Zobrazeno 1 - 10
of 66
pro vyhledávání: '"Scott Horowitz"'
Autor:
Theodore J. Litberg, Rajesh Kumar Reddy Sannapureddi, Zijue Huang, Ahyun Son, Bharathwaj Sathyamoorthy, Scott Horowitz
Publikováno v:
RNA Biology, Vol 20, Iss 1, Pp 495-509 (2023)
Maintaining a healthy protein folding environment is essential for cellular function. Recently, we found that nucleic acids, G-quadruplexes in particular, are potent chaperones for preventing protein aggregation. With the aid of structure-function an
Externí odkaz:
https://doaj.org/article/ace4afa7131b4629b23d62b1584417cc
Autor:
Jemil Ahmed, Tessa C. Fitch, Courtney M. Donnelly, Johnson A. Joseph, Tyler D. Ball, Mikaela M. Bassil, Ahyun Son, Chen Zhang, Aurélie Ledreux, Scott Horowitz, Yan Qin, Daniel Paredes, Sunil Kumar
Publikováno v:
Nature Communications, Vol 13, Iss 1, Pp 1-17 (2022)
Inhibiting alpha-synuclein self-assembly into amyloid structures, associated with Parkinson’s disease, is a potential therapeutic intervention. Here, the authors identify the domains/sequences that are essential for alpha-synuclein aggregation and
Externí odkaz:
https://doaj.org/article/90b6ab61face4e2e9229b5bec4e05f95
Publikováno v:
RNA Biology, Vol 18, Iss 1, Pp 16-23 (2021)
As a mental framework for the transition of self-replicating biological forms, the RNA world concept stipulates a dual function of RNAs as genetic substance and catalyst. The chaperoning function is found intrinsic to ribozymes involved in protein sy
Externí odkaz:
https://doaj.org/article/77166f558b81458d9cd847cb4387c1fe
Autor:
Firas Khatib, Ambroise Desfosses, Foldit Players, Brian Koepnick, Jeff Flatten, Zoran Popović, David Baker, Seth Cooper, Irina Gutsche, Scott Horowitz
Publikováno v:
PLoS Biology, Vol 17, Iss 11, p e3000472 (2019)
With the rapid improvement of cryo-electron microscopy (cryo-EM) resolution, new computational tools are needed to assist and improve upon atomic model building and refinement options. This communication demonstrates that microscopists can now collab
Externí odkaz:
https://doaj.org/article/2ce81750f4844d529b7bcecb4749423f
Autor:
Scott Horowitz, Brian Koepnick, Raoul Martin, Agnes Tymieniecki, Amanda A. Winburn, Seth Cooper, Jeff Flatten, David S. Rogawski, Nicole M. Koropatkin, Tsinatkeab T. Hailu, Neha Jain, Philipp Koldewey, Logan S. Ahlstrom, Matthew R. Chapman, Andrew P. Sikkema, Meredith A. Skiba, Finn P. Maloney, Felix R. M. Beinlich, Foldit Players, University of Michigan students, Zoran Popović, David Baker, Firas Khatib, James C. A. Bardwell
Publikováno v:
Nature Communications, Vol 7, Iss 1, Pp 1-11 (2016)
Building crystal structures into the electron density is an important step in protein structure solution. Here, the authors recruit online game players, students, and experienced crystallographers to compete in a competition to solve a new structure,
Externí odkaz:
https://doaj.org/article/b15fb233272548d7bc0404a5bf35e26f
Autor:
Bastian Groitl, Scott Horowitz, Karl A. T. Makepeace, Evgeniy V. Petrotchenko, Christoph H. Borchers, Dana Reichmann, James C. A. Bardwell, Ursula Jakob
Publikováno v:
Nature Communications, Vol 7, Iss 1, Pp 1-12 (2016)
Under stress conditions the molecular chaperone Hsp33 is activated to process unfolded proteins. Here, the authors use in vivo and in vitro crosslinking and 19F-NMR to elucidate the binding site for misfolded proteins and are able to propose a model
Externí odkaz:
https://doaj.org/article/695b2905d3a942f196334c70c8cf5b8c
Autor:
Scott Horowitz, Brian Koepnick, Raoul Martin, Agnes Tymieniecki, Amanda A. Winburn, Seth Cooper, Jeff Flatten, David S. Rogawski, Nicole M. Koropatkin, Tsinatkeab T. Hailu, Neha Jain, Philipp Koldewey, Logan S. Ahlstrom, Matthew R. Chapman, Andrew P. Sikkema, Meredith A. Skiba, Finn P. Maloney, Felix R. M. Beinlich, Foldit Players, University of Michigan students, Zoran Popović, David Baker, Firas Khatib, James C. A. Bardwell
Publikováno v:
Nature Communications, Vol 7, Iss 1, Pp 1-2 (2016)
Nature Communications 7: Article number:12549 (2016); Published 16 September 2016; Updated 25 October 2016 The original version of this Article contained an error in the spelling of a member of the University of Michigan students Consortium, Sam Lee,
Externí odkaz:
https://doaj.org/article/1232003cb40a496181d47d61db72f8c2
Autor:
Shu Quan, Lili Wang, Evgeniy V Petrotchenko, Karl AT Makepeace, Scott Horowitz, Jianyi Yang, Yang Zhang, Christoph H Borchers, James CA Bardwell
Publikováno v:
eLife, Vol 3 (2014)
Experimental study of the role of disorder in protein function is challenging. It has been proposed that proteins utilize disordered regions in the adaptive recognition of their various binding partners. However apart from a few exceptions, defining
Externí odkaz:
https://doaj.org/article/979cf14817e746ab8b22ff89541be63a
Publikováno v:
Proceedings of the National Academy of Sciences. 120
Maintaining the health of the proteome is a critical cellular task. Recently, we found G-quadruplex (G4) nucleic acids are especially potent at preventing protein aggregation in vitro and could at least indirectly improve the protein folding environm
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::c8a5ac2565b266949cdcfa5a31edc00b
https://doi.org/10.1073/pnas.2216308120
https://doi.org/10.1073/pnas.2216308120
