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Relevant bibliographies by topics / Dynein

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Academic literature on the topic 'Dynein'

Author: Grafiati

Published: 4 June 2021

Last updated: 25 July 2025

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Journal articles on the topic "Dynein"

1

Jha, Rupam, and Thomas Surrey. "Regulation of processive motion and microtubule localization of cytoplasmic dynein." Biochemical Society Transactions 43, no. 1 (2015): 48–57. http://dx.doi.org/10.1042/bst20140252.

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The cytoplasmic dynein complex is the major minus-end-directed microtubule motor. Although its directionality is evolutionary well conserved, differences exist among cytoplasmic dyneins from different species in their stepping behaviour, maximum velocity and force production. Recent experiments also suggest differences in processivity regulation. In the present article, we give an overview of dynein's motile properties, with a special emphasis on processivity and its regulation. Furthermore, we summarize recent findings of different pathways for microtubule plus-end loading of dynein. The pres

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Ishibashi, Kenta, Hitoshi Sakakibara, and Kazuhiro Oiwa. "Force-Generating Mechanism of Axonemal Dynein in Solo and Ensemble." International Journal of Molecular Sciences 21, no. 8 (2020): 2843. http://dx.doi.org/10.3390/ijms21082843.

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In eukaryotic cilia and flagella, various types of axonemal dyneins orchestrate their distinct functions to generate oscillatory bending of axonemes. The force-generating mechanism of dyneins has recently been well elucidated, mainly in cytoplasmic dyneins, thanks to progress in single-molecule measurements, X-ray crystallography, and advanced electron microscopy. These techniques have shed light on several important questions concerning what conformational changes accompany ATP hydrolysis and whether multiple motor domains are coordinated in the movements of dynein. However, due to the lack o

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Rao, Lu, and Arne Gennerich. "Structure and Function of Dynein’s Non-Catalytic Subunits." Cells 13, no. 4 (2024): 330. http://dx.doi.org/10.3390/cells13040330.

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Dynein, an ancient microtubule-based motor protein, performs diverse cellular functions in nearly all eukaryotic cells, with the exception of land plants. It has evolved into three subfamilies—cytoplasmic dynein-1, cytoplasmic dynein-2, and axonemal dyneins—each differentiated by their cellular functions. These megadalton complexes consist of multiple subunits, with the heavy chain being the largest subunit that generates motion and force along microtubules by converting the chemical energy of ATP hydrolysis into mechanical work. Beyond this catalytic core, the functionality of dynein is signi

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Yoshida, T., H. Takanari, and K. Izutsu. "Distribution of cytoplasmic and axonemal dyneins in rat tissues." Journal of Cell Science 101, no. 3 (1992): 579–87. http://dx.doi.org/10.1242/jcs.101.3.579.

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Microtubule-associated protein 1C (MAP 1C) is now defined as brain cytoplasmic dynein. Recent studies have suggested that cytoplasmic dynein is a motor protein responsible for the intracellular microtubule-based motility in neuronal and non-neuronal cells. We have prepared an antibody against bovine brain MAP 1C and have examined the localizations of cytoplasmic dynein in rat tissues. Immunoblots of extracts from the tissues showed that the dynein was present in brain, testis, liver, kidney and lung. Immunohistochemical experiments have demonstrated that dynein is localized in Purkinje cells o

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Vale, R. D., and Y. Y. Toyoshima. "Microtubule translocation properties of intact and proteolytically digested dyneins from Tetrahymena cilia." Journal of Cell Biology 108, no. 6 (1989): 2327–34. http://dx.doi.org/10.1083/jcb.108.6.2327.

