Zobrazeno 1 - 10
of 95
pro vyhledávání: '"C Roger, MacKenzie"'
Autor:
Greg Hussack, Shannon Ryan, Henk van Faassen, Martin Rossotti, C Roger MacKenzie, Jamshid Tanha
Publikováno v:
PLoS ONE, Vol 13, Iss 12, p e0208978 (2018)
An increasing number of antibody-based therapies are being considered for controlling bacterial infections, including Clostridium difficile by targeting toxins A and B. In an effort to develop novel C. difficile immunotherapeutics, we previously isol
Externí odkaz:
https://doaj.org/article/de3cc46448984acaa62e428dea5457e9
Autor:
Kevin A. Henry, C. Roger MacKenzie
Publikováno v:
Frontiers in Immunology, Vol 9 (2018)
Externí odkaz:
https://doaj.org/article/495fa56e74d84a53a935a5dde661bfac
Autor:
Kevin A. Henry, Dae Young Kim, Hiba Kandalaft, Michael J. Lowden, Qingling Yang, Joseph D. Schrag, Greg Hussack, C. Roger MacKenzie, Jamshid Tanha
Publikováno v:
Frontiers in Immunology, Vol 8 (2017)
Human autonomous VH/VL single-domain antibodies (sdAbs) are attractive therapeutic molecules, but often suffer from suboptimal stability, solubility and affinity for cognate antigens. Most commonly, human sdAbs have been isolated from in vitro displa
Externí odkaz:
https://doaj.org/article/3c66507b2be344e0b272244c72b6f273
Autor:
Greg Hussack, Toya Nath Baral, Jason Baardsnes, Henk van Faassen, Shalini Raphael, Kevin A. Henry, Jianbing Zhang, C. Roger MacKenzie
Publikováno v:
Frontiers in Immunology, Vol 8 (2017)
ABTAG is a camelid single-domain antibody (sdAb) that binds to bovine serum albumin (BSA) with low picomolar affinity. In surface plasmon resonance (SPR) analyses using BSA surfaces, bound ABTAG can be completely dissociated from the BSA surfaces at
Externí odkaz:
https://doaj.org/article/c3827df654004995833a10e4a82315bd
Autor:
Seung-Hwan Lee, Michael J. Lowden, Dong-Hyeon Jo, Shannon Ryan, Greg Hussack, Henk van Faassen, Shalini Raphael, Kevin A. Henry, C. Roger MacKenzie
Publikováno v:
Molecular Pharmaceutics. 18:2375-2384
Multispecific antibodies that bridge immune effector and tumor cells have shown promising preclinical and clinical efficacies. Here, we isolated and characterized novel llama single-domain antibodies (sdAbs) against CD16. One sdAb, NRC-sdAb048, bound
Autor:
Kevin A. Henry, Henk van Faassen, Doreen Harcus, Anne Marcil, Jennifer J. Hill, Serge Muyldermans, C. Roger MacKenzie
Publikováno v:
Immunogenetics. 75:195-195
Autor:
Frédéric, Trempe, Martin A, Rossotti, Tahir, Maqbool, C Roger, MacKenzie, Mehdi, Arbabi-Ghahroudi
Publikováno v:
Methods in molecular biology (Clifton, N.J.). 2446
Genetic immunization is a simple, cost-effective, and powerful tool for inducing innate and adaptive immune responses to combat infectious diseases and difficult-to-treat illnesses. DNA immunization is increasingly used in the generation of monoclona
Autor:
Frédéric Trempe, Martin A. Rossotti, Tahir Maqbool, C. Roger MacKenzie, Mehdi Arbabi-Ghahroudi
Publikováno v:
Methods in Molecular Biology ISBN: 9781071620748
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::1d9ad245bc8b63f464f4aa647c27fa4c
https://doi.org/10.1007/978-1-0716-2075-5_3
https://doi.org/10.1007/978-1-0716-2075-5_3
Autor:
Kevin A Henry, Traian Sulea, Henk van Faassen, Greg Hussack, Enrico O Purisima, C Roger MacKenzie, Mehdi Arbabi-Ghahroudi
Publikováno v:
PLoS ONE, Vol 11, Iss 9, p e0163113 (2016)
Staphylococcal protein A (SpA) and streptococcal protein G (SpG) affinity chromatography are the gold standards for purifying monoclonal antibodies (mAbs) in therapeutic applications. However, camelid VHH single-domain Abs (sdAbs or VHHs) are not bou
Externí odkaz:
https://doaj.org/article/2d1ae8285664432b857d78cf57c413ed
Autor:
Kevin A. Henry, Shalini Raphael, Henk van Faassen, Qingling Yang, Martin A Rossotti, Shannon Ryan, Susan Jiang, Eric Brunette, C. Roger MacKenzie, Traian Sulea, Arsalan S. Haqqani, Greg Hussack, Jamshid Tanha
Publikováno v:
The FASEB Journal. 34:8155-8171
Prolonged serum half-life is required for the efficacy of most protein therapeutics. One strategy for half-life extension is to exploit the long circulating half-life of serum albumin by incorporating a binding moiety that recognizes albumin. Here, w