M
Michael P. Koonce
Researcher at Wadsworth Center
Publications - 34
Citations - 2037
Michael P. Koonce is an academic researcher from Wadsworth Center. The author has contributed to research in topics: Microtubule & Dynein. The author has an hindex of 20, co-authored 34 publications receiving 1976 citations. Previous affiliations of Michael P. Koonce include State University of New York System & University at Albany, SUNY.
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Journal ArticleDOI
Cytoplasmic dynein plays a role in mammalian mitotic spindle formation.
TL;DR: The cloned and expressed DNA fragments that encode the putative ATP- hydrolytic sites of the cytoplasmic dynein heavy chain from HeLa cells and from Dictyostelium suggest that cytopsized dyne in plays a unique and important role in the initial events of bipolar spindle formation, while any later roles that it may play are redundant.
Journal ArticleDOI
Towards an in vivo biologically inspired nanofactory
Philip R. LeDuc,Michael S. Wong,Placid M. Ferreira,Richard E. Groff,Kiryn Haslinger,Michael P. Koonce,Woo Y. Lee,J. Christopher Love,J. Andrew McCammon,Nancy A. Monteiro-Riviere,Vincent M. Rotello,Gary W. Rubloff,Robert M. Westervelt,Minami Yoda +13 more
TL;DR: It may, however, be possible to go even further and design 'pseudo-cell' nanofactories that work with molecules already in the body to fight disease.
Journal ArticleDOI
The dynein heavy chain: structure, mechanics and evolution
David J. Asai,Michael P. Koonce +1 more
TL;DR: Structural features of dynein, including a track-binding site that is located at the tip of a long projection, and six nucleotide-binding modules that together form the globular head, suggest that dyneIn produces movement by a mechanism that is different from that used by the other motors.
Journal ArticleDOI
Structural characterization of a dynein motor domain
Montserrat Samsó,Michael Radermacher,Michael Radermacher,Joachim Frank,Joachim Frank,Michael P. Koonce,Michael P. Koonce +6 more
TL;DR: This is the first detailed description of the head domain structure for a dynein molecule, which shows the presence of a central cavity and the outer globular features, along with its large size make dyne in structurally distinct from either myosin or kinesin.
Journal ArticleDOI
Dynein from Dictyostelium: primary structure comparisons between a cytoplasmic motor enzyme and flagellar dynein.
TL;DR: The cloning and sequencing of a cytoplasmic dynein heavy chain gene from the cellular slime mold Dictyostelium discoideum is reported, which contains four GXXXXGKT/S motifs that form part of a consensus sequence for ATP-binding domains; these motifs are clustered near the middle of the polypeptide.