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Tetrahymena cilia contain a three-headed 22S (outer arm) dynein and a single-headed 14S dynein. In this study, we have employed an in vitro assay of microtubule translocation along dynein-coated glass surfaces to characterize the motile properties of 14S dynein, 22S dynein, and proteolytic fragments of 22S dynein. Microtubule translocation produced by intact 22S dynein and 14S dynein differ in a number of respects including (a) the maximal velocities of movement; (b) the ability of 22S dynein but not 14S dynein to utilize ATP gamma S to induce movement; (c) the optimal pH and ionic conditions

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Sanghavi, Paulomi, Pankaj Kumar, Ankit Roy, M. S. Madhusudhan, and Roop Mallik. "On and off controls within dynein–dynactin on native cargoes." Proceedings of the National Academy of Sciences 118, no. 23 (2021): e2103383118. http://dx.doi.org/10.1073/pnas.2103383118.

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The dynein–dynactin nanomachine transports cargoes along microtubules in cells. Why dynactin interacts separately with the dynein motor and also with microtubules is hotly debated. Here we disrupted these interactions in a targeted manner on phagosomes extracted from cells, followed by optical trapping to interrogate native dynein–dynactin teams on single phagosomes. Perturbing the dynactin–dynein interaction reduced dynein’s on rate to microtubules. In contrast, perturbing the dynactin–microtubule interaction increased dynein’s off rate markedly when dynein was generating force against the op

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Yamamoto, Ryosuke, Kangkang Song, Haru-aki Yanagisawa, et al. "The MIA complex is a conserved and novel dynein regulator essential for normal ciliary motility." Journal of Cell Biology 201, no. 2 (2013): 263–78. http://dx.doi.org/10.1083/jcb.201211048.

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Axonemal dyneins must be precisely regulated and coordinated to produce ordered ciliary/flagellar motility, but how this is achieved is not understood. We analyzed two Chlamydomonas reinhardtii mutants, mia1 and mia2, which display slow swimming and low flagellar beat frequency. We found that the MIA1 and MIA2 genes encode conserved coiled-coil proteins, FAP100 and FAP73, respectively, which form the modifier of inner arms (MIA) complex in flagella. Cryo–electron tomography of mia mutant axonemes revealed that the MIA complex was located immediately distal to the intermediate/light chain compl

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Asai, D. J., S. M. Beckwith, K. A. Kandl, H. H. Keating, H. Tjandra, and J. D. Forney. "The dynein genes of Paramecium tetraurelia. Sequences adjacent to the catalytic P-loop identify cytoplasmic and axonemal heavy chain isoforms." Journal of Cell Science 107, no. 4 (1994): 839–47. http://dx.doi.org/10.1242/jcs.107.4.839.

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Paramecium tetraurelia is a unicellular organism that utilizes both axonemal and cytoplasmic dyneins. The highly conserved region containing the catalytic P-loop of the dynein heavy chain was amplified by RNA-directed polymerase chain reaction. Eight different P-loop-containing cDNA fragments were cloned. Southern hybridization analysis indicated that each fragment corresponds to a separate dynein gene and that there are at least 12 dynein heavy chain genes expressed in Paramecium. Seven of the eight cloned contain sequence motif A, which is found in axonemal dyneins, and one contains sequence

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Canty, John T., Ruensern Tan, Emre Kusakci, Jonathan Fernandes, and Ahmet Yildiz. "Structure and Mechanics of Dynein Motors." Annual Review of Biophysics 50, no. 1 (2021): 549–74. http://dx.doi.org/10.1146/annurev-biophys-111020-101511.

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Dyneins make up a family of AAA+ motors that move toward the minus end of microtubules. Cytoplasmic dynein is responsible for transporting intracellular cargos in interphase cells and mediating spindle assembly and chromosome positioning during cell division. Other dynein isoforms transport cargos in cilia and power ciliary beating. Dyneins were the least studied of the cytoskeletal motors due to challenges in the reconstitution of active dynein complexes in vitro and the scarcity of high-resolution methods for in-depth structural and biophysical characterization of these motors. These challen

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Roberts, Anthony J. "Emerging mechanisms of dynein transport in the cytoplasm versus the cilium." Biochemical Society Transactions 46, no. 4 (2018): 967–82. http://dx.doi.org/10.1042/bst20170568.

