Yossef Kliger

ORCID: 0009-0007-4441-8985
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About
Contact & Profiles
Research Areas
  • Cancer Immunotherapy and Biomarkers
  • CAR-T cell therapy research
  • Immunotherapy and Immune Responses
  • HIV Research and Treatment
  • Protein Structure and Dynamics
  • SARS-CoV-2 and COVID-19 Research
  • Virology and Viral Diseases
  • Bacteriophages and microbial interactions
  • Herpesvirus Infections and Treatments
  • Immune Cell Function and Interaction
  • Antimicrobial Peptides and Activities
  • RNA and protein synthesis mechanisms
  • Monoclonal and Polyclonal Antibodies Research
  • Cancer Genomics and Diagnostics
  • HIV/AIDS drug development and treatment
  • Machine Learning in Bioinformatics
  • Clusterin in disease pathology
  • Animal Virus Infections Studies
  • vaccines and immunoinformatics approaches
  • Ferroptosis and cancer prognosis
  • Lipid Membrane Structure and Behavior
  • Pregnancy-related medical research
  • Heat shock proteins research
  • interferon and immune responses
  • Glycosylation and Glycoproteins Research

Compugen (Israel)
2003-2024

Weizmann Institute of Science
1997-2001

The fusion domain of human immunodeficiency virus (HIV-1) envelope glycoprotein (gp120-gp41) is a conserved hydrophobic region located at the N terminus transmembrane (gp41). A V2E mutant has been shown to dominantly interfere with wild-type envelope-mediated syncytium formation and infectivity. To understand this phenomenon, 33-residue peptide (wild type, WT) identical N-terminal segment gp41 its were synthesized, fluorescently labeled, characterized. Both peptides inhibited HIV-1 cell-cell...

10.1074/jbc.272.21.13496 article EN cc-by Journal of Biological Chemistry 1997-05-01

Severe acute respiratory syndrome (SARS) is a febrile illness. The disease has been etiologically linked to novel coronavirus that named the SARS-associated (SARS-CoV), whose genome was recently sequenced. Since it member of Coronaviridae, its spike protein (S2) believed play central role in viral entry by facilitating fusion between and host cell membranes. responsible for viral-induced membrane HIV-1 (gp41) differs length, no sequence homology with S2.Sequence analysis reveals two proteins...

10.1186/1471-2180-3-20 article EN cc-by BMC Microbiology 2003-09-21

HIV-1 transmembrane envelope glycoprotein (gp41) has an unusually long cytoplasmic domain that secondary associations with the inner leaflet of membrane. Two highly amphiphatic α-helices in gp41 have previously been shown to interact lipid bilayers. We detected a conserved leucine zipper-like sequence between two α-helices. A peptide corresponding this segment (residues 789−815, LLP-3) aggregates aqueous solution, but spontaneously inserts into phospholipid membranes and dissociates...

10.1021/bi962935r article EN Biochemistry 1997-04-01

Blocking conformational changes in biologically active proteins holds therapeutic promise. Inspired by the susceptibility of viral entry to inhibition synthetic peptides that block formation helix–helix interactions envelope proteins, we developed a computational approach for predicting interacting helices. Using this approach, which combines correlated mutations analysis and Fourier transform, designed target gp96 clusterin, 2 secreted chaperones known shift between inactive conformations....

10.1073/pnas.0906514106 article EN Proceedings of the National Academy of Sciences 2009-08-06

Abstract Cancers that are poorly immune infiltrated pose a substantial challenge, with current immunotherapies yielding limited clinical success. Stem-like memory T cells (TSCM) have been identified as subgroup of possess strong proliferative capacity and can expand differentiate following interactions dendritic (DCs). In this study, we explored the pattern expression recently discovered inhibitory receptor poliovirus receptor-related immunoglobulin domain protein (PVRIG) its ligand, ligand...

10.1158/2326-6066.cir-23-0752 article EN Cancer Immunology Research 2024-05-16

In a screening effort based on algorithmic predictions for novel G‐protein‐coupled receptor (GPCR) peptide activators, we were able to identify and examine two peptides (P59 P74) which are short, linear, derived from natural, previously unidentified precursor protein containing collagen‐like repeat. Both seemed show an apparent cAMP‐related effect CHO‐K1 cells transiently transfected with either LGR7 or LGR8, usually after treatment cAMP‐generating forskolin, compared the same treated...

10.1111/j.1749-6632.2009.03827.x article EN Annals of the New York Academy of Sciences 2009-04-01

Abstract Poorly immune infiltrated cancers pose a significant challenge, with current immunotherapies yielding limited clinical success. Stem-like memory T cells (TSCM) have been identified as cell subgroup which possess enhanced proliferative capacity that could expand and differentiate upon dendritic (DCs) priming. In this study we investigated the expression of recently discovered inhibitory receptor PVRIG its ligand, PVRL2, in tumor microenvironment (TME). Leveraging single RNA...

10.1158/1538-7445.am2024-7533 article EN Cancer Research 2024-03-22

<div>Abstract<p>Cancers that are poorly immune infiltrated pose a substantial challenge, with current immunotherapies yielding limited clinical success. Stem-like memory T cells (T<sub>SCM</sub>) have been identified as subgroup of possess strong proliferative capacity and can expand differentiate following interactions dendritic (DCs). In this study, we explored the pattern expression recently discovered inhibitory receptor poliovirus receptor-related immunoglobulin...

10.1158/2326-6066.c.7311433.v1 preprint EN 2024-07-02

<div>Abstract<p>Cancers that are poorly immune infiltrated pose a substantial challenge, with current immunotherapies yielding limited clinical success. Stem-like memory T cells (T<sub>SCM</sub>) have been identified as subgroup of possess strong proliferative capacity and can expand differentiate following interactions dendritic (DCs). In this study, we explored the pattern expression recently discovered inhibitory receptor poliovirus receptor-related immunoglobulin...

10.1158/2326-6066.c.7311433 preprint EN 2024-07-02
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