Zobrazeno 1 - 10
of 16
pro vyhledávání: '"Yasmin M, Ramdzan"'
Autor:
Yasmin M. Ramdzan, Mikhail M. Trubetskov, Angelique R. Ormsby, Estella A. Newcombe, Xiaojing Sui, Mark J. Tobin, Marie N. Bongiovanni, Sally L. Gras, Grant Dewson, Jason M.L. Miller, Steven Finkbeiner, Nagaraj S. Moily, Jonathan Niclis, Clare L. Parish, Anthony W. Purcell, Michael J. Baker, Jacqueline A. Wilce, Saboora Waris, Diana Stojanovski, Till Böcking, Ching-Seng Ang, David B. Ascher, Gavin E. Reid, Danny M. Hatters
Publikováno v:
Cell Reports, Vol 19, Iss 5, Pp 919-927 (2017)
Summary: Competing models exist in the literature for the relationship between mutant Huntingtin exon 1 (Httex1) inclusion formation and toxicity. In one, inclusions are adaptive by sequestering the proteotoxicity of soluble Httex1. In the other, inc
Externí odkaz:
https://doaj.org/article/a88e3936e1a84e4ebc9bd6f66ea0df8a
Autor:
Angelique R. Ormsby, Paul R. Gooley, Kiersten M. Ruff, Yasmin M. Ramdzan, Anthony W. Purcell, Ashish Sethi, Archa H. Fox, Danny M. Hatters, Rohit V. Pappu, Estella A. Newcombe
Publikováno v:
Journal of Molecular Biology. 430:1442-1458
Soluble huntingtin exon 1 (Httex1) with expanded polyglutamine (polyQ) engenders neurotoxicity in Huntington's disease. To uncover the physical basis of this toxicity, we performed structural studies of soluble Httex1 for wild-type and mutant polyQ l
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1a9c97edd8dad58827b13a60871954e0
https://doi.org/10.1016/j.jmb.2018.03.031
https://doi.org/10.1016/j.jmb.2018.03.031
Autor:
Till Böcking, Jonathan C. Niclis, Michael J. Baker, Yasmin M. Ramdzan, Xiaojing Sui, Diana Stojanovski, Ching-Seng Ang, Nagaraj S. Moily, Steven Finkbeiner, Angelique R. Ormsby, Estella A. Newcombe, David B. Ascher, Clare L. Parish, Jacqueline A. Wilce, Marie N. Bongiovanni, Danny M. Hatters, Mark J. Tobin, Anthony W. Purcell, Saboora Waris, Mikhail M. Trubetskov, Grant Dewson, Sally L. Gras, Jason Miller, Gavin E. Reid
Publikováno v:
Cell Reports, Vol 19, Iss 5, Pp 919-927 (2017)
Summary: Competing models exist in the literature for the relationship between mutant Huntingtin exon 1 (Httex1) inclusion formation and toxicity. In one, inclusions are adaptive by sequestering the proteotoxicity of soluble Httex1. In the other, inc
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c92b7c62007ec96b46504c86c3aaf146
https://doi.org/10.1016/j.celrep.2017.04.029
https://doi.org/10.1016/j.celrep.2017.04.029
Autor:
Yasmin M. Ramdzan, Rohit V. Pappu, Danny M. Hatters, Kiersten M. Ruff, Anthony W. Purcell, Estella A. Newcombe, Ashish Sethi, Paul R. Gooley, Archa H. Fox, Angelique R. Ormsby
Soluble huntingtin exon 1 (Httex1) with expanded polyglutamine (polyQ) engenders neurotoxicity in Huntington’s disease. To uncover the physical basis of this toxicity, we performed structural studies of soluble Httex1 for wild type and mutant polyQ
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5a791124e02ac0cf9ac65ccd70997294
https://doi.org/10.1101/179663
https://doi.org/10.1101/179663
Autor:
Ross D. Hannan, Angelique R. Ormsby, Aleksandar Stojilovic, Alicia Oshlack, Anthony J. Hannan, Danny M. Hatters, Yasmin M. Ramdzan, Jeannine Diesch, Michelle S. Zajac, Nagaraj S. Moily
Publikováno v:
MOLECULAR AND CELLULAR NEUROSCIENCE
