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Insights into dynein motor domain function from a 3.3 Å crystal structure
Dyneins power the beating of cilia and flagella, transport various intracellular cargos and are necessary for mitosis. All dyneins have a ∼300-kDa motor domain consisting of a ring of six AAA+Expand
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Dynein motors: How AAA+ ring opening and closing coordinates microtubule binding and linker movement
  • H. Schmidt
  • Biology, Medicine
  • BioEssays : news and reviews in molecular…
  • 1 May 2015
Dyneins are a family of motor proteins that move along the microtubule. Motility is generated in the motor domain, which consists of a ring of six AAA+ (ATPases associated with diverse cellularExpand
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Review: Structure and mechanism of the dynein motor ATPase
Dyneins are multiprotein complexes that move cargo along microtubules in the minus end direction. The largest individual component of the dynein complex is the heavy chain. Its C‐terminal 3500Expand
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A structural analysis of the AAA+ domains in Saccharomyces cerevisiae cytoplasmic dynein
Dyneins are large protein complexes that act as microtubule based molecular motors. The dynein heavy chain contains a motor domain which is a member of the AAA+ protein family (ATPases AssociatedExpand
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Responsiveness of subjective quality of life assessment in schizophrenic patients: a quasi-experimental pilot study.
Responsiveness of quality of life (QOL) assessments in chronic schizophrenic patients was investigated by a quasi-experimental pilot study. Satisfaction ratings were assessed over five time pointsExpand
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Mechanism and regulation of dynein motors
Abstract In this chapter, we describe the architecture and motility mechanism of the dynein motor. The two key aspects of dynein motility are the force producing linker power stroke and the cyclicExpand
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The Mechanism of Dynein's Minus End Directionality and an Engineered Plus End Directed Dynein Motor
Cytoplasmic dynein is responsible for nearly all minus-end directed transport along microtubules (MTs). However, little is known about how dynein achieves its directionality. Using an optical trap,Expand