K. B. Møller

发表

Structure-based Design of a Low Molecular Weight, Nonphosphorus, Nonpeptide, and Highly Selective Inhibitor of Protein-tyrosine Phosphatase 1B*

Ole Hvilsted Olsen, Sven Branner, O. Olsen, 2000, The Journal of Biological Chemistry.

Molecular cloning and mammalian expression of human beta 2-glycoprotein I cDNA.

N. Møłler, E. Boel, K. B. Møller, 1991, FEBS letters.

Changing the insulin receptor to possess insulin-like growth factor I ligand specificity.

N. Møłler, K. Norris, A. S. Andersen, 1990, Biochemistry.

The ligand specificities of the insulin receptor and the insulin-like growth factor I receptor reside in different regions of a common binding site.

N. Møłler, N. Møller, L. Schäffer, 1991, Proceedings of the National Academy of Sciences of the United States of America.

Molecular cloning and mammalian expression of human β2‐glycoprotein I cDNA

E. Boel, N. Møller, L. Sottrup-jensen, 1991 .

Enzyme kinetic characterization of protein tyrosine phosphatases.

J. Andersen, G. Peters, N. Møller, 2003, Biochimie.

Water-molecule network and active-site flexibility of apo protein tyrosine phosphatase 1B.

J. Kastrup, L. Iversen, Anja K Pedersen, 2004, Acta crystallographica. Section D, Biological crystallography.

Structure Determination of T Cell Protein-tyrosine Phosphatase*

Sven Branner, G. Peters, L. Iversen, 2002, The Journal of Biological Chemistry.

Structure-based Design of Selective and Potent Inhibitors of Protein-tyrosine Phosphatase β*

M. J. Newman, O. Olsen, L. Iversen, 2004, Journal of Biological Chemistry.

Residue 182 influences the second step of protein-tyrosine phosphatase-mediated catalysis.

J. Kastrup, G. Peters, L. Iversen, 2004, The Biochemical journal.

Structure-based design of selective and potent inhibitors of protein-tyrosine phosphatase beta.

M. J. Newman, O. Olsen, L. Iversen, 2004, Journal of Biological Chemistry.

2-(Oxalylamino)-Benzoic Acid Is a General, Competitive Inhibitor of Protein-tyrosine Phosphatases*

L. Iversen, H. Andersen, C. B. Jeppesen, 2000, The Journal of Biological Chemistry.

Src kinase associates with a member of a distinct subfamily of protein-tyrosine phosphatases containing an ezrin-like domain.

A. Ullrich, N. Møłler, R. Lammers, 1994, Proceedings of the National Academy of Sciences of the United States of America.

Residue 259 Is a Key Determinant of Substrate Specificity of Protein-tyrosine Phosphatases 1B and α*

O. Olsen, G. Peters, L. Iversen, 2000, The Journal of Biological Chemistry.

Selective Down-regulation of the Insulin Receptor Signal by Protein-tyrosine Phosphatases α and ε (*)

A. Ullrich, R. Lammers, N. Møller, 1995, The Journal of Biological Chemistry.

Comparative study of protein tyrosine phosphatase-epsilon isoforms: membrane localization confers specificity in cellular signalling.

J. Clausen, J. Andersen, N. Møłler, 2001, The Biochemical journal.

Steric hindrance as a basis for structure-based design of selective inhibitors of protein-tyrosine phosphatases.

M. J. Newman, O. Olsen, G. Peters, 2001, Biochemistry.