Zobrazeno 1 - 10
of 17
pro vyhledávání: '"Susan H. Tam"'
Autor:
Susan H. Tam, Stephen G. McCarthy, Anthony A. Armstrong, Sandeep Somani, Sheng-Jiun Wu, Xuesong Liu, Alexis Gervais, Robin Ernst, Dorina Saro, Rose Decker, Jinquan Luo, Gary L. Gilliland, Mark L. Chiu, Bernard J. Scallon
Publikováno v:
Antibodies, Vol 6, Iss 3, p 12 (2017)
Engineering of fragment crystallizable (Fc) domains of therapeutic immunoglobulin (IgG) antibodies to eliminate their immune effector functions while retaining other Fc characteristics has numerous applications, including blocking antigens on Fc gamm
Externí odkaz:
https://doaj.org/article/e4effcd57176409f88ce8c9b266a42aa
Autor:
Dennis R. Goulet, Rose Decker, Jose Pardinas, Susan H. Tam, Eva Emmell, Mark L. Chiu, Songmao Zheng, Mehabaw G. Derebe, Catherine N. Leettola, Adam Zwolak
Publikováno v:
Scientific Reports, Vol 7, Iss 1, Pp 1-11 (2017)
Scientific Reports
Scientific Reports
Methods to rapidly generate high quality bispecific antibodies (BsAb) having normal half-lives are critical for therapeutic programs. Here, we identify 3 mutations (T307P, L309Q, and Q311R or “TLQ”) in the Fc region of human IgG1 which disrupt in
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9f0a800975376ddc9448fee52cea3518
http://link.springer.com/article/10.1038/s41598-017-15748-0
http://link.springer.com/article/10.1038/s41598-017-15748-0
Autor:
Anthony A. Armstrong, Eva Emmell, Dennis R. Goulet, Songmao Zheng, Kerry Brosnan, Jose Pardinas, Jeffrey Luo, Susan H. Tam, Mark L. Chiu, Gary L. Gilliland, Adam Zwolak
Publikováno v:
mAbs
The increased number of bispecific antibodies (BsAb) under therapeutic development has resulted in a need for mouse surrogate BsAbs. Here, we describe a one-step method for generating highly pure mouse BsAbs suitable for in vitro and in vivo studies.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c8c47706163315d2d22e8a3cacbaa31f
https://doi.org/10.1080/19420862.2017.1375639
https://doi.org/10.1080/19420862.2017.1375639
Autor:
Abhinav Nath, William M. Atkins, Michael J. Watson, Dennis R. Goulet, Susan H. Tam, Mark L. Chiu, Adam Zwolak
Publikováno v:
Drug Metab Dispos
The serum half-life and clearance of therapeutic monoclonal antibodies (mAbs) are critical factors that impact their efficacy and optimal dosing regimen. The pH-dependent binding of an mAb to the neonatal Fc receptor (FcRn) has long been recognized a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6d7300d8e6dbc19da4b10f42d0aef5a2
https://pubmed.ncbi.nlm.nih.gov/30232177
https://pubmed.ncbi.nlm.nih.gov/30232177
Autor:
Dorina Saro, Susan H. Tam, Sandeep Somani, Mark L. Chiu, Bernard Scallon, Alexis Gervais, Gary L. Gilliland, Xuesong Liu, Sheng-Jiun Wu, Rose Decker, Stephen G. McCarthy, Jinquan Luo, Robin Ernst, Anthony A. Armstrong
Publikováno v:
Antibodies, Vol 6, Iss 3, p 12 (2017)
Antibodies; Volume 6; Issue 3; Pages: 12
Antibodies
Antibodies; Volume 6; Issue 3; Pages: 12
Antibodies
Engineering of fragment crystallizable (Fc) domains of therapeutic immunoglobulin (IgG) antibodies to eliminate their immune effector functions while retaining other Fc characteristics has numerous applications, including blocking antigens on Fc gamm
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4cc3a11d7bef6ec9f4eb105eae0113a1
https://pubmed.ncbi.nlm.nih.gov/31548527
https://pubmed.ncbi.nlm.nih.gov/31548527
Autor:
Bernie Scallon, Rob Perkinson, Gordon Powers, Jill Giles-Komar, Susan H Tam, Connie Kliwinski, John R. Mabus, Teresa M Wilkinson, Pamela J. Hornby, Philip R. Cooper
Publikováno v:
American Journal of Physiology-Gastrointestinal and Liver Physiology. 304:G262-G270
Immunoglobulin G (IgG) is transcytosed across intestinal epithelial cells of suckling mammals by the neonatal Fc receptor (FcRn); however, the contribution of FcRn vs. FcRn-independent uptake to serum IgG levels had not been determined in either rat
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::56fa91da0e4c109cde44755adb181364
https://doi.org/10.1152/ajpgi.00340.2012
https://doi.org/10.1152/ajpgi.00340.2012
Autor:
Stephen G. McCarthy, Anthony A. Armstrong, Gary L. Gilliland, Susan H. Tam, Jinquan Luo, Mark Chiu, Di Zhang
Publikováno v:
mAbs
Immunostimulatory receptors belonging to the tumor necrosis factor receptor (TNFR) superfamily are emerging as promising targets for cancer immunotherapies. To optimize the agonism of therapeutic antibodies to these receptors, Fc engineering of antib
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::019751e7766576ac8512acb6f3191f98
https://doi.org/10.1107/s010876731809565x
https://doi.org/10.1107/s010876731809565x
Publikováno v:
Molecular Immunology. 44:1524-1534
Although it is now clear that certain Fc glycan structures on immunoglobulin G (IgG) antibodies (Abs) can have a dramatic influence on binding to selected Fcgamma receptors (FcgammaR) and on Fc-mediated immune functions, the effects of all known Fc g
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::10361a5ada3ca7f4fb10f8dfa4f85544
https://doi.org/10.1016/j.molimm.2006.09.005
https://doi.org/10.1016/j.molimm.2006.09.005
Publikováno v:
mAbs. 5(3)
Transgenic mice expressing human neonatal Fc receptor (FcRn) instead of mouse FcRn are available for IgG antibody pharmacokinetic (PK) studies. Given the interest in a rodent model that offers reliable predictions of antibody PK in monkeys and humans
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::be365a18c8cff169cdbcfa1b61eb4e99
https://pubmed.ncbi.nlm.nih.gov/23549129
https://pubmed.ncbi.nlm.nih.gov/23549129
Structure–Function Studies on Synthetic Peptides Derived from the 109–118 Lectin Domain of Selectins
Autor:
Susan H. Tam, Miljenko Mervic, Marian T. Nakada, Alexander H. Taylor, Marian Kruszynski, George A. Heavner, William E. Fieles
Publikováno v:
Biochemical and Biophysical Research Communications. 227:712-717
Previously, we identified several peptides corresponding to amino acid sequences within the lectin domains of selectins that inhibit neutrophil (PMN) adhesion to P-selectin. Here we focused on one of the active regions, 109-118, which contains residu
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ee0c47f0fa0e28c00f416f481d46ec8d
https://doi.org/10.1006/bbrc.1996.1574
https://doi.org/10.1006/bbrc.1996.1574