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Sim-D: A SIMD Accelerator for Hard Real-Time Systems

Autor: Spliet, R, Mullins, RD

Emerging safety-critical systems require high-performance data-parallel architectures and, problematically, ones that can guarantee tight and safe worst-case execution times. Given the complexity of existing architectures like GPUs, it is unlikely th

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8abd20a404faaabf580ff14c47210760
https://www.repository.cam.ac.uk/handle/1810/318427

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A novel tropomyosin isoform functions at the mitotic spindle and Golgi in Drosophila

Autor: Goins, LM, Mullins, RD

Publikováno v: Molecular biology of the cell, vol 26, iss 13
Goins, LM; & Mullins, RD. (2015). A novel tropomyosin isoform functions at the mitotic spindle and Golgi in Drosophila. Molecular Biology of the Cell, 26(13), 2491-2504. doi: 10.1091/mbc.E14-12-1619. UCSF: Retrieved from: http://www.escholarship.org/uc/item/3px2m3t0

© 2015 Goins and Mullins. Most eukaryotic cells express multiple isoforms of the actin-binding protein tropomyosin that help construct a variety of cytoskeletal networks. Only one nonmuscle tropomyosin (Tm1A) has previously been described in Drosoph

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=dedup_wf_001::193d6186c50c17626147b2b12dd261a2
https://escholarship.org/uc/item/3px2m3t0

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aE-catenin actin-binding domain alters actin filament conformation and regulates binding of nucleation and disassembly factors

Autor: Mullins, RD, Hansen, SD, Kwiatkowski, AV, Ouyang, CY, Liu, H, Pokutta, S, Watkins, SC, Volkmann, N, Hanein, D, Weis, WI, Nelson, WJ

Publikováno v: Mullins, RD; Hansen, SD; Kwiatkowski, AV; Ouyang, CY; Liu, H; Pokutta, S; et al.(2013). aE-catenin actin-binding domain alters actin filament conformation and regulates binding of nucleation and disassembly factors.. Molecular biology of the cell, 24(23). UC San Francisco: Retrieved from: http://www.escholarship.org/uc/item/7vg7g8q1

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=od_______325::97f3d4adaf69c816fb3dc799dbabd4d0
http://www.escholarship.org/uc/item/7vg7g8q1

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Arp2/3 complex ATP hydrolysis promotes lamellipodial actin network disassembly but is dispensable for assembly

Autor: Mullins, Roland, Ingerman, E, Hsiao, JY, Mullins, RD

Publikováno v: Mullins, Roland; Ingerman, E; Hsiao, JY; & Mullins, RD. (2013). Arp2/3 complex ATP hydrolysis promotes lamellipodial actin network disassembly but is dispensable for assembly. UC San Francisco: Retrieved from: http://www.escholarship.org/uc/item/3x89n633

We examined the role of ATP hydrolysis by the Arp2/3 complex in building the leading edge of a cell by studying the effects of hydrolysis defects on the behavior of the complex in the lamellipodial actin network of Drosophila S2 cells and in a recons

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=od_______325::5c1a6bd476ce4096517e801472a52387
http://www.escholarship.org/uc/item/3x89n633

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The instability of stabilization

Autor: Mullins, RD

Publikováno v: Mullins, RD. (2012). The instability of stabilization. Proceedings of the National Academy of Sciences of the United States of America, 109(27), 10743-10744. doi: 10.1073/pnas.1207980109. UC San Francisco: Retrieved from: http://www.escholarship.org/uc/item/3jx450mr

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=od_______325::327007b05a7a5e9b54f6ac6871d2b2a0
http://www.escholarship.org/uc/item/3jx450mr

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The instability of stabilization

Autor: Mullins Rd

Actin filaments and microtubules control the shape of cells and organize their contents. The proteins that form these cytoskeletal polymers were identified and isolated decades ago—actin in 1942 (1) and tubulin in 1968 (2)—but we still argue abou

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::709d4071908421f86af826233a3abbe1
https://europepmc.org/articles/PMC3390836/

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