Zobrazeno 1 - 10
of 11
pro vyhledávání: '"Madeline, Serr"'
Publikováno v:
Molecular Biology of the Cell. 14:1355-1365
Sequence comparisons and structural analyses show that the dynein heavy chain motor subunit is related to the AAA family of chaperone-like ATPases. The core structure of the dynein motor unit derives from the assembly of six AAA domains into a hexame
Autor:
Andre Silvanovich, Maura McGrail, Thomas S. Hays, Susan Ludmann, Madeline Serr, Janice Gepner
Publikováno v:
The Journal of Cell Biology
The Drosophila Glued gene product shares sequence homology with the p150 component of vertebrate dynactin. Dynactin is a multiprotein complex that stimulates cytoplasmic dynein-mediated vesicle motility in vitro. In this report, we present biochemica
Publikováno v:
The Journal of Cell Biology
The unidirectional movements of the microtubule-associated motors, dyneins, and kinesins, provide an important mechanism for the positioning of cellular organelles and molecules. An intriguing possibility is that this mechanism may underlie the direc
The dynein light intermediate chain (LIC) is a subunit unique to the cytoplasmic form of dynein, but how it contributes to dynein function is not fully understood. Previous work has established that the LIC homodimer binds directly to the dynein heav
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b3bca7e1a14015a07cd91e486d62e1d7
https://europepmc.org/articles/PMC2575169/
https://europepmc.org/articles/PMC2575169/
Publikováno v:
Molecular biology of the cell. 18(6)
In Drosophila, the asymmetric localization of specific mRNAs to discrete regions within the developing oocyte determines the embryonic axes. The microtubule motors dynein and kinesin are required for the proper localization of the determinant ribonuc
Lis1 is required for nuclear migration in fungi, cell cycle progression in mammals, and the formation of a folded cerebral cortex in humans. Lis1 binds dynactin and the dynein motor complex, but the role of Lis1 in many dynein/dynactin-dependent proc
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b6a2981c4a42a36ec089db454111d6a6
https://europepmc.org/articles/PMC1266413/
https://europepmc.org/articles/PMC1266413/
Autor:
Renata Basto, Frédéric Scaërou, Thomas S. Hays, Madeline Serr, Edward J. Wojcik, Roger E. Karess
Publikováno v:
Nature Cell Biology
Nature Cell Biology, Nature Publishing Group, 2001, 3 (11), pp.1001-1007. ⟨10.1038/ncb1101-1001⟩
Nature Cell Biology, Nature Publishing Group, 2001, 3 (11), pp.1001-1007. ⟨10.1038/ncb1101-1001⟩
We describe the dynamics of kinetochore dynein-dynactin in living Drosophila embryos and examine the effect of mutant dynein on the metaphase checkpoint. A functional conjugate of dynamitin with green fluorescent protein accumulates rapidly at promet
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::44ad8c165e27510ca0a156f76ccaf9c8
https://hal.archives-ouvertes.fr/hal-03453064
https://hal.archives-ouvertes.fr/hal-03453064
Publikováno v:
Molecular biology of the cell. 11(11)
The microtubule motor cytoplasmic dynein performs multiple cellular functions; however, the regulation and targeting of the motor to different cargoes is not well understood. A biochemical interaction between the dynein intermediate chain subunit and
Publikováno v:
Molecular biology of the cell. 5(1)
We report the identification and initial characterization of seven Drosophila dynein heavy chain genes. Each gene is single copy and maps to a unique genomic location. Sequence analysis of partial clones reveals that each encodes a highly conserved p
Publikováno v:
Molecular Biology of the Cell; July 2004, Vol. 15 Issue: 7 p3005-14, 10p