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Two classes of dynein power long-distance cargo transport in different cellular contexts. Cytoplasmic dynein-1 is responsible for the majority of transport toward microtubule minus ends in the cell interior. Dynein-2, also known as intraflagellar transport dynein, moves cargoes along the axoneme of eukaryotic cilia and flagella. Both dyneins operate as large ATP-driven motor complexes, whose dysfunction is associated with a group of human disorders. But how similar are their mechanisms of action and regulation? To examine this question, this review focuses on recent advances in dynein-1 and -2

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Dissertations / Theses on the topic "Dynein"

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Malkova, Barbora. "Structural studies of cytoplasmic dynein." Thesis, University of Leeds, 2010. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.540206.

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Liu, Siming. "TESTING THE MULTI-DYNEIN HYPOTHESIS BY MUTATING INNER ARM DYNEIN HEAVY CHAINS IN TETRAHYMENA THERMOPHILA." Miami University / OhioLINK, 2004. http://rave.ohiolink.edu/etdc/view?acc_num=miami1077152822.

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Villemant, Cecile Madeleine. "Investigating dynein light intermediate chains function." Thesis, University of Manchester, 2010. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.518455.

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Kardon, Julia R. "Regulation of the cytoplasmic dynein motor." Diss., Search in ProQuest Dissertations & Theses. UC Only, 2009. http://gateway.proquest.com/openurl?url_ver=Z39.88-2004&rft_val_fmt=info:ofi/fmt:kev:mtx:dissertation&res_dat=xri:pqdiss&rft_dat=xri:pqdiss:3359552.

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Gleave, Emma Sarah. "Structural and single-molecule studies of the cytoplasmic dynein motor domain." Thesis, University of Cambridge, 2014. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.708182.

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Diamant, Aristides G. "The structure of the cytoplasmic dynein tail." Thesis, University of Cambridge, 2015. https://www.repository.cam.ac.uk/handle/1810/249014.

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Cytoplasmic dynein is a molecular motor that moves cargos along microtubules. Dynein, together with its large co-factor dynactin, is responsible for the vast majority of traffic towards the centre of the cell. The largest subunit of the dynein complex is called the dynein heavy chain (DHC). The DHC includes a C-terminal motor domain, which converts ATP hydrolysis into mechanical force, an N-terminal tail domain, and a flexible linker domain to join the two together. An intermediate chain (DIC) and light intermediate chain (DLIC) bind directly to the DHC tail, while light chains (DLCs) bind to

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Roberts, Anthony John. "Structural studies on the mechanism of dynein." Thesis, University of Leeds, 2009. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.511146.

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Lo, Wai Hong. "Biochemical, structural and functional characterization of the light chains of the microtubule-based motor dynein /." View Abstract or Full-Text, 2003. http://library.ust.hk/cgi/db/thesis.pl?BICH%202003%20LO.

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Thesis (Ph. D.)--Hong Kong University of Science and Technology, 2003.<br>Includes bibliographical references (leaves 133-154). Also available in electronic version. Access restricted to campus users.

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Nyarko, Afua A. "Structure and interactions of subunits of cytoplasmic dynein /." View abstract, 2005. http://gateway.proquest.com/openurl?url_ver=Z39.88-2004&res_dat=xri:pqdiss&rft_val_fmt=info:ofi/fmt:kev:mtx:dissertation&rft_dat=xri:pqdiss:3191709.

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Nettesheim, Guilherme, Rafael A. Longoria, Allyson M. Rice, and George T. Shubeita. "Kinesin and dynein respond differently to cytoplasmic drag." Universitätsbibliothek Leipzig, 2015. http://nbn-resolving.de/urn:nbn:de:bsz:15-qucosa-182714.

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Books on the topic "Dynein"

1

Markus, Steven M., ed. Dynein. Springer US, 2023. http://dx.doi.org/10.1007/978-1-0716-2958-1.

