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Igor Bacik

Researcher at National Institutes of Health

Publications -  25
Citations -  3295

Igor Bacik is an academic researcher from National Institutes of Health. The author has contributed to research in topics: MHC class I & Antigen presentation. The author has an hindex of 22, co-authored 25 publications receiving 3243 citations. Previous affiliations of Igor Bacik include Government of the United States of America.

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A novel influenza A virus mitochondrial protein that induces cell death

TL;DR: It is proposed that PB1-F2 functions to kill host immune cells responding to influenza virus infection, and influenza viruses with targeted mutations that interfere with PB1/F2 expression induce less extensive apoptosis in human monocytic cells than those with intact PB1 -F2.
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CD4 Glycoprotein Degradation Induced by Human Immunodeficiency Virus Type 1 Vpu Protein Requires the Function of Proteasomes and the Ubiquitin-Conjugating Pathway

TL;DR: It is shown that the Vpu-induced proteolysis of nascent CD4 can be completely blocked by peptide aldehydes that act as competitive inhibitors of proteasome function and also by lactacystin, which blocks proteasomes activity by covalently binding to the catalytic β subunits of prote asomes.
Journal Article

Antigen processing in vivo and the elicitation of primary CTL responses.

TL;DR: In every circumstance examined, targeting peptides to the ER never diminished, and in some cases greatly enhanced, the TCD8+ immune response and provide an important alternative strategy in the design of live viral or naked DNA vaccines for the treatment of cancer and infectious diseases.
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Intracellular localization of proteasomal degradation of a viral antigen

TL;DR: It is demonstrated that PODs and the MTOC serve as sites of proteasomal degradation of misfolded dNP and probably cellular proteins as well, and imply that antigenic peptides are generated at one or both of these sites.
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Expression of a membrane protease enhances presentation of endogenous antigens to MHC class I-restricted T lymphocytes.

TL;DR: These findings demonstrate that a protease can influence the processing of endogenously synthesized antigens and strongly suggest that longer peptides can be transported from the cytosol to a secretory compartment where trimming of antigenic peptides to the lengths preferred by MHC class I molecules can occur if the appropriate protease is present.