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Akademický článek

Automated System for Multiplexing Detection of COVID-19 and Other Respiratory Pathogens

Autor: Parker Y. L. Tsang, Sunny L. H. Chu, Libby C. W. Li, Deborah M. S. Tai, Berry K. C. Cheung, Firaol Tamiru Kebede, Pete Y. M. Leung, Winston Wong, Teresa Chung, Cyril C. Y. Yip, Rosana W. S. Poon, Jonathan H. K. Chen, Kwok-Yung Yuen, Manson Fok, Johnson Y. N. Lau, Lok-Ting Lau

Publikováno v: IEEE Journal of Translational Engineering in Health and Medicine, Vol 11, Pp 424-434 (2023)

Objective: Infectious diseases are global health challenge, impacted the communities worldwide particularly in the midst of COVID-19 pandemic. The need of rapid and accurate automated systems for detecting pathogens of concern has always been critica

Externí odkaz: https://doaj.org/article/ab49848d365b40c1acc7f1501b289d13

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Radiometal labeling of recombinant proteins by a genetically engineered minimal chelation site: technetium-99m coordination by single-chain Fv antibody fusion proteins through a C-terminal cysteinyl peptide

Autor: F Jamar, M S Tai, Louis M. Weiner, L L Houston, A. M. Peters, Hermann Oppermann, G P Adams, B T Heelan, Andrew J.T. George, John E. McCartney

Publikováno v: Proceedings of the National Academy of Sciences. 92:8358-8362

We describe a method to facilitate radioimaging with technetium-99m (99mTc) by genetic incorporation of a 99mTc chelation site in recombinant single-chain Fv (sFv) antibody proteins. This method relies on fusion of the sFv C terminus with a Gly4Cys p

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::931e2f825c690cb439eb086f4b1f9b90
https://doi.org/10.1073/pnas.92.18.8358

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A bifunctional fusion protein containing Fc-binding fragment B of staphylococcal protein A amino-terminal to antidigoxin single-chain Fv

Autor: H. Oppermann, D. Levinson, James S. Huston, Gay-May Wu, M. Mudgett-Hunter, M S Tai, Edgar Haber

Publikováno v: Biochemistry. 29:8024-8030

A bifunctional molecule was genetically engineered which contained an amino-terminal effector domain that bound immunoglobulin Fc (fragment B of staphylococcal protein A) and a carboxyl-terminal domain that bound digoxin [a single-chain Fv (sFv)]. Ef

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::aefd9602434424299a5d647c0b51f989
https://doi.org/10.1021/bi00487a005

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Targeting c-erbB-2 expressing tumors using single-chain Fv monomers and dimers

Autor: M S, Tai, J E, McCartney, G P, Adams, D, Jin, R M, Hudziak, H, Oppermann, A A, Laminet, M A, Bookman, E J, Wolf, S, Liu

Publikováno v: Cancer research. 55

Single-chain Fv proteins containing a COOH-terminal cysteine (sFv') were constructed by using an antidigoxin 26.10 sFv and an anti-c-erbB-2 741F8 sFv. The fully active sFv' proteins were prepared by expression in Escherichia coli as insoluble inclusi

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::e983a758fc8e13e9dff312237efdd7fc
https://pubmed.ncbi.nlm.nih.gov/7493381

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Engineering disulfide-linked single-chain Fv dimers [(sFv')2] with improved solution and targeting properties: anti-digoxin 26-10 (sFv')2 and anti-c-erbB-2 741F8 (sFv')2 made by protein folding and bonded through C-terminal cysteinyl peptides

Autor: J E, McCartney, M S, Tai, R M, Hudziak, G P, Adams, L M, Weiner, D, Jin, W F, Stafford, S, Liu, M A, Bookman, A A, Laminet

Publikováno v: Protein engineering. 8(3)

Single-chain Fv fusions with C-terminal cysteinyl peptides (sFv') have been engineered using model sFv proteins based upon the 26-10 anti-digoxin IgG and 741F8 anti-c-erbB-2 IgG monoclonal antibodies. As part of the 741F8 sFv construction process, th

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::47bbe486436e833fbf852c1e8d0b85ad
https://pubmed.ncbi.nlm.nih.gov/7479692

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Highly specific in vivo tumor targeting by monovalent and divalent forms of 741F8 anti-c-erbB-2 single-chain Fv

Autor: G P, Adams, J E, McCartney, M S, Tai, H, Oppermann, J S, Huston, W F, Stafford, M A, Bookman, I, Fand, L L, Houston, L M, Weiner

Publikováno v: Cancer research. 53(17)

The in vivo properties of monovalent and divalent single-chain Fv (sFv)-based molecules with the specificity of the anti-c-erbB-2 monoclonal antibody 741F8 were examined in scid mice bearing SK-OV-3 tumor xenografts. 741F8 sFv monomers exhibited rapi

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::db6d20caa7d02368c0dfdd1220d76de1
https://pubmed.ncbi.nlm.nih.gov/7689421

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