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W N Lipscomb

Showing results (51-60 of 120) with videos related to

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Proceedings of the National Academy of Sciences of the United States of America|June 1, 1978
Elimination of cooperativity in aspartate transcarbamylase by nitration of a single tyrosine residueS M Landfear, D R Evans, W N Lipscomb
Proceedings of the National Academy of Sciences of the United States of America|August 15, 1991
Leucine aminopeptidase: bestatin inhibition and a model for enzyme-catalyzed peptide hydrolysisS K Burley, P R David, W N Lipscomb
Proceedings of the National Academy of Sciences of the United States of America|July 1, 1984
Structure of unligated aspartate carbamoyltransferase of Escherichia coli at 2.6-A resolutionH M Ke, R B Honzatko, W N Lipscomb
Proceedings of the National Academy of Sciences of the United States of America|November 1, 1978
Three-dimensional structures of aspartate carbamoyltransferase from Escherichia coli and of its complex with cytidine triphosphateH L Monaco, J L Crawford, W N Lipscomb
Journal of Molecular Biology|February 5, 1987
2.5 A structure of aspartate carbamoyltransferase complexed with the bisubstrate analog N-(phosphonacetyl)-L-aspartateK L Krause, K W Volz, W N Lipscomb
Proceedings of the National Academy of Sciences of the United States of America|April 1, 1982
Zn(II)-induced cooperativity of Escherichia coli ornithine transcarbamoylaseL C Kuo, W N Lipscomb, E R Kantrowitz
Biochemistry|April 4, 1995
Structural aspects of the allosteric inhibition of fructose-1,6-bisphosphatase by AMP: the binding of both the substrate analogue 2,5-anhydro-D-glucitol 1,6-bisphosphate and catalytic metal ions monitored by X-ray crystallographyV Villeret, S Huang, Y Zhang, et al.
Proceedings of the National Academy of Sciences of the United States of America|July 15, 1991
Molecular structure of Bacillus subtilis aspartate transcarbamoylase at 3.0 A resolutionR C Stevens, K M Reinisch, W N Lipscomb
Proceedings of the National Academy of Sciences of the United States of America|March 1, 1985
Structure at 2.9-A resolution of aspartate carbamoyltransferase complexed with the bisubstrate analogue N-(phosphonacetyl)-L-aspartateK L Krause, K W Volz, W N Lipscomb
Proteins|February 1, 1993
Crystal structure of CTP-ligated T state aspartate transcarbamoylase at 2.5 A resolution: implications for ATCase mutants and the mechanism of negative cooperativityR P Kosman, J E Gouaux, W N Lipscomb
Pageof 12

Showing results (51-60 of 120) with videos related to

Sort By:
Pageof 12
Proceedings of the National Academy of Sciences of the United States of America|June 1, 1978
Elimination of cooperativity in aspartate transcarbamylase by nitration of a single tyrosine residueS M Landfear, D R Evans, W N Lipscomb
Proceedings of the National Academy of Sciences of the United States of America|August 15, 1991
Leucine aminopeptidase: bestatin inhibition and a model for enzyme-catalyzed peptide hydrolysisS K Burley, P R David, W N Lipscomb
Proceedings of the National Academy of Sciences of the United States of America|July 1, 1984
Structure of unligated aspartate carbamoyltransferase of Escherichia coli at 2.6-A resolutionH M Ke, R B Honzatko, W N Lipscomb
Proceedings of the National Academy of Sciences of the United States of America|November 1, 1978
Three-dimensional structures of aspartate carbamoyltransferase from Escherichia coli and of its complex with cytidine triphosphateH L Monaco, J L Crawford, W N Lipscomb
Journal of Molecular Biology|February 5, 1987
2.5 A structure of aspartate carbamoyltransferase complexed with the bisubstrate analog N-(phosphonacetyl)-L-aspartateK L Krause, K W Volz, W N Lipscomb
Proceedings of the National Academy of Sciences of the United States of America|April 1, 1982
Zn(II)-induced cooperativity of Escherichia coli ornithine transcarbamoylaseL C Kuo, W N Lipscomb, E R Kantrowitz
Biochemistry|April 4, 1995
Structural aspects of the allosteric inhibition of fructose-1,6-bisphosphatase by AMP: the binding of both the substrate analogue 2,5-anhydro-D-glucitol 1,6-bisphosphate and catalytic metal ions monitored by X-ray crystallographyV Villeret, S Huang, Y Zhang, et al.
Proceedings of the National Academy of Sciences of the United States of America|July 15, 1991
Molecular structure of Bacillus subtilis aspartate transcarbamoylase at 3.0 A resolutionR C Stevens, K M Reinisch, W N Lipscomb
Proceedings of the National Academy of Sciences of the United States of America|March 1, 1985
Structure at 2.9-A resolution of aspartate carbamoyltransferase complexed with the bisubstrate analogue N-(phosphonacetyl)-L-aspartateK L Krause, K W Volz, W N Lipscomb
Proteins|February 1, 1993
Crystal structure of CTP-ligated T state aspartate transcarbamoylase at 2.5 A resolution: implications for ATCase mutants and the mechanism of negative cooperativityR P Kosman, J E Gouaux, W N Lipscomb
Pageof 12