I. Agostini

发表

Two nuclear localization signals in the HIV-1 matrix protein regulate nuclear import of the HIV-1 pre-integration complex.

M. Bukrinsky, S. Nadler, O. Haffar, 2000, Journal of molecular biology.

Phosphorylation of Vpr regulates HIV type 1 nuclear import and macrophage infection.

M. Bukrinsky, O. Chaika, S. Popov, 2002, AIDS research and human retroviruses.

The HIV‐1 Vpr co‐activator induces a conformational change in TFIIB

F. Rey, R. Pomerantz, B. Spire, 1999, FEBS letters.

The human immunodeficiency virus type 1 Vpr transactivator: cooperation with promoter-bound activator domains and binding to TFIIB.

F. Rey, B. Spire, I. Agostini, 1996, Journal of molecular biology.

Heat-shock protein 70 exerts opposing effects on Vpr-dependent and Vpr-independent HIV-1 replication in macrophages.

M. Bukrinsky, Yuqi Zhao, L. Dubrovsky, 2004, Blood.

A role for human immunodeficiency virus type 1 Vpr during infection of peripheral blood mononuclear cells.

F. Rey, José, B. Spire, 1998, The Journal of general virology.

Human immunodeficiency virus type 1 Vpr protein binds to the uracil DNA glycosylase DNA repair enzyme

F. Rey, S. Benichou, R. Benarous, 1996, Journal of virology.

DNA Repair Enzyme Uracil DNA Glycosylase Is Specifically Incorporated into Human Immunodeficiency Virus Type 1 Viral Particles through a Vpr-Independent Mechanism

F. Rey, I. Agostini, R. Vigne, 1999, Journal of Virology.

Heat-shock protein 70 can replace viral protein R of HIV-1 during nuclear import of the viral preintegration complex.

M. Bukrinsky, S. Popov, L. Dubrovsky, 2000, Experimental cell research.

Characterization of human immunodeficiency virus type 1 vif gene in long-term asymptomatic individuals.

H. Agut, B. Autran, I. Agostini, 2000, Virology.

Heat-shock protein 70 exerts opposing effects on Vpr-dependent and Vpr-independent HIV-1 replication in macrophages.

M. Bukrinsky, Yuqi Zhao, L. Dubrovsky, 2004, Blood.