Zobrazeno 1 - 5
of 5
pro vyhledávání: '"Olatomirin O. Kolade"'
Autor:
Ansgar J. Pommer, Olatomirin O. Kolade, Stephen B. Carr, Colin Kleanthous, Cristina A. Bouchcinsky, Andrew M. Hemmings, Ulrike C. Kühlmann
Publikováno v:
Biochimie. 84:439-446
Nuclease E colicins that exert their cytotoxic activity through either non-specific DNase or specific rRNase action are inhibited by immunity proteins in a high affinity interaction that gives complete protection to the producing host cell from the d
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ac2085fa87b92bd98c5b7f3cd721d528
https://doi.org/10.1016/s0300-9084(02)01451-7
https://doi.org/10.1016/s0300-9084(02)01451-7
Publikováno v:
Journal of pharmaceutical sciences. 104(2)
Adjuvant-containing drug products can be exposed to high levels of interfacial shear during manufacture. This may affect the integrity of the adjuvant, alter its interaction with the drug substance or change the physical characteristics of the drug p
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::fc8957b1e563b262129983fb229c5e98
https://pubmed.ncbi.nlm.nih.gov/25175154
https://pubmed.ncbi.nlm.nih.gov/25175154
Autor:
Margaret Wexler, D. Bellini, Olatomirin O. Kolade, Jonathan D. Todd, Andrew W. B. Johnston, Andrew M. Hemmings, Gary Sawers
Publikováno v:
Microbiology (Reading, England). 149(Pt 5)
Rhizobium leguminosarum fur mutants were unaffected in Fe-dependent regulation of several operons that specify different Fe uptake systems, yet cloned R. leguminosarum fur partially corrected an Escherichia coli fur mutant and R. leguminosarum Fur pr
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::bc6a942766e5a3096e5c2609f246695b
https://pubmed.ncbi.nlm.nih.gov/12724397
https://pubmed.ncbi.nlm.nih.gov/12724397
Autor:
Margaret Wexler, Olatomirin O. Kolade, Andrew M. Hemmings, P. Bellini, Andrew W. B. Johnston, J. G. Grossmann
Publikováno v:
Biochemical Society transactions. 30(4)
The X-ray crystal structure of the apo-form of the Fur protein from Rhizobium leguminosarum has been solved at 2.7 å resolution. Small-angle X-ray scattering was used to give information on the solution conformation of the protein. The Fur homodimer
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::07d9aebf9dda9817a99511352ce3766c
https://pubmed.ncbi.nlm.nih.gov/12196192
https://pubmed.ncbi.nlm.nih.gov/12196192
Autor:
Yong Hoon Lee1,2, Olatomirin O. Kolade1,3, Nomura, Kinya1, Arvidson, Dennis N.3, Sheng Yang He1,3,4 hes@msu.edu
Publikováno v:
Journal of Biological Chemistry. 6/3/2005, Vol. 280 Issue 22, p21409-21417. 9p. 2 Color Photographs, 5 Diagrams, 3 Graphs.