D. Szczesna

发表

Familial Hypertrophic Cardiomyopathy Mutations in the Regulatory Light Chains of Myosin Affect Their Structure, Ca2+Binding, and Phosphorylation*

J. Stull, D. Szczesna, D. Ghosh, 2001, The Journal of Biological Chemistry.

Altered regulation of cardiac muscle contraction by troponin T mutations that cause familial hypertrophic cardiomyopathy.

D. Szczesna, G. Guzman, J. Potter, 2001, The Journal of biological chemistry.

Conformational changes of F-actin in myosin-free ghost single fibre induced by either phosphorylated or dephosphorylated heavy meromyosin.

D. Szczesna, D. Levitsky, Y. Borovikov, 1987, Biochimica et biophysica acta.

Factors influencing interaction of phosphorylated and dephosphorylated myosin with actin.

D. Szczesna, D. Stepkowski, I. Ka̧kol, 1985, Biochimica et biophysica acta.

The Role of the Four Ca Binding Sites of Troponin C in the Regulation of Skeletal Muscle Contraction (*)

D. Szczesna, G. Guzman, J. Potter, 1996, The Journal of Biological Chemistry.

Myosin S1 changes the orientation of caldesmon on actin.

P. Graceffa, D. Szczesna, S. Lehrer, 1994, Biochemistry.

The role of troponin in the Ca(2+)-regulation of skeletal muscle contraction.

D. Szczesna, J. Potter, 2002, Results and problems in cell differentiation.

The effect of pH on the Ca2+ affinity of the Ca2+ regulatory sites of skeletal and cardiac troponin C in skinned muscle fibres

B. Parsons, D. Szczesna, J. Potter, 1997, Journal of Muscle Research & Cell Motility.

Abnormal Contractile Function in Transgenic Mice Expressing a Familial Hypertrophic Cardiomyopathy-linked Troponin T (I79N) Mutation*

D. Szczesna, A. Gomes, J. Potter, 2001, The Journal of Biological Chemistry.

Altered Regulation of Cardiac Muscle Contraction by Troponin T Mutations That Cause Familial Hypertrophic Cardiomyopathy*

D. Szczesna, G. Guzman, J. Potter, 2000, The Journal of Biological Chemistry.

The tropomyosin domain is flexible and disordered in reconstituted thin filaments.

D. Szczesna, P. Fajer, 1995, Biochemistry.

Linear dichroism of acrylodan-labeled tropomyosin and myosin subfragment 1 bound to actin in myofibrils.

D. Szczesna, S. Lehrer, 1992, Biophysical journal.

Decoration of actin filaments with skeletal muscle heavy meromyosin containing either phosphorylated or dephosphorylated regulatory light chains.

D. Szczesna, H. Osińska, D. Stepkowski, 1985, Biochimica et biophysica acta.

Regulatory light chains of striated muscle myosin. Structure, function and malfunction.

D. Szczesna, 2003, Current drug targets. Cardiovascular & haematological disorders.

Phosphorylation of the regulatory light chains of myosin affects Ca2+ sensitivity of skeletal muscle contraction.

J. Stull, D. Szczesna, G. Zhi, 2002, Journal of applied physiology.

The Regulatory Light Chains of Myosin Modulate Cross-bridge Cycling in Skeletal Muscle (*)

D. Szczesna, J. Potter, Jiaju Zhao, 1996, The Journal of Biological Chemistry.

Effect of phosphorylation of myosin light chains on interaction of heavy meromyosin with regulated F-actin in ghost fibers

D. Szczesna, N. N. Lebedeva, Y. Borovikov, 1987, Experientia.

The binding of fluorescent phallotoxins to actin in myofibrils

D. Szczesna, S. Lehrer, 1993, Journal of Muscle Research & Cell Motility.

The Functional Role of the Domains of Troponin-C Investigated with Thrombin Fragments of Troponin-C Reconstituted into Skinned Muscle Fibers (*)

D. Szczesna, J. Potter, Z. Sheng, 1995, The Journal of Biological Chemistry.