Osnat Rosen
Israel Institute for Biological Research
26 Papers
123 Citations
Osnat Rosen is an academic researcher from Israel Institute for Biological Research. The author has contributed to research in topics: V3 loop & Medicine. The author has an hindex of 8, co-authored 18 publications. Previous affiliations of Osnat Rosen include City University of New York & New York University.
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Papers
Epitope Mapping of Antibody–Antigen Complexes by Nuclear Magnetic Resonance Spectroscopy
Osnat Rosen,Jacob Anglister +1 more
TL;DR: This chapter discusses some of the methods used to study antibodies in complexes that exhibit a wide range of binding affinities from very weak and transient to very tight, including dynamic filtering, comparison of HSQC peaks' intensities, transverse relaxation time, measurements of (1)H-(15)N nuclear Overhauser effect (NOE) values, and measurements of T (1rho) relaxation time.
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NMR mapping of RANTES surfaces interacting with CCR5 using linked extracellular domains.
Einat Schnur,Naama Kessler,Yuri Zherdev,Eran Noah,Tali Scherf,Fa-Xiang Ding,Svetlana Rabinovich,Boris Arshava,Victoria Kurbatska,Ainars Leonciks,Alexander Tsimanis,Osnat Rosen,Fred Naider,Jacob Anglister +13 more
TL;DR: The chemical and biosynthetic approaches for linking GPCR surface regions discussed herein should be widely applicable to the investigation of interactions of extracellular segments of chemokine receptors with their respective ligands.
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Specific and Rapid SARS-CoV-2 Identification Based on LC-MS/MS Analysis
Ofir Schuster,Anat Zvi,Osnat Rosen,Hagit Achdout,Amir Ben-Shmuel,Ohad Shifman,Shmuel Yitzhaki,Orly Laskar,Liron Feldberg +8 more
- 26 Jan 2021
TL;DR: In this paper, the authors presented a novel method for SARS-CoV-2 identification based on mass spectrometry, which combines a multistep procedure for the rational down-selection of a set of reliable markers out of all optional in silico derived tryptic peptides in viral proteins, followed by monitoring of peptides derived from tryptic digests of purified proteins, cell-cultured SARS co-virus, and nasopharyngeal (NP) swab matrix spiked with the virus.
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HIV-1 peptide vaccine candidates: selecting constrained V3 peptides with highest affinity to antibody 447-52D.
B. Mester,Revital Manor,Amit Mor,Boris Arshava,Osnat Rosen,Fa-Xiang Ding,Fred Naider,Jacob Anglister +7 more
TL;DR: It is possible that constrained peptides which mimic the R5A and R5B conformations of the V3 and retain high-affinity binding to 447-52D are good candidates for eliciting a broad neutralizing antibody response similar to that of 447 -52D.
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Mimicking the structure of the V3 epitope bound to HIV-1 neutralizing antibodies.
Amit Mor,Eugenia Segal,B. Mester,Boris Arshava,Osnat Rosen,Fa-Xiang Ding,Joseph M. Russo,Amnon Dafni,Fabian Schvartzman,Tali Scherf,Fred Naider,Jacob Anglister +11 more
TL;DR: This study indicated that cyclic V3 peptides manifested significantly reduced conformational space compared to their linear homologues and that in all cases cyclic peptides exhibited cross-strand interactions suggestive of beta-hairpin-like structures, Nevertheless, the singly constrained V3-peptides retained significant flexibility and did not form an idealized beta- hairpin.
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