Guenther Woehlke

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Microtubule Interaction Site of the Kinesin Motor

Guenther Woehlke, Aaron K Ruby, Cynthia L. Hart, Bernice Ly, Nora Hom-Booher, Ronald D. Vale
Cell
1997

Kinesin and myosin are motor proteins that share a common structural core and bind to microtubules and actin filaments, respectively. While the actomyosin interface has been well studied, the… (More)

The kinesin KIF1C and microtubule plus ends regulate podosome dynamics in macrophages.

P. Kopp, Reiner Lammers, +5 authors Stefan Linder
Molecular biology of the cell
2006

Microtubules are important for the turnover of podosomes, dynamic, actin-rich adhesions implicated in migration and invasion of monocytic cells. The molecular basis for this functional dependency,… (More)

Subunit Interactions and cooperativity in the microtubule-severing AAA ATPase spastin.

Thomas Eckert, Susanne Link, +4 authors Guenther Woehlke
The Journal of biological chemistry
2012

Spastin is a hexameric ring AAA ATPase that severs microtubules. To see whether the ring complex funnels the energy of multiple ATP hydrolysis events to the site of mechanical action, we investigate… (More)

Importance of a flexible hinge near the motor domain in kinesin-driven motility.

Maika Grummt, Guenther Woehlke, Ulrike Henningsen, Sara Fuchs, Michael Schleicher, Manfred Schliwa
The EMBO journal
1998

Conventional kinesin is a molecular motor consisting of an N-terminal catalytic motor domain, an extended stalk and a small globular C-terminus. Whereas the structure and function of the catalytic… (More)

Unusual properties of the fungal conventional kinesin neck domain from Neurospora crassa.

Athina Kallipolitou, Dominga Deluca, +6 authors Guenther Woehlke
The EMBO journal
2001

Fungal conventional kinesins are unusually fast microtubule motor proteins. To compare the functional organization of fungal and animal conventional kinesins, a set of C-terminal deletion mutants of… (More)

Universal and unique features of kinesin motors: insights from a comparison of fungal and animal conventional kinesins.

Jochen Kirchner, Guenther Woehlke, Manfred Schliwa
Biological chemistry
1999

Kinesins are microtubule motors that use the energy derived from the hydrolysis of ATP to move unidirectionally along microtubules. The founding member of this still growing superfamily is… (More)

Structure of a fast kinesin: implications for ATPase mechanism and interactions with microtubules.

Yoo Han Song, Alexander Marx, +5 authors Eckhard Mandelkow
The EMBO journal
2001

We determined the crystal structure of the motor domain of the fast fungal kinesin from Neurospora crassa (NcKin). The structure has several unique features. (i) Loop 11 in the switch 2 region is… (More)

Molecular motors

Life implies movement. Most forms of movement in the living world are powered by tiny protein machines known as molecular motors. Among the best known are motors that use sophisticated intramolecular… (More)

Surface topography of microtubule walls decorated with monomeric and dimeric kinesin constructs.

Andreas H Hoenger, M Doerhoefer, +4 authors E. -M. Mandelkow
Biological chemistry
2000

The surface topography of opened-up microtubule walls (sheets) decorated with monomeric and dimeric kinesin motor domains was investigated by freeze-drying and unidirectional metal shadowing.… (More)

Kinetic and mechanistic basis of the nonprocessive Kinesin-3 motor NcKin3.

Sarah Adio, Marieke J. Bloemink, Michaela Hartel, Sven Leier, Michael A. Geeves, Guenther Woehlke
The Journal of biological chemistry
2006

Kinesin-3 motors have been shown to transport cellular cargo along microtubules and to function according to mechanisms that differ from the conventional hand-over-hand mechanism. To find out whether… (More)

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