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Francis Kajumo

Researcher at Albert Einstein College of Medicine

Publications -  15
Citations -  2715

Francis Kajumo is an academic researcher from Albert Einstein College of Medicine. The author has contributed to research in topics: Viral entry & Coreceptor activity. The author has an hindex of 14, co-authored 15 publications receiving 2650 citations. Previous affiliations of Francis Kajumo include Aaron Diamond AIDS Research Center.

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A Recombinant Human Immunodeficiency Virus Type 1 Envelope Glycoprotein Complex Stabilized by an Intermolecular Disulfide Bond between the gp120 and gp41 Subunits Is an Antigenic Mimic of the Trimeric Virion-Associated Structure

TL;DR: A disulfide bond is introduced between the C-terminal region of gp120 and the immunodominant segment of the gp41 ectodomain, producing a properly folded envelope glycoprotein complex which has antigenic properties which resemble those of the virion-associated complex.
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A binding pocket for a small molecule inhibitor of HIV-1 entry within the transmembrane helices of CCR5

TL;DR: HIV-1 entry into CD4(+) cells requires the sequential interactions of the viral envelope glycoproteins with CD4 and a coreceptor such as the chemokine receptors CCR5 and CXCR4 to be blocked, and the TAK-779 molecule is explored.
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CD81 is an entry coreceptor for hepatitis C virus.

TL;DR: Results indicate that CD81 functions as a post-attachment entry coreceptor and that other cellular factors act in concert with CD81 to mediate HCV binding and entry into hepatocytes.
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Differential Inhibition of Human Immunodeficiency Virus Type 1 Fusion, gp120 Binding, and CC-Chemokine Activity by Monoclonal Antibodies to CCR5

TL;DR: Surprisingly, there was no correlation between the ability of a MAb to inhibit HIV-1 fusion-entry and its ability to inhibit either the binding of a gp120-soluble CD4 complex to CCR5 or CC-chemokine activity.
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Amino-Terminal Substitutions in the CCR5 Coreceptor Impair gp120 Binding and Human Immunodeficiency Virus Type 1 Entry

TL;DR: It is shown that substitutions of the negatively charged aspartic acid residues at positions 2 and 11 and a glutamic acid residue at position 18 (E18A), individually or in combination, impair or abolish CCR5-mediated HIV-1 entry for the ADA and JR-FL M-tropic strains and the DH123 dual- Tropic strain.