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J Reizer

Showing results (121-130 of 128) with videos related to

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The Journal of Biological Chemistry|May 27, 1994
In vitro asymmetric binding of the pleiotropic regulatory protein, FruR, to the ace operator controlling glyoxylate shunt enzyme synthesisJ C Cortay, D Nègre, M Scarabel, et al.
Biochemistry|July 26, 1991
Polypeptide backbone resonance assignments and secondary structure of Bacillus subtilis enzyme IIIglc determined by two-dimensional and three-dimensional heteronuclear NMR spectroscopyW J Fairbrother, J Cavanagh, H J Dyson, et al.
The Journal of Biological Chemistry|March 3, 1995
Novel proteins of the phosphotransferase system encoded within the rpoN operon of Escherichia coli. Enzyme IIANtr affects growth on organic nitrogen and the conditional lethality of an erats mutantB S Powell, D L Court, T Inada, et al.
Structure (London, England : 1993)|February 15, 1997
The structure of an energy-coupling protein from bacteria, IIBcellobiose, reveals similarity to eukaryotic protein tyrosine phosphatasesR L van Montfort, T Pijning, K H Kalk, et al.
Journal of Molecular Biology|June 17, 1994
Crystallization of enzyme IIB of the cellobiose-specific phosphotransferase system of Escherichia coliR L van Montfort, T Pijning, K H Kalk, et al.
Research in Microbiology|November 11, 1991
Sequence and evolution of the FruR protein of Salmonella typhimurium: a pleiotropic transcriptional regulatory protein possessing both activator and repressor functions which is homologous to the periplasmic ribose-binding proteinN B Vartak, J Reizer, A Reizer, et al.
Protein Science : a Publication of the Protein Society|February 1, 1994
Enzyme IIBcellobiose of the phosphoenol-pyruvate-dependent phosphotransferase system of Escherichia coli: backbone assignment and secondary structure determined by three-dimensional NMR spectroscopyE Ab, G K Schuurman-Wolters, M H Saier, et al.
Nature|September 13, 2000
Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic pathogenC K Stover, X Q Pham, A L Erwin, et al.
Pageof 13

Showing results (121-130 of 128) with videos related to

Sort By:
Pageof 13
You have reached the last page of results.This site can display upto 128 results.
The Journal of Biological Chemistry|May 27, 1994
In vitro asymmetric binding of the pleiotropic regulatory protein, FruR, to the ace operator controlling glyoxylate shunt enzyme synthesisJ C Cortay, D Nègre, M Scarabel, et al.
Biochemistry|July 26, 1991
Polypeptide backbone resonance assignments and secondary structure of Bacillus subtilis enzyme IIIglc determined by two-dimensional and three-dimensional heteronuclear NMR spectroscopyW J Fairbrother, J Cavanagh, H J Dyson, et al.
The Journal of Biological Chemistry|March 3, 1995
Novel proteins of the phosphotransferase system encoded within the rpoN operon of Escherichia coli. Enzyme IIANtr affects growth on organic nitrogen and the conditional lethality of an erats mutantB S Powell, D L Court, T Inada, et al.
Structure (London, England : 1993)|February 15, 1997
The structure of an energy-coupling protein from bacteria, IIBcellobiose, reveals similarity to eukaryotic protein tyrosine phosphatasesR L van Montfort, T Pijning, K H Kalk, et al.
Journal of Molecular Biology|June 17, 1994
Crystallization of enzyme IIB of the cellobiose-specific phosphotransferase system of Escherichia coliR L van Montfort, T Pijning, K H Kalk, et al.
Research in Microbiology|November 11, 1991
Sequence and evolution of the FruR protein of Salmonella typhimurium: a pleiotropic transcriptional regulatory protein possessing both activator and repressor functions which is homologous to the periplasmic ribose-binding proteinN B Vartak, J Reizer, A Reizer, et al.
Protein Science : a Publication of the Protein Society|February 1, 1994
Enzyme IIBcellobiose of the phosphoenol-pyruvate-dependent phosphotransferase system of Escherichia coli: backbone assignment and secondary structure determined by three-dimensional NMR spectroscopyE Ab, G K Schuurman-Wolters, M H Saier, et al.
Nature|September 13, 2000
Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic pathogenC K Stover, X Q Pham, A L Erwin, et al.
Pageof 13