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Journal of Bacteriology|June 1, 1991
Intramolecular second-site revertants to the phosphorylation site mutation in OmpR, a kinase-dependent transcriptional activator in Escherichia coliR E Brissette, K L Tsung, M InouyeGenes to Cells : Devoted to Molecular & Cellular Mechanisms|February 1, 1996
Differential thermoregulation of two highly homologous cold-shock genes, cspA and cspB, of Escherichia coliJ P Etchegaray, P G Jones, M InouyeMolecular & General Genetics : MGG|November 1, 1987
Overproduction of an antisense RNA containing the oop RNA sequence of bacteriophage lambda induces clear plaque formationK M Takayama, N Houba-Herin, M InouyeMolecular Microbiology|December 1, 1993
Identification of a phosphorylation site and functional analysis of conserved aspartic acid residues of OmpR, a transcriptional activator for ompF and ompC in Escherichia coliJ Delgado, S Forst, S Harlocker, et al.The Journal of Biological Chemistry|December 25, 1986
Interaction of a transcriptional activator, OmpR, with reciprocally osmoregulated genes, ompF and ompC, of Escherichia coliS Norioka, G Ramakrishnan, K Ikenaka, et al.Molecular Microbiology|January 1, 1997
Promoter-independent cold-shock induction of cspA and its derepression at 37 degrees C by mRNA stabilizationL Fang, W Jiang, W Bae, et al.Proceedings of the National Academy of Sciences of the United States of America|May 24, 1994
Crystal structure of CspA, the major cold shock protein of Escherichia coliH Schindelin, W Jiang, M Inouye, et al.Gene|April 8, 1994
Cloning and sequences of two macrolide-resistance-encoding genes from mycinamicin-producing Micromonospora griseorubidaM Inouye, T Morohoshi, S Horinouchi, et al.International Journal of Clinical and Experimental Pathology|December 22, 2017
Primary parotid adenocarcinoma metastasis to the spleen with PIK3CA mutation: cytological findings and review of the literatureCasey M Inouye, Valsamo Anagnostou, Qing Kay LiThe Journal of Biological Chemistry|October 20, 1995
Functional analysis of the propeptide of subtilisin E as an intramolecular chaperone for protein folding. Refolding and inhibitory abilities of propeptide mutantsY Li, Z Hu, F Jordan, et al.Pageof 56