Zobrazeno 1 - 10
of 10
pro vyhledávání: '"Thomas L. Luntz"'
Publikováno v:
Biochemical Journal. 302:95-101
Asn-52 of rat cytochrome c and baker's yeast iso-1-cytochrome c was changed to isoleucine by site-directed mutagenesis and the mutated proteins expressed in and purified from cultures of transformed yeast. This mutation affected the affinity of the h
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9e8ccbcec50caabe9a094c996cb4311b
https://doi.org/10.1042/bj3020095
https://doi.org/10.1042/bj3020095
Publikováno v:
Protein Expression and Purification. 3:441-452
A complete protocol for the expression of recombinant cytochrome c genes from yeast, Drosophila melanogaster, and rat in a yeast strain, GM-3C-2, which does not express its own cytochromes c is described. The construction of the expression vectors, t
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::48b80d327720118ec13fedc673d22480
https://doi.org/10.1016/1046-5928(92)90061-z
https://doi.org/10.1016/1046-5928(92)90061-z
Publikováno v:
Proceedings of the National Academy of Sciences. 87:8697-8701
Drosophila melanogaster and rat cytochromes c in which proline-30 was converted to alanine or valine were expressed in a strain of baker's yeast, Saccharomyces cerevisiae, where they sustained aerobic growth. The mutations had no significant effect o
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::559a8c7b9a57bb750e85af92d67e7626
https://doi.org/10.1073/pnas.87.22.8697
https://doi.org/10.1073/pnas.87.22.8697
Autor:
Robert E. London, Arron S. L. Xu, Hiroshi Kubota, Jeffrey M. Macdonald, Lola M. Reid, Thomas L. Luntz, Edward W. Hsu
Publikováno v:
Principles of Tissue Engineering (Second Edition)
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::643c78450d0ff6803e9a941c9f7ad420
https://doi.org/10.1016/b978-012436630-5/50045-3
https://doi.org/10.1016/b978-012436630-5/50045-3
Autor:
Patrick Aebischer, Richard A. Altschuler, Pascal Ambrosini, David J. Anderson, Anthony Atala, François A. Auger, Efstathios S. Avgoustiniatos, David W. Barnes, Eugene Bell, Marie C. Béné, John G. Bishop, T. Bohrer, Lawrence J. Bonassar, Amy D. Bradshaw, Kelvin G.M. Brockbank, Leon W. Browder, Scott P. Bruder, Mary Bartlett Bunge, Arnold I. Caplan, Thomas Ming Swi Chang, Robert G. Chapman, Una Chen, Richard A.F. Clark, Réjean Cloutier, Clark K. Colton, Joanne C. Cousins, Stephen C. Cowin, Gislin Dagnelie, Thomas F. Deuel, Charles N. Durfor, Brian E. Edwards, Carol A. Erickson, Gilbert C. Faure, Denise Faustman, Dario O. Fauza, Eric G. Fine, Lee G. Fradkin, Lisa E. Freed, Claudia Gaffey, John D. Gearhart, Lucie Germain, Francine Goulet, Howard P. Greisler, Alan J. Grodzinsky, Craig R. Halberstadt, Janet Hardin-Young, C. Hasse, Matthias Hebrok, Kiki B. Hellman, Walter D. Holder, Edward Hsu, Jeffrey A. Hubbell, Mark S. Humayun, H. David Humes, Donald E. Ingber, Hugo O. Jauregui, Roger D. Kamm, Ravi S. Kane, Jens O.M. Karlsson, Anne Kessinger, Byung-Soo Kim, Naomi Kleitman, Joachim Kohn, Hiroshi Kubota, Robert P. Lanza, Douglas A. Lauffenburger, Kuen Yong Lee, Peter I. Lelkes, Robert E. London, Jack W. Love, Thomas L. Luntz, Michael J. Lysaght, Jeffrey M. Macdonald, Manuela Martins-Green, Robert W. Massof, John M. McPherson, Douglas A. Melton, Antonios G. Mikos, Josef M. Miller, Neal A. Miller, David J. Mooney, Jennifer E. Morgan, Melvin L. Moss, Claudy Mullon, Christopher S. Muratore, Gail K. Naughton, Robert M. Nerem, Björn Reino Olsen, Gregory M. Organ, James M. Pachence, Nancy L. Parenteau, Terence A. Partridge, Jacques Penaud, A. Robin Poole, Denis Rancourt, Yehoash Raphael, A.H. Reddi, Lola M. Reid, J. Dezz Ropp, Robert N. Ross, M. Rothmund, R. Bruce Rutherford, E. Helene Sage, Jacqueline Sagen, W. Mark Saltzman, Gordon H. Sato, Jochen Schacht, Michael J. Shamblott, Graham Sharp, Albert K. Shung, Adam J. Singer, Barry A. Solomon, Ruth R. Solomon, Susan J. Sullivan, Shuichi Takayama, Jeffrey Teumer, Robert C. Thomson, Mehmet Toner, Vickery Trinkaus-Randall, Ross Tubo, Brian R. Unsworth, Charles A. Vacanti, Joseph P. Vacanti, Martin P. Vacanti, Robert F. Valentini, Gordana Vunjak-Novakovic, Lars U. Wahlberg, Taylor G. Wang, John F. Warner, George M. Whitesides, Jay M. Wilson, Haiyun Wu, Arron S.L. Xu, Lian Xue, Ioannis V. Yannas, Michael J. Yaszemski, Nan Zhang, Beth A. Zielinski, A. Zielke, U. Zimmerman
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::29045b09162a51ba8a261d09baa1b169
https://doi.org/10.1016/b978-012436630-5/50000-3
https://doi.org/10.1016/b978-012436630-5/50000-3
Publikováno v:
Biochemistry. 31(35)
The methionine 80 sulfur-heme iron bond of rat cytochrome c, whose stability is decreased by mutating the phylogenetically invariant residue proline 30 to alanine and increased when tyrosine 67 is changed to phenylalanine, recovers its wild-type char
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5c03db74e2037da01e1791cbaa2ec082
https://pubmed.ncbi.nlm.nih.gov/1326327
https://pubmed.ncbi.nlm.nih.gov/1326327
Publikováno v:
Bioenergetics ISBN: 9781468458374
For a protein as old as cytochrome c, which shows exquisite adaptation to its particular environment in the species carrying it, and which has been extensively studied, the properties of site-directed mutants should be readily predictable and fall wi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::7b83ca87b84344b9cba7c2a90e84488f
https://doi.org/10.1007/978-1-4684-5835-0_12
https://doi.org/10.1007/978-1-4684-5835-0_12
The tyrosine-67 to phenylalanine mutated rat cytochrome c is similar to the unmutated protein in its spectral, reduction potential, and enzymic electron-transfer properties. However, the loss of the 695-nm band, characteristic of the ferric form of t
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::fe738ef6c84649a5744f3b50ff5866da
https://europepmc.org/articles/PMC287170/
https://europepmc.org/articles/PMC287170/
Autor:
Emanuel Margoliash, Thomas L. Luntz
Publikováno v:
Cytochrome Systems ISBN: 9781461290780
The information encoded in the amino acid sequence of a protein, the major expression of the genetic make-up of the organism in that particular protein, has been interpreted in many ways in attempts to understand important structural and functional c
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::5234085be19742576d11f5efa78eac93
https://doi.org/10.1007/978-1-4613-1941-2_36
https://doi.org/10.1007/978-1-4613-1941-2_36