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Articles 31 - 33 of 33
Full-Text Articles in Life Sciences
Single-Particle Imaging Reveals Intraflagellar Transport–Independent Transport And Accumulation Of Eb1 In Chlamydomonas Flagella, J. Aaron Harris, Yi Liu, Pinfen Yang, Peter Kner, Karl F. Lechtreck
Single-Particle Imaging Reveals Intraflagellar Transport–Independent Transport And Accumulation Of Eb1 In Chlamydomonas Flagella, J. Aaron Harris, Yi Liu, Pinfen Yang, Peter Kner, Karl F. Lechtreck
Biological Sciences Faculty Research and Publications
The microtubule (MT) plus-end tracking protein EB1 is present at the tips of cilia and flagella; end-binding protein 1 (EB1) remains at the tip during flagellar shortening and in the absence of intraflagellar transport (IFT), the predominant protein transport system in flagella. To investigate how EB1 accumulates at the flagellar tip, we used in vivo imaging of fluorescent protein–tagged EB1 (EB1-FP) in Chlamydomonas reinhardtii. After photobleaching, the EB1 signal at the flagellar tip recovered within minutes, indicating an exchange with unbleached EB1 entering the flagella from the cell body. EB1 moved independent of IFT trains, and EB1-FP recovery did …
Copper Oxide Nanoparticles Inhibit The Metabolic Activity Of Saccharomyces Cerevisiae , Michael Joseph Mashock, Anthony D. Kappell, Nadia Hallaj, Krassimira R. Hristova
Copper Oxide Nanoparticles Inhibit The Metabolic Activity Of Saccharomyces Cerevisiae , Michael Joseph Mashock, Anthony D. Kappell, Nadia Hallaj, Krassimira R. Hristova
Biological Sciences Faculty Research and Publications
Copper oxide nanoparticles (CuO NPs) are used increasingly in industrial applications and consumer products and thus may pose risk to human and environmental health. The interaction of CuO NPs with complex media and the impact on cell metabolism when exposed to sublethal concentrations are largely unknown. In the present study, the short-term effects of 2 different sized manufactured CuO NPs on metabolic activity of Saccharomyces cerevisiae were studied. The role of released Cu2+ during dissolution of NPs in the growth media and the CuO nanostructure were considered. Characterization showed that the 28 nm and 64 nm CuO NPs used …
Myc-Binding Protein Orthologue Interacts With Akap240 In The Central Pair Apparatus Of The Chlamydomonas Flagella, Venkatramanan G. Rao, Ruhi B. Sarafdar, Twinkle S. Chowdhury, Priyanka Sivadas, Pinfen Yang, Prabhakar M. Dongre, Jacinta S. D'Souza
Myc-Binding Protein Orthologue Interacts With Akap240 In The Central Pair Apparatus Of The Chlamydomonas Flagella, Venkatramanan G. Rao, Ruhi B. Sarafdar, Twinkle S. Chowdhury, Priyanka Sivadas, Pinfen Yang, Prabhakar M. Dongre, Jacinta S. D'Souza
Biological Sciences Faculty Research and Publications
Background
Flagella and cilia are fine thread-like organelles protruding from cells that harbour them. The typical ‘9 + 2’ cilia confer motility on these cells. Although the mechanistic details of motility remain elusive, the dynein-driven motility is regulated by various kinases and phosphatases. A-kinase anchoring proteins (AKAPs) are scaffolds that bind to a variety of such proteins. Usually, they are known to possess a dedicated domain that in vitro interacts with the regulatory subunits (RI and RII) present in the cAMP-dependent protein kinase (PKA) holoenzyme. These subunits conventionally harbour contiguous stretches of a.a. residues that reveal the presence of the …