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D A Rudnick

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Proceedings of the National Academy of Sciences of the United States of America|November 1, 1992
Analogs of palmitoyl-CoA that are substrates for myristoyl-CoA:protein N-myristoyltransferaseD A Rudnick, T Lu, E Jackson-Machelski, et al.
The Journal of Biological Chemistry|April 15, 1992
Substrate specificity of Saccharomyces cerevisiae myristoyl-CoA: protein N-myristoyltransferase. Analysis of fatty acid analogs containing carbonyl groups, nitrogen heteroatoms, and nitrogen heterocycles in an in vitro enzyme assay and subsequent identification of inhibitors of human immunodeficiency virus I replicationB Devadas, T Lu, A Katoh, et al.
The Journal of Biological Chemistry|May 15, 1991
The substrate specificity of Saccharomyces cerevisiae myristoyl-CoA:protein N-myristoyltransferase. Analysis of myristic acid analogs containing oxygen, sulfur, double bonds, triple bonds, and/or an aromatic residueN S Kishore, T B Lu, L J Knoll, et al.
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Showing results (11-20 of 13) with videos related to

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Pageof 2
You have reached the last page of results.This site can display upto 13 results.
Proceedings of the National Academy of Sciences of the United States of America|November 1, 1992
Analogs of palmitoyl-CoA that are substrates for myristoyl-CoA:protein N-myristoyltransferaseD A Rudnick, T Lu, E Jackson-Machelski, et al.
The Journal of Biological Chemistry|April 15, 1992
Substrate specificity of Saccharomyces cerevisiae myristoyl-CoA: protein N-myristoyltransferase. Analysis of fatty acid analogs containing carbonyl groups, nitrogen heteroatoms, and nitrogen heterocycles in an in vitro enzyme assay and subsequent identification of inhibitors of human immunodeficiency virus I replicationB Devadas, T Lu, A Katoh, et al.
The Journal of Biological Chemistry|May 15, 1991
The substrate specificity of Saccharomyces cerevisiae myristoyl-CoA:protein N-myristoyltransferase. Analysis of myristic acid analogs containing oxygen, sulfur, double bonds, triple bonds, and/or an aromatic residueN S Kishore, T B Lu, L J Knoll, et al.
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