A. J. Morris

发表

Association of the Insulin Receptor with Phospholipase C-γ (PLCγ) in 3T3-L1 Adipocytes Suggests a Role for PLCγ in Metabolic Signaling by Insulin*

P. Vollenweider, J. Olefsky, N. Webster, 1998, The Journal of Biological Chemistry.

Site-directed mutagenesis identifies aspartate 33 as a previously unidentified critical residue in the catalytic mechanism of rabbit aldolase A.

A. J. Morris, D. Tolan, 1993, The Journal of biological chemistry.

Activated Phosphatidylinositol 3-Kinase Is Sufficient to Mediate Actin Rearrangement and GLUT4 Translocation in 3T3-L1 Adipocytes*

A. Klippel, J. Olefsky, L. Williams, 1996, The Journal of Biological Chemistry.

Insulin-stimulated GLUT4 Translocation Is Mediated by a Divergent Intracellular Signaling Pathway (*)

J. Olefsky, D. Rose, M. Mueckler, 1995, The Journal of Biological Chemistry.

Lysine-146 of rabbit muscle aldolase is essential for cleavage and condensation of the C3-C4 bond of fructose 1,6-bis(phosphate).

A. J. Morris, D. Tolan, 1994, Biochemistry.

Evidence for an insulin receptor substrate 1 independent insulin signaling pathway that mediates insulin-responsive glucose transporter (GLUT4) translocation.

P. Vollenweider, J. Olefsky, D. Rose, 1996, Proceedings of the National Academy of Sciences of the United States of America.

Ligand-independent GLUT4 translocation induced by guanosine 5'-O-(3-thiotriphosphate) involves tyrosine phosphorylation.

P. Vollenweider, J. Olefsky, D. Rose, 1998, Endocrinology.

Association of the insulin receptor with phospholipase C-gamma (PLCgamma) in 3T3-L1 adipocytes suggests a role for PLCgamma in metabolic signaling by insulin.

P. Vollenweider, J. Olefsky, N. Webster, 1998, The Journal of biological chemistry.

The small guanosine triphosphate-binding protein Rab4 is involved in insulin-induced GLUT4 translocation and actin filament rearrangement in 3T3-L1 cells.

P. Vollenweider, Y. Le Marchand-Brustel, J. Olefsky, 1997, Endocrinology.

New superfamily members identified for Schiff-base enzymes based on verification of catalytically essential residues.

Karen N. Allen, A. J. Morris, D. Tolan, 2006, Biochemistry.

The Molecular Nature of the F-actin Binding Activity of Aldolase Revealed with Site-directed Mutants (*)

A. J. Morris, L. Pagliaro, D. Tolan, 1996, The Journal of Biological Chemistry.

Structure of a fructose-1,6-bis(phosphate) aldolase liganded to its natural substrate in a cleavage-defective mutant at 2.3 A(,).

A. J. Morris, K. Choi, D. Tolan, 1999, Biochemistry.

A lysine to arginine substitution at position 146 of rabbit aldolase A changes the rate-determining step to Schiff base formation.

A. J. Morris, R. C. Davenport, D. Tolan, 1996, Protein engineering.