Zobrazeno 1 - 10
of 13
pro vyhledávání: '"Kenneth W Drombosky"'
Autor:
Bankanidhi Sahoo, Irene Arduini, Kenneth W Drombosky, Ravindra Kodali, Laurie H Sanders, J Timothy Greenamyre, Ronald Wetzel
Publikováno v:
PLoS ONE, Vol 11, Iss 6, p e0155747 (2016)
Expansion of the polyglutamine (polyQ) track of the Huntingtin (HTT) protein above 36 is associated with a sharply enhanced risk of Huntington's disease (HD). Although there is general agreement that HTT toxicity resides primarily in N-terminal fragm
Externí odkaz:
https://doaj.org/article/0d7d5852f7b5410c952937e6b1b377c6
Autor:
Dailu Chen, Kenneth W. Drombosky, Zhiqiang Hou, Levent Sari, Omar M. Kashmer, Bryan D. Ryder, Valerie A. Perez, DaNae R. Woodard, Milo M. Lin, Marc I. Diamond, Lukasz A. Joachimiak
Publikováno v:
Nature Communications, Vol 10, Iss 1, Pp 1-14 (2019)
The biophysical mechanisms of how disease-associated tau mutations drive amyloid formation are not well understood. Here the authors use biophysical approaches, cell models and MD simulations and find that the intrinsically disordered repeat domain o
Externí odkaz:
https://doaj.org/article/03b30e34ee8f4915b39c71a3c1b8c803
Autor:
Kenneth W. Drombosky, Sascha Rode, Ravi Kodali, Tija C. Jacob, Michael J. Palladino, Ronald Wetzel
Publikováno v:
Neurobiology of Disease, Vol 120, Iss , Pp 126-138 (2018)
In Huntington disease (HD), an expanded polyglutamine (polyQ > 37) sequence within huntingtin (htt) exon1 leads to enhanced disease risk. It has proved difficult, however, to determine whether the toxic form generated by polyQ expansion is a misfolde
Externí odkaz:
https://doaj.org/article/9884ce11e91d4fe08225fe51b3471656
Autor:
Sascha Rode, Ronald Wetzel, Michael J. Palladino, Ravi Kodali, Kenneth W. Drombosky, Tija C. Jacob
Publikováno v:
Neurobiology of Disease, Vol 120, Iss, Pp 126-138 (2018)
In Huntington disease (HD), an expanded polyglutamine (polyQ > 37) sequence within huntingtin (htt) exon1 leads to enhanced disease risk. It has proved difficult, however, to determine whether the toxic form generated by polyQ expansion is a misfolde
Autor:
Levent Sari, Dailu Chen, Bryan D. Ryder, Marc I. Diamond, Omar M. Kashmer, Milo M. Lin, Valerie A. Perez, Kenneth W. Drombosky, Zhiqiang Hou, Lukasz A. Joachimiak, Da Nae R. Woodard
Tauopathies are neurodegenerative diseases characterized by intracellular amyloid deposits of tau protein. Missense mutations in the tau gene (MAPT) correlate with aggregation propensity and cause dominantly inherited tauopathies, but their biophysic
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a28d063d5b3305fc464d1f74b79fe8a2
https://doi.org/10.1101/330266
https://doi.org/10.1101/330266
Autor:
Philip M. Bauer, Alessandro Bisello, Dale F. Mierke, Kristen L. Leslie, Jeremy M. Fitzpatrick, Kenneth W. Drombosky, Bin Wang, Peter A. Friedman, Noah Peyser, Stacey Barrick, Maria Pellegrini, Tatyana Mamonova, Gyun Jee Song
Publikováno v:
Journal of Biological Chemistry. 290:2879-2887
The regulation of the cell cycle by the ubiquitin-proteasome system is dependent on the activity of E3 ligases. Skp2 (S-phase kinase associated protein-2) is the substrate recognition subunit of the E3 ligase that ubiquitylates the cell cycle inhibit
Publikováno v:
Journal of Molecular Biology. 426:816-829
Polyglutamine (polyQ) amyloid fibrils are observed in disease tissue and have been implicated as toxic agents responsible for neurodegeneration in expanded CAG repeat diseases like Huntington’s disease (HD). Despite intensive efforts, the mechanism
Autor:
Kenneth W. Drombosky, Bankanidhi Sahoo, Ronald Wetzel, Irene Arduini, J. Timothy Greenamyre, Ravindra Kodali, Laurie H. Sanders
Publikováno v:
PLoS ONE
PLoS ONE, Vol 11, Iss 6, p e0155747 (2016)
PLoS ONE, Vol 11, Iss 6, p e0155747 (2016)
Expansion of the polyglutamine (polyQ) track of the Huntingtin (HTT) protein above 36 is associated with a sharply enhanced risk of Huntington's disease (HD). Although there is general agreement that HTT toxicity resides primarily in N-terminal fragm
Publikováno v:
Methods in Molecular Biology ISBN: 9781493929771
Fluorescence correlation spectroscopy (FCS) is a highly sensitive analytical technique used to measure dynamic molecular parameters, such as diffusion time (from which particle size can be calculated), conformation, and concentration of fluorescent m
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::2b3c0537db6d38ebb0ee83f726d83bbc
https://doi.org/10.1007/978-1-4939-2978-8_5
https://doi.org/10.1007/978-1-4939-2978-8_5
Publikováno v:
Methods in molecular biology (Clifton, N.J.). 1345
Fluorescence correlation spectroscopy (FCS) is a highly sensitive analytical technique used to measure dynamic molecular parameters, such as diffusion time (from which particle size can be calculated), conformation, and concentration of fluorescent m