Zobrazeno 1 - 10
of 17
pro vyhledávání: '"Mei-sheng Tai"'
Autor:
John E. McCartney, James S. Huston, Louis M. Weiner, Mei-Sheng Tai, L. L. Houston, Gregory P. Adams, James D. Marks, Walter F. Stafford
Publikováno v:
Clinical Cancer Research. 12:1599-1605
Radiolabeled single-chain Fv (sFv) molecules display highly specific tumor retention in the severe combined immunodeficient (SCID) mouse model; however, the absolute quantity of sFv retained in the tumors is diminished by the rapid renal elimination
Autor:
Jamie Eisenberg, John E. McCartney, Michael A. Bookman, Gregory P. Adams, E J Wolf, Walter F. Stafford, Mei-Sheng Tai, L. L. Houston, Louis M. Weiner, James S. Huston
Publikováno v:
Cancer Immunology, Immunotherapy. 40:299-306
Single-chain Fv molecules in monovalent (sFv) and divalent [(sFv')2] forms exhibit highly specific tumor targeting in mice as a result of their small size and rapid systemic clearance. As a consequence, there is a rapid reversal of the sFv blood/tumo
Autor:
John E. McCartney, Axel A. Laminet, James S. Huston, Louis M. Werner, Mei-Sheng Tai, Gregory P. Adams, Sen Liu, Josephine Schultz, Jamie Eisenberg, E J Wolf, Gerald Apell, L. L. Houston, Hermann Oppermann, Walter F. Stafford, Bruce J. Giantonio, Michael A. Bookman
Publikováno v:
International Journal of Pharmacognosy. 33:75-91
Single-chain Fv fragments (sFv) that bind tumor-associated antigens exhibit highly specific tumor targeting characteristics, based on studies of intravenous sFv administration to immunodeficient mice bearing human tumor xenografts. These features sug
Autor:
Sen Liu, Gregory P. Adams, Mei-Sheng Tai, Hermann Oppermann, Donald Jin, John E. McCartney, James S. Huston, Robert M. Hudziak, Axel A. Laminet, Irwin Fand, Michael A. Bookman, Louis M. Weiner, Walter F. Stafford, L. L. Houston
Publikováno v:
"Protein Engineering, Design and Selection". 8:301-314
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
Autor:
James S. Huston, Haimanti Dorai, Mei-Sheng Tai, Hermann Oppermann, Axel A. Laminet, John E. McCartney, L. L. Houston, Robert M. Hudziak
Publikováno v:
Nature Biotechnology. 12:890-897
The production of several single-chain Fv (sFv) antibody proteins was examined by three modes of mammalian cell expression. Our primary model was the 741F8 anti-c-erbB-2 sFv, assembled as either the VH-VL or VL-VH, and expressed alone, with C-termina
Publikováno v:
Cell Biophysics. 22:189-224
The single-chain Fv (sFv) has proven attractive for immuno-targeting, both alone and as a targeting element within sFv fusion proteins. This chapter summarizes the features of sFv proteins that have sparked this interest, starting with the conservati
Autor:
James S. Huston, Gregory P. Adams, John E. McCartney, Mei-Sheng Tai, Robert M. Hudziak, Hermann Oppermann, Walter F. Stafford, Sen Liu, Irwin Fand, Gerald Apell, Axel Laminet, Michael A. Bookman, L. L. Houston, Louis M. Weiner
Publikováno v:
Cell biophysics.
This investigation has utilized novel forms of the single-chain Fv (sFv), wherein a cysteine-containing peptide has been fused to the sFv carboxyl terminus to facilitate disulfide bonding or specific cross-linking of this sFv' to make divalent (sFv')
Autor:
Donald Jin, James S. Huston, Peter C. Keck, Hermann Oppermann, John Mccartney, Cristina Mottola-hartshorn, Mei-Sheng Tai, Frederick Warren
Publikováno v:
International reviews of immunology. 10(2-3)
A single-chain antibody or single-chain Fv (sFv) incorporates the complete antibody binding site in a single polypeptide chain of minimal size, with an approximate molecular weight of 26,000. In antibodies, the antigen combining site is part of the F
Autor:
Meredith Mudgett-Hunter, Frederick Warren, Edgar Haber, Hermann Oppermann, James S. Huston, Mei-Sheng Tai, John Mccartney
Publikováno v:
Methods in Enzymology ISBN: 9780121821043
Publisher Summary This chapter describes the minimal antibody binding site through the protein engineering of single-chain Fv analog and fusion proteins. In this approach, the genes encoding VH and VL domains of a given monoclonal antibody are connec
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::a2315b9cef81fe78eb01eb97b141c576
https://doi.org/10.1016/0076-6879(91)03005-2
https://doi.org/10.1016/0076-6879(91)03005-2
Publikováno v:
Biophysical Chemistry. 20:95-105
Ultracentrifugal analysis of ribosomal purity is complicated by the rapid reequilibration of ribosomes with their subunits, and this is further enhanced by the effects of hydrostatic pressure. Fixation of the ribosome system prior to ultracentrifugal