A. Albert

The peptidyl-prolyl isomerase Pin1 interacts with hSpt5 phosphorylated by Cdk9.

H. Handa, O. Bensaude, S. Lavoie, 2001, Journal of molecular biology.

A hyperphosphorylated form of RNA polymerase II is the major interphase antigen of the phosphoprotein antibody MPM-2 and interacts with the peptidyl-prolyl isomerase Pin1.

S. Lavoie, A. Albert, M. Vincent, 1999, Journal of cell science.

Heat shock-induced alterations in phosphorylation of the largest subunit of RNA polymerase II as revealed by monoclonal antibodies CC-3 and MPM-2.

S. Lavoie, A. Albert, M. Vincent, 1999, Biochemistry and cell biology = Biochimie et biologie cellulaire.

The multifunctional nuclear protein p54nrb is multiphosphorylated in mitosis and interacts with the mitotic regulator Pin1.

A. Traish, S. Lavoie, A. Albert, 2005, Journal of molecular biology.

Multisite phosphorylation of Pin1-associated mitotic phosphoproteins revealed by monoclonal antibodies MPM-2 and CC-3

S. Lavoie, A. Albert, M. Vincent, 2004, BMC Cell Biology.

[Unexpected roles of the peptidyl-prolyl cis/trans isomerase Pin1].

S. Lavoie, A. Albert, M. Vincent, 2003, Medecine sciences : M/S.