Wolfgang A. Linke

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...

Nature of PEVK-titin elasticity in skeletal muscle

Linke, Wolfgang A., Ivemeyer, Marc, Mundel, Peter, Stockmeier, Marc R., Kolmerer, Bernhard

A unique sequence within the giant titin molecule, the PEVK domain, has been suggested to greatly contribute to passive force development of relaxed skeletal muscle during stretch. To explore the...

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...

A troponin switch that regulates muscle contraction by stretch instead of calcium

Agianian, Bogos, Kržič, Uroš, Qiu, Feng, Linke, Wolfgang A, Leonard, Kevin, Bullard, Belinda

The flight muscles of many insects have a form of regulation enabling them to contract at high frequencies. The muscles are activated by periodic stretches at low Ca2+ levels. The same muscles also...

The molecular elasticity of the insect flight muscle proteins projectin and kettin

Bullard, Belinda, Garcia, Tzintzuni, Benes, Vladimir, Leake, Mark C., Linke, Wolfgang A., Oberhauser, Andres F.

Projectin and kettin are titin-like proteins mainly responsible for the high passive stiffness of insect indirect flight muscles, which is needed to generate oscillatory work during flight. Here we...

Nature of PEVK-titin elasticity in skeletal muscle

Linke, Wolfgang A., Ivemeyer, Marc, Mundel, Peter, Stockmeier, Marc R., Kolmerer, Bernhard

A unique sequence within the giant titin molecule, the PEVK domain, has been suggested to greatly contribute to passive force development of relaxed skeletal muscle during stretch. To explore the...

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...

A troponin switch that regulates muscle contraction by stretch instead of calcium

Agianian, Bogos, Kržič, Uroš, Qiu, Feng, Linke, Wolfgang A, Leonard, Kevin, Bullard, Belinda

The flight muscles of many insects have a form of regulation enabling them to contract at high frequencies. The muscles are activated by periodic stretches at low Ca2+ levels. The same muscles also...

The molecular elasticity of the insect flight muscle proteins projectin and kettin

Bullard, Belinda, Garcia, Tzintzuni, Benes, Vladimir, Leake, Mark C., Linke, Wolfgang A., Oberhauser, Andres F.

Projectin and kettin are titin-like proteins mainly responsible for the high passive stiffness of insect indirect flight muscles, which is needed to generate oscillatory work during flight. Here we...

Fibre type-specific increase in passive muscle tension in spinal cord-injured subjects with spasticity

Olsson, M Charlotte, Krüger, Martina, Meyer, Lars-Henrik, Ahnlund, Lena, Gransberg, Lennart, Linke, Wolfgang A, ...

Patients with spasticity typically present with an increased muscle tone that is at least partly caused by an exaggerated stretch reflex. However, intrinsic changes in the skeletal muscles, such as...

Isoform Diversity of Giant Proteins in Relation to Passive and Active Contractile Properties of Rabbit Skeletal Muscles

Prado, Lucas G., Makarenko, Irina, Andresen, Christian, Krüger, Martina, Opitz, Christiane A., Linke, Wolfgang A.

The active and passive contractile performance of skeletal muscle fibers largely depends on the myosin heavy chain (MHC) isoform and the stiffness of the titin spring, respectively. Open questions...

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...

I-Band Titin in Cardiac Muscle Is a Three-Element Molecular Spring and Is Critical for Maintaining Thin Filament Structure

Linke, Wolfgang A., Rudy, Diane E., Centner, Thomas, Gautel, Mathias, Witt, Christian, Labeit, Siegfried, ...

In cardiac muscle, the giant protein titin exists in different length isoforms expressed in the molecule's I-band region. Both isoforms, termed N2-A and N2-B, comprise stretches of Ig-like modules...

Differentiation- and stress-dependent nuclear cytoplasmic redistribution of myopodin, a novel actin-bundling protein

Weins, Astrid, Schwarz, Karin, Faul, Christian, Barisoni, Laura, Linke, Wolfgang A., Mundel, Peter

We report the cloning and functional characterization of myopodin, the second member of the synaptopodin gene family. Myopodin shows no significant homology to any known protein except synaptopodin....

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...