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  • Xinnan Wang, Dominic Winter, Ghazaleh Ashrafi, Julia Schlehe, Yao Liang Wong, Dennis Selkoe +4 others
  • 2011
Cells keep their energy balance and avoid oxidative stress by regulating mitochondrial movement, distribution, and clearance. We report here that two Parkinson's disease proteins, the Ser/Thr kinase PINK1 and ubiquitin ligase Parkin, participate in this regulation by arresting mitochondrial movement. PINK1 phosphorylates Miro, a component of the primary(More)
Kinesin motor proteins execute a variety of intracellular microtubule-based transport functions [1]. Kinesin motor domains contain a catalytic core, which is conserved throughout the kinesin superfamily, followed by a neck region, which is conserved within subfamilies and has been implicated in controlling the direction of motion along a microtubule [2](More)
Myosin-II thick filament formation in Dictyostelium is an excellent system for investigating the phenomenon of self-assembly, as the myosin molecule itself contains all the information required to form a structure of defined size. Phosphorylation of only three threonine residues can dramatically change the assembly state of myosin-II. We show here that the(More)
This study aimed to investigate whether endorsement of "difficulty coping" questions on two self-report measures would be affected by whether or not women had to put their name on the questionnaires. In addition, a small survey of mental health professionals was conducted to see what they thought the study would find. Women (n= 211) attending maternal and(More)
We have used site-directed spin-labeling and electron paramagnetic resonance spectroscopy to monitor a conformational change at the nucleotide site of kinesin. Cys-lite kinesin (K349 monomer) with the mutation S188C was spin labeled with MSL or MTSL. This residue is at the junction between the switch 1 region (which is a structure known to be sensitive to(More)
Figure 3C should have appeared as shown below. The GFP-AD-Cterm (3x Thr) and GFP-AD-Cterm (3x Asp) constructs are slightly less soluble than their headless counterparts. This may be due to the fact that they are somewhat more prone to aggregation over time than the headless proteins. The change does not affect the conclusions of the paper. Citation: (2005)(More)
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