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King, Stephen M. Dyneins: Structure, biology and disease. Academic Press, 2012.

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Khobrekar, Noopur V. Novel Functions for Dynein Adaptor RILP in Neuronal Autophagy. [publisher not identified], 2021.

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Hu, Daniel Jun-Kit. Roles for Cytoplasmic Dynein and the Unconventional Kinesin, KIF1a, during Cortical Development. [publisher not identified], 2015.

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Kemal, Shahrnaz. Distinct Roles for Dynein Regulatory Proteins NudE and NudEL in Brain Development. [publisher not identified], 2013.

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Weil, Sarah J. Novel Regulatory Mechanisms of Cytoplasmic Dynein: A Role for the Complex Base. [publisher not identified], 2013.

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Villarin, Joseph Manuel. Regulation of Cytoplasmic Dynein via Local Synthesis of its Cofactors, Lis1 and p150Glued. [publisher not identified], 2016.

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8

Freidlin, Mark I., ed. The Dynkin Festschrift. Birkhäuser Boston, 1994. http://dx.doi.org/10.1007/978-1-4612-0279-0.

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Urabe, Tohsuke. Dynkin Graphs and Quadrilateral Singularities. Springer Berlin Heidelberg, 1993. http://dx.doi.org/10.1007/bfb0084369.

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Urabe, Tohsuke. Dynkin graphs and quadrilateral singularities. Springer-Verlag, 1993.

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Book chapters on the topic "Dynein"

1

Lau, Clinton K. "Reconstitution of Dynein/Dynactin Transport Using Recombinant Dynein." In Methods in Molecular Biology. Springer US, 2023. http://dx.doi.org/10.1007/978-1-0716-2958-1_9.

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Oiwa, Kazuhiro. "Dynein Motility: Mechanism." In Encyclopedia of Biophysics. Springer Berlin Heidelberg, 2020. http://dx.doi.org/10.1007/978-3-642-35943-9_752-1.

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Oiwa, Kazuhiro. "Dynein Motility: Mechanism." In Encyclopedia of Biophysics. Springer Berlin Heidelberg, 2013. http://dx.doi.org/10.1007/978-3-642-16712-6_752.

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Diamant, Aristides G., and Andrew P. Carter. "Dynein Family Classification." In Encyclopedia of Biophysics. Springer Berlin Heidelberg, 2013. http://dx.doi.org/10.1007/978-3-642-16712-6_765.

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Cordova, Nicolas J., Ronald D. Vale, and George F. Oster. "Dynein-Microtubule Interactions." In Biologically Inspired Physics. Springer US, 1991. http://dx.doi.org/10.1007/978-1-4757-9483-0_19.

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Pfister, K. K. "Dynein." In Encyclopedia of Biological Chemistry. Elsevier, 2013. http://dx.doi.org/10.1016/b978-0-12-378630-2.00424-2.

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"Dynein." In Encyclopedia of Genetics, Genomics, Proteomics and Informatics. Springer Netherlands, 2008. http://dx.doi.org/10.1007/978-1-4020-6754-9_4972.

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Pfister, K. Kevin. "Dynein." In Encyclopedia of Biological Chemistry. Elsevier, 2004. http://dx.doi.org/10.1016/b0-12-443710-9/00188-5.

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Gibbons, Ian R. "Dynein, axonemal." In Guidebook to the Cytoskeletal and Motor Proteins. Oxford University PressOxford, 1999. http://dx.doi.org/10.1093/oso/9780198599579.003.00117.

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Abstract Axonemal dynein forms a double row of projections, the outer and inner arms, that are attached to the A tubule of each axonemal doublet and extend toward the B tubule of the adjacent doublet.10 The outer dynein arms are distributed along the length of the A tubule, with a constant spacing of 24 nm. The arrangement of inner dynein arms is more complex, with three distinct species of inner arm that are distributed along each A tubule in unevenly spaced triplets.

