Zobrazeno 61 - 70
of 711
pro vyhledávání: '"D, Cope"'
Publikováno v:
Infection and Immunity. 68:4092-4101
Haemophilus influenzae can utilize different protein-bound forms of heme for growth in vitro. A previous study (I. Maciver, J. L. Latimer, H. H. Liem, U. Muller-Eberhard, Z. Hrkal, and E. J. Hansen. Infect. Immun. 64:3703–3712, 1996) indicated that
Autor:
Leslie D. Cope, Eric R. Lafontaine, Jo L. Latimer, Eric J. Hansen, George H. McCracken, Christoph Aebi
Publikováno v:
Journal of Bacteriology. 182:1364-1373
The UspA1 and UspA2 proteins of Moraxella catarrhalis are structurally related, are exposed on the bacterial cell surface, and migrate as very high-molecular-weight complexes in sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Previous anal
Autor:
Eric J. Hansen, Christine K. Ward, Sheryl R. Lumbley, Teresa Lagergård, Leslie D. Cope, Marla K. Stevens, Jo L. Latimer
Publikováno v:
Infection and Immunity. 67:3900-3908
Haemophilus ducreyi expresses a soluble cytolethal distending toxin (CDT) that kills HeLa, HEp-2, and other human epithelial cells in vitro. H. ducreyi CDT activity is encoded by a three-gene cluster ( cdtABC ), and antibody to the cdtC gene product
Autor:
Clive A. Slaughter, Leslie D. Cope, Eric J. Hansen, Frederick W. Henderson, George H. McCracken, Eric R. Lafontaine, Christoph Aebi, Charles A. Hasemann
Publikováno v:
Journal of Bacteriology. 181:4026-4034
The uspA1 and uspA2 genes of M. catarrhalis O35E encode two different surface-exposed proteins which were previously shown to share a 140-amino-acid region with 93% identity (C. Aebi, I. Maciver, J. L. Latimer, L. D. Cope, M. K. Stevens, S. E. Thomas
Autor:
Jong I. Lee, Julio F. Mata-Segreda, Jakob Wirz, II Peter G. Conrad, Elizabeth D. Cope, Bruno Hellrung, Richard S. Givens, Marek Mac, Yavor Kamdzhilov, Richard L. Schowen, Dominik Heger
Publikováno v:
Journal of the American Chemical Society. 130:3307-3309
The p-hydroxyphenacyl group 1 is an effective photoremovable protecting group, because it undergoes an unusual photo-Favorskii rearrangement concomitant with the fast release (
Autor:
Jo L. Latimer, Eric R. Lafontaine, Sheryl L. Lumbley, Leslie D. Cope, Eric J. Hansen, George H. McCracken, Christoph Aebi
Publikováno v:
Infection and Immunity. 66:3113-3119
The UspA surface antigen of Moraxella catarrhalis was recently shown to be comprised of two different proteins (UspA1 and UspA2) which share an internal region containing 140 amino acids with 93% identity (C. Aebi, I. Maciver, J. L. Latimer, L. D. Co
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Autor:
Clive A. Slaughter, Sharon E. Thomas, Jo L. Latimer, Christoph Aebi, Leslie D. Cope, George H. McCracken, Eric J. Hansen
Publikováno v:
Infection and Immunity. 66:540-548
A monoclonal antibody (MAb) (MAb 10F3) directed against the CopB outer membrane protein of Moraxella catarrhalis previously was found to enhance pulmonary clearance of M. catarrhalis in an animal model (M. Helminen, I. Maciver, J. L. Latimer, L. D. C
Publikováno v:
Infection and Immunity. 66:4511-4516
Utilization of heme-hemopexin as a source of heme by Haemophilus influenzae type b is dependent on expression by this bacterium of the 100-kDa HxuA protein, which is both present on the bacterial cell surface and released into the culture supernatant
Autor:
Eric J. Hansen, Leslie D. Cope, Christoph Aebi, Sharon E. Thomas, George H. McCracken, Marla K. Stevens, Isobel Maciver, Jo L. Latimer
Publikováno v:
Infection and Immunity. 65:4367-4377
The high-molecular-weight UspA protein of Moraxella catarrhalis has been described as being both present on the surface of all M. catarrhalis disease isolates examined to date and a target for a monoclonal antibody (MAb 17C7) which enhanced pulmonary