 Aug;71(8):5774-81.


Cell cycle-dependent translocations of a major nucleolar phosphoprotein, B23, and some characteristics of its variants.

Zatsepina OV, Todorov IT, Philipova RN, Krachmarov CP, Trendelenburg MF, Jordan EG.

Eur J Cell Biol. 1997 May;73(1):58-70.


Activation of the JC virus Tat-responsive transcriptional control element by association of the Tat protein of human immunodeficiency virus 1 with cellular protein Pur alpha.

Krachmarov CP, Chepenik LG, Barr-Vagell S, Khalili K, Johnson EM.

Proc Natl Acad Sci U S A. 1996 Nov 26;93(24):14112-7. Erratum in: Proc Natl Acad Sci U S A 1997 Aug 19;94(17):9571.


Association of human Pur alpha with the retinoblastoma protein, Rb, regulates binding to the single-stranded DNA Pur alpha recognition element.

Johnson EM, Chen PL, Krachmarov CP, Barr SM, Kanovsky M, Ma ZW, Lee WH.

J Biol Chem. 1995 Oct 13;270(41):24352-60.


Cooperative action of cellular proteins YB-1 and Pur alpha with the tumor antigen of the human JC polyomavirus determines their interaction with the viral lytic control element.

Chen NN, Chang CF, Gallia GL, Kerr DA, Johnson EM, Krachmarov CP, Barr SM, Frisque RJ, Bollag B, Khalili K.

Proc Natl Acad Sci U S A. 1995 Feb 14;92(4):1087-91.


Association of actin with DNA and nuclear matrix from Guerin ascites tumour cells.

Valkov NI, Ivanova MI, Uscheva AA, Krachmarov CP.

Mol Cell Biochem. 1989 May 4;87(1):47-56.


Supercoils in plant DNA: nucleoid sedimentation studies.

Stoilov LM, Zlatanova JS, Vassileva AP, Ivanchenko MG, Krachmarov CP, Genchev DD.

J Cell Sci. 1988 Feb;89 ( Pt 2):243-52.


Association of DNA with the nuclear lamina in Ehrlich ascites tumor cells.

Krachmarov C, Iovcheva C, Hancock R, Dessev G.

J Cell Biochem. 1986;31(1):59-74.


Isolation and characterization of nuclear lamina from Ehrlich ascites tumor cells.

Krachmarov C, Tasheva B, Markov D, Hancock R, Dessev G.

J Cell Biochem. 1986;30(4):351-9.


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