Michael Kulke

PEVK Domain of Titin: An Entropic Spring with Actin-Binding Properties (2002)

Linke,Wolfgang A., Kulke,Michael, Li,Hongbin, Fujita-Becker,Setsuko, Neagoe,Ciprian, Manstein,Dietmar J., ...

The PEVKdomain of the giant muscle protein titin is a proline-rich sequence with unknown secondary/tertiary structure. Here we compared the force-extension behavior of cloned cardiac PEVK titin...

PEVK Domain of Titin: An Entropic Spring with Actin-Binding Properties (2002)

Linke,Wolfgang A., Kulke,Michael, Li,Hongbin, Fujita-Becker,Setsuko, Neagoea,Ciprian, Manstein,Dietmar J., ...

The PEVKdomain of the giant muscle protein titin is a proline-rich sequence with unknown secondary/tertiary structure. Here we compared the force-extension behavior of cloned cardiac PEVK titin...

PEVK Domain of Titin: An Entropic Spring with Actin-Binding Properties (2002)

Linke, Wolfgang A., Kulke, Michael, Li, Hongbin, Fujita-Becker, Setsuko, Neagoe, Ciprian, Manstein, Dietmar J., ...

The PEVKdomain of the giant muscle protein titin is a proline-rich sequence with unknown secondary/tertiary structure. Here we compared the force-extension behavior of cloned cardiac PEVK titin...

PEVK Domain of Titin: An Entropic Spring with Actin-Binding Properties (2002)

Linke, Wolfgang A., Kulke, Michael, Li, Hongbin, Fujita-Becker, Setsuko, Neagoea, Ciprian, Manstein, Dietmar J., ...

The PEVKdomain of the giant muscle protein titin is a proline-rich sequence with unknown secondary/tertiary structure. Here we compared the force-extension behavior of cloned cardiac PEVK titin...

Interaction between PEVK-titin and actin filaments: origin of a viscous force component in cardiac myofibrils (2001)

Kulke,Michael, Fujita-Becker,Setsuko, Rostkova,E., Neagoe,C., Labeit,D., Manstein,Dietmar J., ...

The giant muscle protein titin contains a unique sequence, the PEVK domain, the elastic properties of which contribute to the mechanical behavior of relaxed cardiomyocytes. Here, human N2-B–cardiac...

Interaction between PEVK-titin and actin filaments: origin of a viscous force component in cardiac myofibrils (2001)

Kulke, Michael, Fujita-Becker, Setsuko, Rostkova, E., Neagoe, C., Labeit, D., Manstein, Dietmar J., ...

The giant muscle protein titin contains a unique sequence, the PEVK domain, the elastic properties of which contribute to the mechanical behavior of relaxed cardiomyocytes. Here, human N2-B–cardiac...

Damped elastic recoil of the titin spring in myofibrils of human myocardium

Opitz, Christiane A., Kulke, Michael, Leake, Mark C., Neagoe, Ciprian, Hinssen, Horst, Hajjar, Roger J., ...

The giant protein titin functions as a molecular spring in muscle and is responsible for most of the passive tension of myocardium. Because the titin spring is extended during diastolic stretch, it...

Damped elastic recoil of the titin spring in myofibrils of human myocardium

Opitz, Christiane A., Kulke, Michael, Leake, Mark C., Neagoe, Ciprian, Hinssen, Horst, Hajjar, Roger J., ...

The giant protein titin functions as a molecular spring in muscle and is responsible for most of the passive tension of myocardium. Because the titin spring is extended during diastolic stretch, it...

Titin-based contribution to shortening velocity of rabbit skeletal myofibrils

Minajeva, Ave, Neagoe, Ciprian, Kulke, Michael, Linke, Wolfgang A

The shortening velocity of skeletal muscle fibres is determined principally by actomyosin cross-bridges. However, these contractile elements are in parallel with elastic elements, whose main...

Kettin, a major source of myofibrillar stiffness in Drosophila indirect flight muscle

Kulke, Michael, Neagoe, Ciprian, Kolmerer, Bernhard, Minajeva, Ave, Hinssen, Horst, Bullard, Belinda, ...

Kettin is a high molecular mass protein of insect muscle that in the sarcomeres binds to actin and α-actinin. To investigate kettin's functional role, we combined immunolabeling experiments with...