Zobrazeno 1 - 10
of 18
pro vyhledávání: '"David E. Wilkes"'
Autor:
Jonathan A Eisen, Robert S Coyne, Martin Wu, Dongying Wu, Mathangi Thiagarajan, Jennifer R Wortman, Jonathan H Badger, Qinghu Ren, Paolo Amedeo, Kristie M Jones, Luke J Tallon, Arthur L Delcher, Steven L Salzberg, Joana C Silva, Brian J Haas, William H Majoros, Maryam Farzad, Jane M Carlton, Roger K Smith, Jyoti Garg, Ronald E Pearlman, Kathleen M Karrer, Lei Sun, Gerard Manning, Nels C Elde, Aaron P Turkewitz, David J Asai, David E Wilkes, Yufeng Wang, Hong Cai, Kathleen Collins, B Andrew Stewart, Suzanne R Lee, Katarzyna Wilamowska, Zasha Weinberg, Walter L Ruzzo, Dorota Wloga, Jacek Gaertig, Joseph Frankel, Che-Chia Tsao, Martin A Gorovsky, Patrick J Keeling, Ross F Waller, Nicola J Patron, J Michael Cherry, Nicholas A Stover, Cynthia J Krieger, Christina del Toro, Hilary F Ryder, Sondra C Williamson, Rebecca A Barbeau, Eileen P Hamilton, Eduardo Orias
Publikováno v:
PLoS Biology, Vol 4, Iss 9, p e286 (2006)
The ciliate Tetrahymena thermophila is a model organism for molecular and cellular biology. Like other ciliates, this species has separate germline and soma functions that are embodied by distinct nuclei within a single cell. The germline-like micron
Externí odkaz:
https://doaj.org/article/05012f5a3b544655a50cce2f034ce46a
Publikováno v:
Journal of Eukaryotic Microbiology. 63:138-141
Dynein heavy chains are motor proteins that comprise a large gene family found across eukaryotes. We have investigated this gene family in four ciliate species: Ichthyophthirius, Oxytricha, Paramecium, and Tetrahymena. Ciliates appear to encode more
Publikováno v:
Frontiers in Biology. 8:119-126
The dynein motor protein family is involved in a wide variety of functions in eukaryotic cells. The axonemal dynein class and cytoplasmic dynein-1 subclass have been well characterized. However, the cytoplasmic dynein-2 subclass of the family has onl
Publikováno v:
Cell Motility and the Cytoskeleton. 65:342-351
Dyneins are responsible for essential movements in eukaryotic cells. The motor activity of each dynein complex resides in its complement of heavy chains. In the present study, we examined 136 heavy chain sequences from the completed genomes of 11 div
Autor:
Ekaterina Kniazeva, David E. Wilkes, Alice E. Wiedeman, Vidyalakshmi Rajagopalan, Clarence W. C. Chan, David J. Asai
Publikováno v:
Cell Motility and the Cytoskeleton. 64:82-96
Dyneins are large protein complexes that produce directed movement on microtubules. In situ, dyneins comprise combinations of heavy, intermediate, light-intermediate, and light chains. The light chains regulate the locations and activities of dyneins
Autor:
David J. Asai, David E. Wilkes
Publikováno v:
The Journal of Eukaryotic Microbiology. 51:23-29
Dynein is the large molecular motor that translocates to the (-) ends of microtubules. Dynein was first isolated from Tetrahymena cilia four decades ago. The analysis of the primary structure of the dynein heavy chain and the discovery that many orga
Autor:
Michael W. Mather, Donna Cassidy-Hanley, Ujjwal Kumar, Hong Cai, Harry W. Dickerson, Chad G. Pearson, Justin Johnson, Jessica B. Hostetler, Jianying Gu, Dhanasekaran Shanmugam, Yufeng Wang, Yves Van de Peer, Irtisha Singh, David S. Roos, Martin Wu, Vidyalakshmi Rajagopalan, Linda Hannick, Vinita Joardar, Robert S. Coyne, Theodore G. Clark, Diana Radune, R. C. Findly, David E. Wilkes, Jonathan H. Badger, David J. Asai, Daniel Brami, Milton H. Saier, Akhil B. Vaidya, Cindy Martens
Publikováno v:
Genome Biology
Coyne, Robert S; Hannick, Linda; Shanmugam, Dhanasekaran; Hostetler, Jessica B; Brami, Daniel; Joardar, Vinita S; et al.(2011). Comparative genomics of the pathogenic ciliate Ichthyophthirius multifiliis, its free-living relatives and a host species provide insights into adoption of a parasitic lifestyle and prospects for disease control. Genome Biology, 12(10), R100. doi: http://dx.doi.org/10.1186/gb-2011-12-10-r100. Retrieved from: http://www.escholarship.org/uc/item/94n9s295
GENOME BIOLOGY
Coyne, Robert S; Hannick, Linda; Shanmugam, Dhanasekaran; Hostetler, Jessica B; Brami, Daniel; Joardar, Vinita S; et al.(2011). Comparative genomics of the pathogenic ciliate Ichthyophthirius multifiliis, its free-living relatives and a host species provide insights into adoption of a parasitic lifestyle and prospects for disease control. Genome Biology, 12(10), R100. doi: http://dx.doi.org/10.1186/gb-2011-12-10-r100. Retrieved from: http://www.escholarship.org/uc/item/94n9s295
GENOME BIOLOGY
Background Ichthyophthirius multifiliis, commonly known as Ich, is a highly pathogenic ciliate responsible for 'white spot', a disease causing significant economic losses to the global aquaculture industry. Options for disease control are extremely l
Autor:
David E, Wilkes, Nicole, Bennardo, Clarence W C, Chan, Yu-Loung, Chang, Elizabeth O, Corpuz, Jennifer, DuMond, Jordan A, Eboreime, Julianna, Erickson, Jonathan, Hetzel, Erin E, Heyer, Mark J, Hubenschmidt, Ekaterina, Kniazeva, Hallie, Kuhn, Michelle, Lum, Andrea, Sand, Alicia, Schep, Oksana, Sergeeva, Natt, Supab, Caroline R, Townsend, Liesl Van, Ryswyk, Hadley E, Watson, Alice E, Wiedeman, Vidyalakshmi, Rajagopalan, David J, Asai
Publikováno v:
Methods in cell biology. 92
We describe the protocol through which we identify and characterize dynein subunit genes in the ciliated protozoan Tetrahymena thermophila. The gene(s) of interest is found by searching the Tetrahymena genome, and it is characterized in silico includ
Autor:
Vidyalakshmi, Rajagopalan, Elizabeth O, Corpuz, Mark J, Hubenschmidt, Caroline R, Townsend, David J, Asai, David E, Wilkes
Publikováno v:
Methods in molecular biology (Clifton, N.J.). 586
Cilia and eukaryotic flagella are important structures required for the motility of cells, the movement of medium across the surfaces of cells, and the connections between the receptor and synthetic portions of sensory cells. The axoneme forms the cy
Publikováno v:
Cell motility and the cytoskeleton. 66(8)
Dynein-2 is the motor responsible for retrograde intraflagellar transport. In situ, dynein-2 comprises four subunits: the dynein-2 heavy chain (DYH2); the dynein-2 intermediate chain; the dynein-2 light-intermediate chain (D2LIC); and dynein light ch