Zobrazeno 1 - 10
of 14
pro vyhledávání: '"Stefano Bonissone"'
Autor:
Elaine C. Chen, Pavlo Gilchuk, Seth J. Zost, Philipp A. Ilinykh, Elad Binshtein, Kai Huang, Luke Myers, Stefano Bonissone, Samuel Day, Chandrahaas R. Kona, Andrew Trivette, Joseph X. Reidy, Rachel E. Sutton, Christopher Gainza, Summer Diaz, Jazmean K. Williams, Christopher N. Selverian, Edgar Davidson, Erica Ollmann Saphire, Benjamin J. Doranz, Natalie Castellana, Alexander Bukreyev, Robert H. Carnahan, James E. Crowe, Jr.
Publikováno v:
Cell Reports, Vol 42, Iss 4, Pp 112370- (2023)
Summary: Understanding the human antibody response to emerging viral pathogens is key to epidemic preparedness. As the size of the B cell response to a pathogenic-virus-protective antigen is poorly defined, we perform deep paired heavy- and light-cha
Externí odkaz:
https://doaj.org/article/bf9215d14449450b85f7bee1f2faf9da
Autor:
Samuel H. Payne, Stefano Bonissone, Si Wu, Roslyn N. Brown, Dmitry N. Ivankov, Dmitrij Frishman, Ljiljana Paša-Tolić, Richard D. Smith, Pavel A. Pevzner
Publikováno v:
mBio, Vol 3, Iss 6 (2012)
ABSTRACT Signal peptides are a cornerstone mechanism for cellular protein localization, yet until now experimental determination of signal peptides has come from only a narrow taxonomic sampling. As a result, the dominant view is that Sec-cleaved sig
Externí odkaz:
https://doaj.org/article/d97b16dedef64b4e89c86a8a1c5f39b4
Autor:
Elaine C. Chen, Pavlo Gilchuk, Seth J. Zost, Philipp A. Ilinykh, Elad Binshtein, Kai Huang, Luke Myers, Stefano Bonissone, Samuel Day, Chandrahaas R. Kona, Andrew Trivette, Joseph X. Reidy, Rachel E. Sutton, Christopher Gainza, Summer Monroig, Edgar Davidson, Erica Ollmann Saphire, Benjamin J. Doranz, Natalie Castellana, Alexander Bukreyev, Robert H. Carnahan, James E. Crowe
SUMMARYUnderstanding the human antibody response to emerging viral pathogens is key to epidemic preparedness. As the size of the B cell response to a pathogenic virus protective antigen is undefined, we performed deep paired heavy and light chain seq
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::4c031083e2c67b85af42a3d437ac6fcd
https://doi.org/10.1101/2022.01.12.476089
https://doi.org/10.1101/2022.01.12.476089
Autor:
Piotr Deszyński, Konrad Krawczyk, Stefano Bonissone, Igor Jaszczyszyn, Adam Volanakis, Jakub Młokosiewicz, Natalie Castellana, Rajkumar Ganesan
Publikováno v:
Nucleic Acids Research
Nanobodies, a subclass of antibodies found in camelids, are versatile molecular binding scaffolds composed of a single polypeptide chain. The small size of nanobodies bestows multiple therapeutic advantages (stability, tumor penetration) with the fir
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::49443003512c84806959babf7d6c4507
https://pubmed.ncbi.nlm.nih.gov/34747487
https://pubmed.ncbi.nlm.nih.gov/34747487
Autor:
Jakub Młokosiewicz, Rajkumar Ganesan, Piotr Deszyński, Stefano Bonissone, Igor Jaszczyszyn, Adam Volanakis, Konrad Krawczyk, Natalie Castellana
Nanobodies, a subclass of antibodies found in camelids, are a versatile molecular binding scaffold composed of a single polypeptide chain. The small size of nanobodies bestows multiple therapeutic advantages (stability, tumor penetration) with the fi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::305a6b1f156017b212aca081d4af770b
https://doi.org/10.1101/2021.08.04.21261581
https://doi.org/10.1101/2021.08.04.21261581
Autor:
Stefano Bonissone
Immunoglobulins are highly diverse, diverging from their originating germline genes driven primarily by somatic recombination and hypermutation. However, somatic gene conversion is a strong driver of immunoglobulin diversity in some species, includin
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9c3a26ca548b37ae366dae996b14d10a
Autor:
Stefano Bonissone, Pavel A. Pevzner
Publikováno v:
Journal of Computational Biology. 23:483-494
The somatic recombination of V, D, and J gene segments in B-cells introduces a great deal of diversity, and divergence from reference segments. Many recent studies of antibodies focus on the population of antibody transcripts that show which V, D, an
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9275611c19818cca9e2bc2d1c00da000
https://doi.org/10.1089/cmb.2016.0010
https://doi.org/10.1089/cmb.2016.0010
Autor:
Jeremy Stinson, Wendy N. Sandoval, Jennie R. Lill, Laura DePalatis, Pavel A. Pevzner, Eugene Kurpilyansky, Stefano Bonissone, Alla Lapidus, Ekaterina Starostina, Yana Safonova
Publikováno v:
Bioinformatics
The analysis of concentrations of circulating antibodies in serum (antibody repertoire) is a fundamental, yet poorly studied, problem in immunoinformatics. The two current approaches to the analysis of antibody repertoires [next generation sequencing
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8f9ebf24f0e417383ba0cc39be03df11
https://doi.org/10.1093/bioinformatics/btv238
https://doi.org/10.1093/bioinformatics/btv238
Publikováno v:
Molecular & Cellular Proteomics. 12:14-28
N-terminal methionine excision (NME) and N-terminal acetylation (NTA) are two of the most common protein post-translational modifications. NME is a universally conserved activity and a highly specific mechanism across all life forms. NTA is very comm
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5a17e95d1b50dd48ef176afa4204d514
https://doi.org/10.1074/mcp.m112.019075
https://doi.org/10.1074/mcp.m112.019075
Autor:
David L. Tabb, Seong Won Cha, Stefano Bonissone, Pavel A. Pevzner, Seungjin Na, Sunghee Woo, Vineet Bafna
Publikováno v:
Journal of proteome research, vol 14, iss 9
Aiming toward an improved understanding of the regulation of proteins in cancer, recent studies from the Clinical Proteomic Tumor Analysis Consortium (CPTAC) have focused on analyzing cancer tissue using proteomic technologies and workflows. Although
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5cee30ce3235421a63651fb8bf180b2d
https://pubmed.ncbi.nlm.nih.gov/26139413
https://pubmed.ncbi.nlm.nih.gov/26139413