Zobrazeno 1 - 10
of 30
pro vyhledávání: '"A A, Laminet"'
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
Autor:
Sabine E. Axmann, Axel A. Laminet, Andreas Plückthun, Ernst Jaeger, Karl-Peter Rücknagel, Ralph Zahn
Publikováno v:
Journal of Molecular Biology. 242:150-184
From equilibrium measurements with urea we found a three-state thermodynamic and kinetic folding behavior for the precursor and mature form of Escherichia coli β-lactamase TEM2. The thermodynamic intermediate H of Escherichia coli β-lactamase and i
Publikováno v:
The Journal of biological chemistry. 271(1)
The phosphotyrosine binding (PTB) domain specifically binds to tyrosine-phosphorylated proteins, but differs in structure and mechanism of action from the SH2 domain family. We quantitated the affinity, specificity, and kinetics of the interaction of
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
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
Publikováno v:
Journal of molecular biology. 242(2)
From equilibrium measurements with urea we found a three-state thermodynamic and kinetic folding behavior for the precursor and mature form of Escherichia coli beta-lactamase TEM2. The thermodynamic intermediate H of Escherichia coli beta-lactamase a
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')
Publikováno v:
Molecular microbiology. 5(1)
The rate of folding of the precursor of beta-lactamase is not influenced by the presence of SecB under conditions in which GroEL/ES retards the folding. Wild-type beta-lactamase and several mutants in the signal or the mature protein, affecting eithe