r-IGTP. Repositorio Institucional de Producción Científica del Instituto de Investigación Germans Trias i Pujol
instname
r-IGTP. Repositorio Institucional de Producción Científica del Instituto de Investigación Germans Trias i Pujol
instname
Huntington's disease is caused by polyglutamine (polyQ)-expansion mutations in the CAG tandem repeat of the Huntingtin gene. The central feature of Huntington's disease pathology is the aggregation of mutant Huntingtin (Htt) protein into micrometer-s
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::35fb8afd54155fb132440eecd45db961
https://pubmed.ncbi.nlm.nih.gov/28743452
https://pubmed.ncbi.nlm.nih.gov/28743452
Autor:
Yasmin M. Ramdzan, Kristijan D. Jovanoski, Danny M. Hatters, Angelique R. Ormsby, Yee-Foong Mok
Publikováno v:
The Journal of Biological Chemistry
Background: How misfolded proteins such as mutant huntingtin aggregate in the cell remains enigmatic. Results: We built a platform to view how aggregation proceeds and assessed the impact of quality control chaperones hsp40 and hsp70. Conclusion: hsp
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ac712c25ccf79cf91a0b703c0ec51d7b
https://doi.org/10.1074/jbc.m113.486944
https://doi.org/10.1074/jbc.m113.486944
Autor:
Anthony W. Purcell, Cheryl Chia, Yasmin M. Ramdzan, Dominic C.H. Ng, Angelique R. Ormsby, Saskia Polling, Paul A. Gleeson, Ivan Hong Wee Ng, Nathan P. Croft, Marie A. Bogoyevitch, Danny M. Hatters
Publikováno v:
Nature Methods. 9:467-470
We applied pulse-shape analysis (PulSA) to monitor protein localization changes in mammalian cells by flow cytometry. PulSA enabled high-throughput tracking of protein aggregation, translocation from the cytoplasm to the nucleus and trafficking from
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::27a37e1529cfa379acd11d04f4b88d36
https://doi.org/10.1038/nmeth.1930
https://doi.org/10.1038/nmeth.1930
Autor:
Steven Finkbeiner, Yasmin M. Ramdzan, Andrew F. Hill, Rebecca M. Nisbet, Jason Miller, Danny M. Hatters
Publikováno v:
Chemistry & Biology. 17(4):371-379
Proteins prone to misfolding form large macroscopic deposits in many neurodegenerative diseases. Yet the in situ aggregation kinetics remains poorly understood because of an inability to demarcate precursor oligomers from monomers. We developed a nov
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::95da4b9a2e3fb7abdfcb2871fc84407d
Autor:
Wei Hong, Toh, Fiona J, Houghton, Pei Zhi Cheryl, Chia, Yasmin M, Ramdzan, Danny M, Hatters, Paul A, Gleeson
Publikováno v:
Methods in molecular biology (Clifton, N.J.). 1270
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 simultaneously, enabling a multidimensional analysis of protein localization in a cell at hi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::6a8fae652a492eb120a12e9303846f75
https://pubmed.ncbi.nlm.nih.gov/25702121
https://pubmed.ncbi.nlm.nih.gov/25702121
Autor:
Wei Hong Toh, Fiona J. Houghton, Danny M. Hatters, Paul A. Gleeson, Pei Zhi Cheryl Chia, Yasmin M. Ramdzan
Publikováno v:
Membrane Trafficking ISBN: 9781493923083
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 simultaneously, enabling a multidimensional analysis of protein localization in a cell at hi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::a0a74e912e814c957b200a68f827607d
https://doi.org/10.1007/978-1-4939-2309-0_17
https://doi.org/10.1007/978-1-4939-2309-0_17