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Vallee, Richard. "Dynein, cytoplasmic." In Guidebook to the Cytoskeletal and Motor Proteins. Oxford University PressOxford, 1999. http://dx.doi.org/10.1093/oso/9780198599579.003.00118.

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Abstract Cytoplasmic dynein is a large, two-headed ATPase which produces force along microtubules in the retrograde direction (toward the microtubufe minus end). It is involved in a wide range of functions, including retrograde axonal transport and mitosis, and it associates with numerous subcellular structures, including kinetochores and a variety of membrane-bounded organelles.

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Conference papers on the topic "Dynein"

1

Lin, Mi, Kaixin Wang, Zewei Lin, et al. "HexSR-DyNeRF: HexPlane-based super-resolution dynamic neural radiance fields." In Second Advanced Imaging and Information Processing Conference (AIIP 2024), edited by Xinzhu Sang. SPIE, 2024. http://dx.doi.org/10.1117/12.3046480.

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Tang, Ziyu, Xiren Zhou, Shikang Liu, Chuyang Wei, Ao Chen, and Huanhuan Chen. "Learning in the Model Space: Fault Diagnosis by Co-objective Learning in DynInt Model Space." In ICASSP 2025 - 2025 IEEE International Conference on Acoustics, Speech and Signal Processing (ICASSP). IEEE, 2025. https://doi.org/10.1109/icassp49660.2025.10889439.

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"Simple qualitative deterministic model of dynein." In Engineering Mechanics 2018. Institute of Theoretical and Applied Mechanics of the Czech Academy of Sciences, 2018. http://dx.doi.org/10.21495/91-8-717.

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Chen, Duanduan, Kyosuke Shinohara, Jun Ren, and Hiroshi Hamada. "The Protein-Driven Ciliary Motility in Embryonic Nodes: A Computational Model of Ciliary Ultrastructure." In ASME 2013 International Mechanical Engineering Congress and Exposition. American Society of Mechanical Engineers, 2013. http://dx.doi.org/10.1115/imece2013-62460.

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The movement of embryonic cilia presents a crucial function in specifying left-right axis for vertebrates. Those mono-cilia are primary (9+0) cilia, whose characteristic architecture is based on a cylindrical arrangement of 9 microtubule doublets. Dynein motors located between adjacent doublets convert the chemical energy of ATP hydrolysis into mechanical work that induces doublet sliding. Passive components, such as the mediated cytoplasm, the ciliary membrane, and other possibly-existent structures constraint the ciliary motion and maintain the cilia structural integrity, thus resulting in t

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Xu, Gang, Kate S. Wilson, Ruth J. Okamoto, Jin-Yu Shao, Susan K. Dutcher, and Philip V. Bayly. "The Apparent Flexural Rigidity of the Flagellar Axoneme Depends on Resistance to Inter-Doublet Sliding." In ASME 2012 Summer Bioengineering Conference. American Society of Mechanical Engineers, 2012. http://dx.doi.org/10.1115/sbc2012-80220.

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Cilia are thin subcellular organelles that bend actively to propel fluid. The ciliary cytoskeleton (the axoneme) consists of nine outer microtubule doublets surrounding a central pair of singlet microtubules. Large bending deformations of the axoneme involve relative sliding of the outer doublets, driven by the motor protein dynein. Ciliary structure and function have been studied extensively, but details of the mechanics and coordination of the axoneme remain unclear. In particular, dynein activity must be switched on and off at specific times and locations to produce an oscillatory, propulsi

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Ueno, H., T. Yasunaga, C. Shingyoji, T. Yamaguchi, and K. Hirose. "Dynein Pulls Microtubules Without Rotating Its Stalk." In ASME 2009 Summer Bioengineering Conference. American Society of Mechanical Engineers, 2009. http://dx.doi.org/10.1115/sbc2009-206430.

