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J W Stebbins

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Biochemistry|March 3, 1992

Conversion of the noncooperative Bacillus subtilis aspartate transcarbamoylase into a cooperative enzyme by a single amino acid substitutionJ W Stebbins, E R Kantrowitz

The Journal of Biological Chemistry|September 5, 1989

The importance of the link between Glu204 of the catalytic chain and Arg130 of the regulatory chain for the homotropic and heterotropic properties of Escherichia coli aspartate transcarbamoylaseJ W Stebbins, E R Kantrowitz

Gene|December 12, 1996

A single vector cloning, mutagenesis and expression systemE M Towler, J W Stebbins, C Debouck

Biochemistry|April 24, 1990

Importance of residues Arg-167 and Gln-231 in both the allosteric and catalytic mechanisms of Escherichia coli aspartate transcarbamoylaseJ W Stebbins, Y Zhang, E R Kantrowitz

Biochemistry|March 21, 1989

Three residues involved in binding and catalysis in the carbamyl phosphate binding site of Escherichia coli aspartate transcarbamylaseJ W Stebbins, W Xu, E R Kantrowitz

Neurochemical Research|August 5, 1998

Characterization of myelin-associated glycoprotein (MAG) proteolysis in the human central nervous systemJ W Stebbins, H Jaffe, J R Möller

Biochemistry|February 21, 1989

A loop involving catalytic chain residues 230-245 is essential for the stabilization of both allosteric forms of Escherichia coli aspartate transcarbamylaseS A Middleton, J W Stebbins, E R Kantrowitz

Biochemistry|February 25, 1997

Determination of a native proteolytic site in myelin-associated glycoproteinJ W Stebbins, H Jaffe, H M Fales, et al.

The Journal of Biological Chemistry|October 7, 1994

Glutamic acid 86 is important for positioning the 80's loop and arginine 54 at the active site of Escherichia coli aspartate transcarbamoylase and for the structural stabilization of the C1-C2 interfaceD P Baker, J W Stebbins, E DeSena, et al.

Protein Science : a Publication of the Protein Society|November 1, 1992

Arginine 54 in the active site of Escherichia coli aspartate transcarbamoylase is critical for catalysis: a site-specific mutagenesis, NMR, and X-ray crystallographic studyJ W Stebbins, D E Robertson, M F Roberts, et al.

Pageof 2

Search research articles

Showing results (1-10 of 11) with videos related to

Sort By:

Pageof 2

Biochemistry|March 3, 1992

Conversion of the noncooperative Bacillus subtilis aspartate transcarbamoylase into a cooperative enzyme by a single amino acid substitutionJ W Stebbins, E R Kantrowitz

The Journal of Biological Chemistry|September 5, 1989

The importance of the link between Glu204 of the catalytic chain and Arg130 of the regulatory chain for the homotropic and heterotropic properties of Escherichia coli aspartate transcarbamoylaseJ W Stebbins, E R Kantrowitz

Gene|December 12, 1996

A single vector cloning, mutagenesis and expression systemE M Towler, J W Stebbins, C Debouck

Biochemistry|April 24, 1990

Importance of residues Arg-167 and Gln-231 in both the allosteric and catalytic mechanisms of Escherichia coli aspartate transcarbamoylaseJ W Stebbins, Y Zhang, E R Kantrowitz

Biochemistry|March 21, 1989

Three residues involved in binding and catalysis in the carbamyl phosphate binding site of Escherichia coli aspartate transcarbamylaseJ W Stebbins, W Xu, E R Kantrowitz

Neurochemical Research|August 5, 1998

Characterization of myelin-associated glycoprotein (MAG) proteolysis in the human central nervous systemJ W Stebbins, H Jaffe, J R Möller

Biochemistry|February 21, 1989

A loop involving catalytic chain residues 230-245 is essential for the stabilization of both allosteric forms of Escherichia coli aspartate transcarbamylaseS A Middleton, J W Stebbins, E R Kantrowitz

Biochemistry|February 25, 1997

Determination of a native proteolytic site in myelin-associated glycoproteinJ W Stebbins, H Jaffe, H M Fales, et al.

The Journal of Biological Chemistry|October 7, 1994

Glutamic acid 86 is important for positioning the 80's loop and arginine 54 at the active site of Escherichia coli aspartate transcarbamoylase and for the structural stabilization of the C1-C2 interfaceD P Baker, J W Stebbins, E DeSena, et al.

Protein Science : a Publication of the Protein Society|November 1, 1992

Arginine 54 in the active site of Escherichia coli aspartate transcarbamoylase is critical for catalysis: a site-specific mutagenesis, NMR, and X-ray crystallographic studyJ W Stebbins, D E Robertson, M F Roberts, et al.

Pageof 2