Ishikawa T 2012 Dyneins are microtubule-based, ATP-driven motor proteins with six tandemly linked AAA+ domains, a long N-terminal tail and a coiled-coil stalk. Cytoplasmic dyneins function as individual homodimers and are responsible for minus-end-oriented transport along microtubules. Axonemal dyneins of flagella/cilia are anchored in arrays to peripheral microtubule doublets by their N-terminal tails, and generate sliding motions of adjacent microtubule doublets toward the plus end. The coiled-coil stalk is responsible for communication between the AAA+ domains and the microtubule binding domain. A number of isoforms of axonemal dyneins are integrated to generate bending motion. In this article I will review recent structural studies and address the question as to how dyneins generate force and cause bending in flagella/cilia. https://sonar.ch/global/documents/278452 eng info:eu-repo/semantics/altIdentifier/doi/10.1016/j.jsb.2012.05.016 info:eu-repo/semantics/altIdentifier/pmid/22664481 Journal of structural biology. - 2012 Axonemal Dyneins Crystallography, X-Ray Cytoplasm Dyneins Microscopy, Electron Structural biology of cytoplasmic and axonemal dyneins. http://purl.org/coar/resource_type/c_6501