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Dynein is a motor protein that hydrolyses ATP and moves toward the minus end of a microtubule (MT). A dynein molecule has one to three heavy chains, each consisting of three domains: a head, a stalk and a tail. ATP is bound and hydrolysed in the head, which has a ring-like structure composed of 6 AAA+ domains. The stalk is an antiparallel coiled-coil, 10–15 nm long, and has a nucleotide-dependent MT-binding domain at the tip (1) (Fig. 1). It has been proposed that the nucleotide-dependent binding affinity of the tubulin-binding site at the tip of the stalk is modulated by the two alpha helices

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Anders, K. L., K. B. R. Belchamber, D. C. A. Gaboriau, P. J. Barnes, and L. E. Donnelly. "Dynein Has Defective Activity in COPD Macrophage Phagocytosis." In American Thoracic Society 2019 International Conference, May 17-22, 2019 - Dallas, TX. American Thoracic Society, 2019. http://dx.doi.org/10.1164/ajrccm-conference.2019.199.1_meetingabstracts.a3779.

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Bayly, Philip V., and Kate S. Wilson. "Unstable Oscillations and Wave Propagation in Flagella." In ASME 2015 International Design Engineering Technical Conferences and Computers and Information in Engineering Conference. American Society of Mechanical Engineers, 2015. http://dx.doi.org/10.1115/detc2015-46920.

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Flagella are active, beam-like, sub-cellular organelles that use wavelike oscillations to propel the cell. The mechanisms underlying the coordinated beating of flagella remain incompletely understood despite the fundamental importance of these organelles. The axoneme (the cytoskeletal structure of flagella) consists of microtubule doublets connected by passive and active elements. The motor protein dynein is known to drive active bending, but dynein activity must be regulated to generate oscillatory, propulsive waveforms. Mathematical models of flagella motion generate quantitative predictions

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anders, katie, Kylie BR Belchamber, Peter J. Barnes, and Louise E. Donnelly. "Inhibition of dynein motors improves macrophage phagocytosis in COPD." In ERS International Congress 2017 abstracts. European Respiratory Society, 2017. http://dx.doi.org/10.1183/1393003.congress-2017.pa981.

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Ashikari, N., Y. Shitaka, H. Sakaue, et al. "Quantitative characterization of guided motion of dynein-microtubule system." In 2011 International Conference on Solid State Devices and Materials. The Japan Society of Applied Physics, 2011. http://dx.doi.org/10.7567/ssdm.2011.p-11-1.

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Reports on the topic "Dynein"

1

Song, Chunying. Role of Dynein Light Chain 1 in Tamoxifen Resistance in Breast Cancer. Defense Technical Information Center, 2007. http://dx.doi.org/10.21236/ada469357.

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King, Megan, and Mark Lemmon. The Role of Dynamin in the Regulation of Signaling by the erbB Family of Receptor Tyrosine Kinases. Defense Technical Information Center, 2003. http://dx.doi.org/10.21236/ada416747.

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Avni, Adi, and Gitta L. Coaker. Proteomic investigation of a tomato receptor like protein recognizing fungal pathogens. United States Department of Agriculture, 2015. http://dx.doi.org/10.32747/2015.7600030.bard.

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Maximizing food production with minimal negative effects on the environment remains a long-term challenge for sustainable food production. Microbial pathogens cause devastating diseases, minimizing crop losses by controlling plant diseases can contribute significantly to this goal. All plants possess an innate immune system that is activated after recognition of microbial-derived molecules. The fungal protein Eix induces defense responses in tomato and tobacco. Plants recognize Eix through a leucine-rich-repeat receptor- like-protein (LRR-RLP) termed LeEix. Despite the knowledge obtained from

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Health hazard evaluation report: HETA-83-307-1561, U.S. Environmental Protection Agency, Chem-Dyne Hazardous Waste Site, Hamilton, Ohio. U.S. Department of Health and Human Services, Public Health Service, Centers for Disease Control, National Institute for Occupational Safety and Health, 1985. http://dx.doi.org/10.26616/nioshheta833071561.

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