Christopher Batters
Current Organizations / Institutes
The organizations/institutes from the scholar's latest article
Research Subjects
Christopher Batters has a total of 14 co-authors. Here are the top co-authors by number of shared publications:
- Claudia Veigel
Ludwig-Maximilians-Universität München, Department of Cellular Physiology, Biomedical Centre (BMC) Grosshadnerstraße 9
2 shared publications Beate Averbeck
1 shared publicationChristine Werner
1 shared publicationClaudia Veigel
Ludwig-Maximilians-Universität München
1 shared publicationConstanze Helbig
1 shared publicationDario Saczko-Brack
1 shared publication
Latest Publications
- 1 January 2015
- Published by Elsevier in Biophysical Journal
- Vol. 108 (2) , 618a
Regulation of Myosin VI Studied by Electron Microscopy
- 1 January 2015
- Published by Elsevier in Biophysical Journal
- Vol. 108 (2) , 618a
Regulation of Myosin VI Studied by Electron Microscopy
- 1 January 2015
- Published by Elsevier in Biophysical Journal
- Vol. 108 (2) , 303a
In vivo and in vitro Studies of Myosin-XXI Dynamics
- 1 January 2015
- Published by Elsevier in Biophysical Journal
- Vol. 108 (2) , 303a
In vivo and in vitro Studies of Myosin-XXI Dynamics
- 1 July 2011
- Published by Springer Nature
- Vol. 778, 97-109
Using Optical Tweezers to Study the Fine Details of Myosin ATPase Mechanochemical Cycle
Optical tweezers offer the capability to directly observe nanometre displacements and apply piconewton forces to single proteins. This method has been applied to the study of many different biological systems. Optical tweezers have proven to be particularly useful in studying the fine details of the mechanisms of molecular motor proteins, and how their movement is coordinated with ATPase activity. This includes actin, microtubule, and also DNA- and RNA-based motor systems. Here, we provide the information necessary to reproduce the “three-bead geometry” widely applied to the study of actomyosin interactions, the “paradigm system” for motors that only interact intermittently with their filament substrate, and discuss how single-molecule interactions can be detected, calibrated and analysed.
- 1 July 2011
- Published by Springer Nature
- Vol. 778, 97-109
Using Optical Tweezers to Study the Fine Details of Myosin ATPase Mechanochemical Cycle
Optical tweezers offer the capability to directly observe nanometre displacements and apply piconewton forces to single proteins. This method has been applied to the study of many different biological systems. Optical tweezers have proven to be particularly useful in studying the fine details of the mechanisms of molecular motor proteins, and how their movement is coordinated with ATPase activity. This includes actin, microtubule, and also DNA- and RNA-based motor systems. Here, we provide the information necessary to reproduce the “three-bead geometry” widely applied to the study of actomyosin interactions, the “paradigm system” for motors that only interact intermittently with their filament substrate, and discuss how single-molecule interactions can be detected, calibrated and analysed.
- 1 February 2009
- Published by Elsevier in Biophysical Journal
- Vol. 96 (3) , 139a-140a
Single Molecule Investigation of the Acto-Myosin-10 Complex Using Optical Tweezers
- 1 February 2009
- Published by Elsevier in Biophysical Journal
- Vol. 96 (3) , 139a-140a
Single Molecule Investigation of the Acto-Myosin-10 Complex Using Optical Tweezers