Zobrazeno 1 - 10
of 22
pro vyhledávání: '"Manuel F. Juette"'
Autor:
Chad M. Kurylo, Matthew M. Parks, Manuel F. Juette, Boris Zinshteyn, Roger B. Altman, Jordana K. Thibado, C. Theresa Vincent, Scott C. Blanchard
Publikováno v:
Cell Reports, Vol 25, Iss 1, Pp 236-248.e6 (2018)
Summary: Prevailing dogma holds that ribosomes are uniform in composition and function. Here, we show that nutrient limitation-induced stress in E. coli changes the relative expression of rDNA operons to alter the rRNA composition within the actively
Externí odkaz:
https://doaj.org/article/d3e78170d5eb4275abba28b85e6953b7
Autor:
Emily J Rundlet, Jordan D Carelli, Manuel F Juette, Alan Brown, Sichen Shao, Angelica Ferguson, Michael R Wasserman, Mikael Holm, Jack Taunton, Scott C Blanchard
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::f283d1488342aeaee8a063972c7671b3
https://doi.org/10.7554/elife.81608.sa2
https://doi.org/10.7554/elife.81608.sa2
Autor:
Daniel Hilger, Brian K. Kobilka, Signe Mathiasen, Maria Hauge, Matthieu Masureel, Scott C. Blanchard, Harel Weinstein, Jonathan A. Javitch, G. Glenn Gregorio, Daniel S. Terry, Jose Manuel Perez-Aguilar, Zhou Zhou, Hong Zhao, Manuel F. Juette
Publikováno v:
Nature
SUMMARY G protein-coupled receptor (GPCR)-mediated signal transduction is central to human physiology and disease intervention, yet the molecular mechanisms responsible for ligand-dependent signaling responses remain poorly understood. In Class A GPC
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::363ac570ebe4397bdf87806c5d92aeae
https://doi.org/10.1038/nature22354
https://doi.org/10.1038/nature22354
Autor:
Paul Huter, Daniel N. Wilson, Scott C. Blanchard, Stefan Arenz, Fabian Nguyen, Manuel F. Juette, Michael Graf, Yury S. Polikanov
Publikováno v:
Proceedings of the National Academy of Sciences. 113:7527-7532
The ribosome is one of the major targets for therapeutic antibiotics; however, the rise in multidrug resistance is a growing threat to the utility of our current arsenal. The orthosomycin antibiotics evernimicin (EVN) and avilamycin (AVI) target the
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c06d954fe29237266212734469948395
https://doi.org/10.1073/pnas.1604790113
https://doi.org/10.1073/pnas.1604790113
Autor:
Daniel S. Terry, Scott C. Blanchard, Hong Zhao, Michael R. Wasserman, Zhou Zhou, Manuel F. Juette, Roger B. Altman
Publikováno v:
Nature methods
Molecular recognition is often driven by transient processes beyond the reach of detection. Single-molecule fluorescence microscopy methods are uniquely suited for detecting such non-accumulating intermediates, yet achieving the time resolution and s
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6d44fef1a15a6b91f50c18594ebf9102
http://europepmc.org/articles/PMC4814340
http://europepmc.org/articles/PMC4814340
Autor:
Matthew Parks, Boris Zinshteyn, Chad M. Kurylo, Scott C. Blanchard, Jordana K. Thibado, C. Theresa Vincent, Manuel F. Juette, Roger B. Altman
Publikováno v:
Cell Reports, Vol 25, Iss 1, Pp 236-248.e6 (2018)
Cell reports
Cell reports
SUMMARY Prevailing dogma holds that ribosomes are uniform in composition and function. Here, we show that nutrient limitation-induced stress in E. coli changes the relative expression of rDNA operons to alter the rRNA composition within the actively
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::206cae96bd6625e6913e56ad1ad5018e
http://urn.kb.se/resolve?urn=urn:nbn:se:uu:diva-367391
http://urn.kb.se/resolve?urn=urn:nbn:se:uu:diva-367391
Autor:
Yury S. Polikanov, Thomas A. Steitz, Benjamin J. Burnett, Scott C. Blanchard, Agata L. Starosta, George P. Dinos, Wanli Lu, Daniel S. Terry, Daniel N. Wilson, Roger B. Altman, Manuel F. Juette, Kevin A. Reynolds
Publikováno v:
Molecular Cell. 58:832-844
The increase in multi-drug resistant bacteria is limiting the effectiveness of currently approved antibiotics, leading to a renewed interest in antibiotics with distinct chemical scaffolds. We have solved the structures of the Thermus thermophilus 70
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5c1867bfaba49c19132aa2c0dc1a431a
https://doi.org/10.1016/j.molcel.2015.04.014
https://doi.org/10.1016/j.molcel.2015.04.014
Autor:
Michael R. Wasserman, Daniel S. Terry, Manuel F. Juette, Qinsi Zheng, Scott C. Blanchard, Zhou Zhou, Roger B. Altman
Publikováno v:
Current Opinion in Chemical Biology. 20:103-111
Single-molecule Förster resonance energy transfer (smFRET) is an essential and maturing tool to probe biomolecular interactions and conformational dynamics in vitro and, increasingly, in living cells. Multi-color smFRET enables the correlation of mu
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::169fd8e73c5460637db7eadd79a8e0eb
https://doi.org/10.1016/j.cbpa.2014.05.010
https://doi.org/10.1016/j.cbpa.2014.05.010
Autor:
Daniel S. Terry, Roger B. Altman, Chad M. Kurylo, Scott C. Blanchard, Matt M. Parks, Manuel F. Juette, Boris Zinshteyn, Jose L. Alejo Amaya, Theresa Vincent, Michael R. Wasserman
Publikováno v:
Biophysical Journal. 116:12a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::61b4821ad882b90560c96fde03f67d55
https://doi.org/10.1016/j.bpj.2018.11.106
https://doi.org/10.1016/j.bpj.2018.11.106
Autor:
Steffen Jockusch, Scott C. Blanchard, James B. Munro, Manuel F. Juette, Rachel A. Kolster, Qinsi Zheng, Olga Boudker, Hong Zhao, Daniel S. Terry, Nurunisa Akyuz, G. Glenn Gregorio, Roger B. Altman, Jonathan A. Javitch, Walther Mothes, Zhou Zhou
Publikováno v:
The FASEB Journal. 29
Advances in single-molecule imaging and fluorescence technologies now enable direct insights into functional dynamic processes in diverse families of integral membrane proteins. These data pave the...
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::bf978f31222a8e6f2fb7766d7d312137
https://doi.org/10.1096/fasebj.29.1_supplement.498.3
https://doi.org/10.1096/fasebj.29.1_supplement.498.3