T. Kaabache

发表

The gamma-carboxyglutamic acid domain of anticoagulant protein S is involved in activated protein C cofactor activity, independently of phospholipid binding.

B. Villoutreix, M. Aiach, B. L. Le Bonniec, 2005, Blood.

The gamma-carboxyglutamic acid ( Gla ) domain of anticoagulant protein S is involved in activated protein C-cofactor activity , independently of phospholipid binding Running title : PS Gla domain-mediated APC-cofactor activity

B. Villoutreix, M. Aiach, D. Borgel, 2004 .

The protein S thrombin‐sensitive region modulates phospholipid binding and the γ‐carboxyglutamic acid‐rich (Gla) domain conformation in a non‐specific manner

M. Aiach, D. Borgel, F. Saller, 2006, Journal of thrombosis and haemostasis : JTH.

Implication of protein S thrombin-sensitive region with membrane binding via conformational changes in the gamma-carboxyglutamic acid-rich domain.

M. Aiach, P. Gaussem, C. Garbay, 2001, The Biochemical journal.

Expression and characterization of recombinant protein S with the Ser 460 Pro mutation.

M. Aiach, P. Gaussem, D. Borgel, 2000, Thrombosis research.

Membrane binding and anticoagulant properties of protein S natural variants.

F. Bernardi, M. Pinotti, G. Marchetti, 2010, Thrombosis research.

Molecular bases of type II protein S deficiency: the I203‐D204 deletion in the EGF4 domain alters GLA domain function

M. Pinotti, F. Bernardi, M. Pinotti, 2006, Journal of thrombosis and haemostasis : JTH.

Direct solution hybridization of guanidine thiocyanate-solubilized cells for quantitation of mRNAs in hepatocytes.

G. Feldmann, D. Bernuau, B. Lardeux, 1995, Analytical biochemistry.

B. Villoutreix, J. Emmerich, M. Aiach, 2007 .