Search Results - "Ramdzan, Yasmin M"

Huntingtin Inclusions Trigger Cellular Quiescence, Deactivate Apoptosis, and Lead to Delayed Necrosis by Ramdzan, Yasmin M., Trubetskov, Mikhail M., Ormsby, Angelique R., Newcombe, Estella A., Sui, Xiaojing, Tobin, Mark J., Bongiovanni, Marie N., Gras, Sally L., Dewson, Grant, Miller, Jason M.L., Finkbeiner, Steven, Moily, Nagaraj S., Niclis, Jonathan, Parish, Clare L., Purcell, Anthony W., Baker, Michael J., Wilce, Jacqueline A., Waris, Saboora, Stojanovski, Diana, Böcking, Till, Ang, Ching-Seng, Ascher, David B., Reid, Gavin E., Hatters, Danny M.

“…Competing models exist in the literature for the relationship between mutant Huntingtin exon 1 (Httex1) inclusion formation and toxicity. In one, inclusions…”
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Tadpole-like Conformations of Huntingtin Exon 1 Are Characterized by Conformational Heterogeneity that Persists regardless of Polyglutamine Length by Newcombe, Estella A., Ruff, Kiersten M., Sethi, Ashish, Ormsby, Angelique R., Ramdzan, Yasmin M., Fox, Archa, Purcell, Anthony W., Gooley, Paul R., Pappu, Rohit V., Hatters, Danny M.

“…Soluble huntingtin exon 1 (Httex1) with expanded polyglutamine (polyQ) engenders neurotoxicity in Huntington's disease. To uncover the physical basis of this…”
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Tracking Mutant Huntingtin Aggregation Kinetics in Cells Reveals Three Major Populations That Include an Invariant Oligomer Pool by Olshina, Maya A., Angley, Lauren M., Ramdzan, Yasmin M., Tang, Jinwei, Bailey, Michael F., Hill, Andrew F., Hatters, Danny M.

“…Huntington disease is caused by expanded polyglutamine sequences in huntingtin, which procures its aggregation into intracellular inclusion bodies (IBs)…”
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Transcriptional profiles for distinct aggregation states of mutant Huntingtin exon 1 protein unmask new Huntington's disease pathways by Moily, Nagaraj S., Ormsby, Angelique R., Stojilovic, Aleksandar, Ramdzan, Yasmin M., Diesch, Jeannine, Hannan, Ross D., Zajac, Michelle S., Hannan, Anthony J., Oshlack, Alicia, Hatters, Danny M.

“…Huntington's disease is caused by polyglutamine (polyQ)-expansion mutations in the CAG tandem repeat of the Huntingtin gene. The central feature of…”
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Tracking protein aggregation and mislocalization in cells with flow cytometry by Ramdzan, Yasmin M, Polling, Saskia, Chia, Cheryl P Z, Ng, Ivan H W, Ormsby, Angelique R, Croft, Nathan P, Purcell, Anthony W, Bogoyevitch, Marie A, Ng, Dominic C H, Gleeson, Paul A, Hatters, Danny M

“…Protein localization changes in cells are monitored at high-throughput applying pulse-shape analysis to flow-cytometry data. The authors use the technique in…”
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Misfolded Polyglutamine, Polyalanine, and Superoxide Dismutase 1 Aggregate via Distinct Pathways in the Cell by Polling, Saskia, Mok, Yee-Foong, Ramdzan, Yasmin M., Turner, Bradley J., Yerbury, Justin J., Hill, Andrew F., Hatters, Danny M.

“…Protein aggregation into intracellular inclusions is a key feature of many neurodegenerative disorders. A common theme has emerged that inappropriate…”
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A Platform to View Huntingtin Exon 1 Aggregation Flux in the Cell Reveals Divergent Influences from Chaperones hsp40 and hsp70 by Ormsby, Angelique R., Ramdzan, Yasmin M., Mok, Yee-Foong, Jovanoski, Kristijan D., Hatters, Danny M.

“…Our capacity for tracking how misfolded proteins aggregate inside a cell and how different aggregation states impact cell biology remains enigmatic. To address…”
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High‐Throughput Quantitation of Intracellular Trafficking and Organelle Disruption by Flow Cytometry by Chia, Pei Zhi Cheryl, Ramdzan, Yasmin M., Houghton, Fiona J., Hatters, Danny M., Gleeson, Paul A.

“…Current methods for the quantitation of membrane protein trafficking rely heavily on microscopy, which has limited quantitative capacity for analyses of cell…”
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Application of flow cytometry to analyze intracellular location and trafficking of cargo in cell populations by Toh, Wei Hong, Houghton, Fiona J, Chia, Pei Zhi Cheryl, Ramdzan, Yasmin M, Hatters, Danny M, Gleeson, Paul A

“…Pulse shape analysis (PulSA) is a flow cytometry-based method that involves the measurement of the pulse width and height of a fluorescently labeled molecule…”
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A Biosensor of Src Family Kinase Conformation by Exposable Tetracysteine Useful for Cell-Based Screening by Irtegun, Sevgi, Wood, Rebecca, Lackovic, Kurt, Schweiggert, Jörg, Ramdzan, Yasmin M, Huang, David C. S, Mulhern, Terrence D, Hatters, Danny M

“…We developed a new approach to distinguish distinct protein conformations in live cells. The method, exposable tetracysteine (XTC), involved placing an…”
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ReAsH/FlAsH labeling and image analysis of tetracysteine sensor proteins in cells by Irtegun, Sevgi, Ramdzan, Yasmin M, Mulhern, Terrence D, Hatters, Danny M

“…Fluorescent proteins and dyes are essential tools for the study of protein trafficking, localization and function in cells. While fluorescent proteins such as…”
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Pulse shape analysis (PulSA) to track protein translocalization in cells by flow cytometry: applications for polyglutamine aggregation by Ramdzan, Yasmin M, Wood, Rebecca, Hatters, Danny M

“…Pulse shape analysis (PulSA) is a flow cytometry-based method that can be used to study protein localization patterns in cells. Examples for its use include…”
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Conformation Sensors that Distinguish Monomeric Proteins from Oligomers in Live Cells by Ramdzan, Yasmin M., Nisbet, Rebecca M., Miller, Jason, Finkbeiner, Steven, Hill, Andrew F., Hatters, Danny M.

“…Proteins prone to misfolding form large macroscopic deposits in many neurodegenerative diseases. Yet the in situ aggregation kinetics remains poorly understood…”
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ReAsH/FlAsH Labeling and Image Analysis of Tetracysteine Sensor Proteins in Cells by Irtegun, Sevgi, Ramdzan, Yasmin M., Mulhern, Terrence D., Hatters, Danny M.

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