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Kinesin's second step

We have identified dimeric kinesin mutants that become stalled on the microtubule after one ATP turnover, unable to bind and hydrolyze ATP at their second site. We have used these mutants to determine the regulatory signal that allows ATP to bind to the forward head, such that processive movement ca...

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Veröffentlicht in:Proc Natl Acad Sci U S A
Hauptverfasser: Klumpp, Lisa M., Hoenger, Andreas, Gilbert, Susan P.
Format: Artigo
Sprache:Inglês
Veröffentlicht: National Academy of Sciences 2004
Schlagworte:
Online-Zugang:https://ncbi.nlm.nih.govhttps://pmc.ncbi.nlm.nih.gov/articles/PMC373481/
https://ncbi.nlm.nih.govhttps://pubmed.ncbi.nlm.nih.gov/14985504/
https://ncbi.nlm.nih.govhttps://doi.org/10.1073/pnas.0307691101
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