Werner Kliche

Crystal structure of the motor domain of a class-I myosin (2002)

Kollmar,Martin, Dürrwang,Ulrike, Kliche,Werner, Manstein,Dietmar J., Kull,F. Jon

The crystal structure of the motor domain of Dictyostelium discoideum myosin-IE, a monomeric unconventional myosin, was determined. The crystallographic asymmetric unit contains four independently...

Crystal structure of the motor domain of a class-I myosin (2002)

Kollmar, Martin, Dürrwang, Ulrike, Kliche, Werner, Manstein, Dietmar J., Kull, F. Jon

The crystal structure of the motor domain of Dictyostelium discoideum myosin-IE, a monomeric unconventional myosin, was determined. The crystallographic asymmetric unit contains four independently...

Structure of a genetically engineered molecular motor (2001)

Kliche,Werner, Fujita-Becker,Setsuko, Kollmar,Martin, Manstein,Dietmar J., Kull,F. Jon

Molecular motors move unidirectionally along polymer tracks, producing movement and force in an ATP-dependent fashion. They achieve this by amplifying small conformational changes in the...

Structure of a genetically engineered molecular motor (2001)

Kliche,Werner, Fujita-Becker,Setsuko, Kollmar,Martin, Manstein,Dietmar J., Kull,F. Jon

Molecular motors move unidirectionally along polymer tracks, producing movement and force in an ATP-dependent fashion. They achieve this by amplifying small conformational changes in the...

Structure of a genetically engineered molecular motor (2001)

Kliche, Werner, Fujita-Becker, Setsuko, Kollmar, Martin, Manstein, Dietmar J., Kull, F. Jon

Molecular motors move unidirectionally along polymer tracks, producing movement and force in an ATP-dependent fashion. They achieve this by amplifying small conformational changes in the...

Structure of a genetically engineered molecular motor (2001)

Kliche, Werner, Fujita-Becker, Setsuko, Kollmar, Martin, Manstein, Dietmar J., Kull, F. Jon

Molecular motors move unidirectionally along polymer tracks, producing movement and force in an ATP-dependent fashion. They achieve this by amplifying small conformational changes in the...

Stepwise Modulation of ATPase Activity, Nucleotide Trapping, and Sliding Motility of Myosin S1 by Modification of the Thiol Region with Residues of Increasing Size (2000)

Tiepold,Markus, Kliche,Werner, Pfannstiel,Jörg, Faulstich,Heinz

Stepwise Modulation of ATPase Activity, Nucleotide Trapping, and Sliding Motility of Myosin S1 by Modification of the Thiol Region with Residues of Increasing Size (2000)

Tiepold, Markus, Kliche, Werner, Pfannstiel, Jörg, Faulstich, Heinz

Thiol-specific cross-linkers of variable length reveal a similar separation of SH1 and SH2 in myosin subfragment 1 in the presence and absence of MgADP (1999)

Kliche,Werner, Pfannstiel,Jörg, Tiepold,Markus, Stoeva,Stanka, Faulstich,Heinz

A series of thiol-specific cross-linking reagents were prepared for studying the kinetics of cross-linking between SH1 (Cys707) and SH2 (Cys697) in rabbit skeletal muscle myosin subfragment 1. The...

Thiol-specific cross-linkers of variable length reveal a similar separation of SH1 and SH2 in myosin subfragment 1 in the presence and absence of MgADP (1999)

Kliche, Werner, Pfannstiel, Jörg, Tiepold, Markus, Stoeva, Stanka, Faulstich, Heinz

A series of thiol-specific cross-linking reagents were prepared for studying the kinetics of cross-linking between SH1 (Cys707) and SH2 (Cys697) in rabbit skeletal muscle myosin subfragment 1. The...

Strukturelle und funktionelle Analyse von Myosin Subfragment 1 mit längenvariablen thiolspezifischen cross-linkern (1999)

Kliche, Werner

Strukturelle und funktionelle Analyse von Myosin Subfragment 1 mit längenvariablen thiolspezifischen cross-linkern / (1999)

Kliche, Werner.

Heidelberg, Universiẗat, Diss., 1999.

Measurement of the distance between two thiols in a protein by kinetic analysis of a series of cross-linking reactions (1998)

Faulstich,Heinz, Kliche,Werner, Tiepold,Markus

Measurement of the distance between two thiols in a protein by kinetic analysis of a series of cross-linking reactions (1998)

Faulstich, Heinz, Kliche, Werner, Tiepold, Markus

Crystal structure of the motor domain of a class-I myosin

Kollmar, Martin, Dürrwang, Ulrike, Kliche, Werner, Manstein, Dietmar J., Kull, F.Jon

The crystal structure of the motor domain of Dictyostelium discoideum myosin-IE, a monomeric unconventional myosin, was determined. The crystallographic asymmetric unit contains four independently...

Structure of a genetically engineered molecular motor

Kliche, Werner, Fujita-Becker, Setsuko, Kollmar, Martin, Manstein, Dietmar J., Kull, F.Jon

Molecular motors move unidirectionally along polymer tracks, producing movement and force in an ATP-dependent fashion. They achieve this by amplifying small conformational changes in the...

Crystal structure of the motor domain of a class-I myosin

Kollmar, Martin, Dürrwang, Ulrike, Kliche, Werner, Manstein, Dietmar J., Kull, F.Jon

The crystal structure of the motor domain of Dictyostelium discoideum myosin-IE, a monomeric unconventional myosin, was determined. The crystallographic asymmetric unit contains four independently...

Structure of a genetically engineered molecular motor

Kliche, Werner, Fujita-Becker, Setsuko, Kollmar, Martin, Manstein, Dietmar J., Kull, F.Jon

Molecular motors move unidirectionally along polymer tracks, producing movement and force in an ATP-dependent fashion. They achieve this by amplifying small conformational changes in the...