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Eg5 steps it up!
Understanding how molecular motors generate force and move microtubules in mitosis is essential to understanding the physical mechanism of cell division. Recent measurements have shown that one mitotic kinesin superfamily member, Eg5, is mechanically processive and capable of crosslinking and slidin...
| Autores principales: | , , |
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| Formato: | Texto |
| Lenguaje: | English |
| Publicado: |
BioMed Central
2006
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| Materias: | |
| Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1716758/ https://www.ncbi.nlm.nih.gov/pubmed/17173688 http://dx.doi.org/10.1186/1747-1028-1-31 |
| _version_ | 1782131326205296640 |
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| author | Valentine, Megan T Fordyce, Polly M Block, Steven M |
| author_facet | Valentine, Megan T Fordyce, Polly M Block, Steven M |
| author_sort | Valentine, Megan T |
| collection | PubMed |
| description | Understanding how molecular motors generate force and move microtubules in mitosis is essential to understanding the physical mechanism of cell division. Recent measurements have shown that one mitotic kinesin superfamily member, Eg5, is mechanically processive and capable of crosslinking and sliding microtubules in vitro. In this review, we highlight recent work that explores how Eg5 functions under load, with an emphasis on the nanomechanical properties of single enzymes. |
| format | Text |
| id | pubmed-1716758 |
| institution | National Center for Biotechnology Information |
| language | English |
| publishDate | 2006 |
| publisher | BioMed Central |
| record_format | MEDLINE/PubMed |
| spelling | pubmed-17167582006-12-23 Eg5 steps it up! Valentine, Megan T Fordyce, Polly M Block, Steven M Cell Div Review Understanding how molecular motors generate force and move microtubules in mitosis is essential to understanding the physical mechanism of cell division. Recent measurements have shown that one mitotic kinesin superfamily member, Eg5, is mechanically processive and capable of crosslinking and sliding microtubules in vitro. In this review, we highlight recent work that explores how Eg5 functions under load, with an emphasis on the nanomechanical properties of single enzymes. BioMed Central 2006-12-15 /pmc/articles/PMC1716758/ /pubmed/17173688 http://dx.doi.org/10.1186/1747-1028-1-31 Text en Copyright © 2006 Valentine et al; licensee BioMed Central Ltd. http://creativecommons.org/licenses/by/2.0 This is an Open Access article distributed under the terms of the Creative Commons Attribution License ( (http://creativecommons.org/licenses/by/2.0) ), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. |
| spellingShingle | Review Valentine, Megan T Fordyce, Polly M Block, Steven M Eg5 steps it up! |
| title | Eg5 steps it up! |
| title_full | Eg5 steps it up! |
| title_fullStr | Eg5 steps it up! |
| title_full_unstemmed | Eg5 steps it up! |
| title_short | Eg5 steps it up! |
| title_sort | eg5 steps it up! |
| topic | Review |
| url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1716758/ https://www.ncbi.nlm.nih.gov/pubmed/17173688 http://dx.doi.org/10.1186/1747-1028-1-31 |
| work_keys_str_mv | AT valentinemegant eg5stepsitup AT fordycepollym eg5stepsitup AT blockstevenm eg5stepsitup |