Zobrazeno 1 - 10
of 12
pro vyhledávání: '"Michele L. Rollence"'
Autor:
James Nagle, Michele L. Rollence, Steven W. Dodd, Paul L. Hallberg, Mark S. Oelkuct, David Filpula, Timothy K. Lee
Publikováno v:
Journal of Industrial Microbiology. 14:371-376
Two single-chain antibodies were engineered and tested as novel binding proteins with specificity for immunoglobulin M. Genes for the two single-chain Fv proteins were assembled from the variable light chain cDNA and variable heavy chain cDNA of mono
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::21e0043907487a213c9405acf7b17c28
https://doi.org/10.1007/bf01569953
https://doi.org/10.1007/bf01569953
Publikováno v:
"Protein Engineering, Design and Selection". 7:1017-1026
Single-chain Fv proteins are known to aggregate and form multimeric species. We report here that these molecules represent a new class of molecular assembly, which we have termed multivalent Fvs. Each binding site in a multivalent Fv comprises the va
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::98652df86e1e9c2e93766e01d7eb5779
https://doi.org/10.1093/protein/7.8.1017
https://doi.org/10.1093/protein/7.8.1017
Autor:
Brian A. Bell, Takashi Yokota, Karl D. Hardman, Diane E. Milenic, Mare Whitlow, James F. Wood, Margaret E. Schott, David Filpula, Steven L. Hubert, Sheau-Line Feng, Michele L. Rollence, Jeffrey Schlom
Publikováno v:
"Protein Engineering, Design and Selection". 6:989-995
The effects of linker length on binding affinity and degree of aggregation have been examined in the antifluorescein 4-4-20 and anticarcinoma CC49 single-chain Fvs. Longer linkers in the antifluorescein sFvs have higher affinities for fluorescein and
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6319453d129059f78ba3b8b411e35a98
https://doi.org/10.1093/protein/6.8.989
https://doi.org/10.1093/protein/6.8.989
Autor:
Michele L. Rollence, Timothy K. Lee, Nina Z. Essig, Aniruddha Achari, David Filpula, James Nagle
Publikováno v:
ACS Symposium Series ISBN: 9780841233140
Antibody Expression and Engineering
Antibody Expression and Engineering
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::96f0a9f7b9db2f31c4db2369e535632a
https://doi.org/10.1021/bk-1995-0604.ch006
https://doi.org/10.1021/bk-1995-0604.ch006
Autor:
Malcolm A. J. Finkelman, Michele L. Rollence, Jennifer Lin Chun Liu, Marc Whitlow, W. Thomas Mueller, Lois M. Dinterman, Ziyang Zhong, Chi-Huey Wong
Publikováno v:
Journal of the American Chemical Society. 113:683-684
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::33605a31ebad9ea0efd712d0d59701f5
https://doi.org/10.1021/ja00002a051
https://doi.org/10.1021/ja00002a051
Autor:
Theodore A.G. Smith, Neeraja Idamakanti, Jennifer Marshall-Neff, Michele L. Rollence, Patrick Wright, Michele Kaloss, Laura King, Christine Mech, Lisa Dinges, William O. Iverson, Alfred D. Sherer, Judit E. Markovits, Russette M. Lyons, Michael Kaleko, Susan C. Stevenson
Publikováno v:
Human Gene Therapy; 11/20/2003, Vol. 14 Issue 17, p1595-1604, 10p
Autor:
Theodore A.G. Smith, Neeraja Idamakanti, Michele L. Rollence, Jennifer Marshall-Neff, Jin Kim, Kathy Mulgrew, Glen R. Nemerow, Michael Kaleko, Susan C. Stevenson
Publikováno v:
Human Gene Therapy; 5/20/2003, Vol. 14 Issue 8, p777-787, 11p
Autor:
Jay F. Wood, Marc Whitlow, Michael W. Pantoliano, Michele L. Rollence, Philip N. Bryan, Karl D. Hardman, Steven Witt Dodd
Publikováno v:
Biochemistry. 28:7205-7213
Six individual amino acid substitutions at separate positions in the tertiary structure of subtilisin BPN' (EC 3.4.21.14) were found to increase the stability of this enzyme, as judged by differential scanning calorimetry and decreased rates of therm
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c4d15404d0432e060efd293abbc18936
https://doi.org/10.1021/bi00444a012
https://doi.org/10.1021/bi00444a012
Publikováno v:
Critical Reviews in Biotechnology. 8:217-224
A procedure has been developed for the isolation and identification of mutants of the bacterial serine protease, subtilisin, which exhibit enhanced thermostability. The cloned subtilisin BPN' gene from Bacillus amyloliquefaciens was treated with a va
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c5c51687ba9c0285bb865d03695686cf
https://doi.org/10.3109/07388558809147558
https://doi.org/10.3109/07388558809147558
Autor:
Gary L. Gilliland, James Patrick Wood, Barry C. Finzel, Michael W. Pantoliano, Michele L. Rollence, Philip N. Brayan, Thomas L. Poulos, Andrew Howard
Publikováno v:
Proteins: Structure, Function, and Genetics. 1:326-334
A procedure has been developed for the isolation and identification of mutants in the bacterial serine protease subtilisin that exhibit enhanced thermal stability. The cloned subtilisin BPN' gene from Bacillus amyloliquefaciens was treated with bisul
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8bdef516296d7873a99876351aacad57
https://doi.org/10.1002/prot.340010406
https://doi.org/10.1002/prot.340010406