Zobrazeno 1 - 10
of 39
pro vyhledávání: '"Joshua A. Riback"'
Autor:
Katherine Leon, Rebecca L. Cunningham, Joshua A. Riback, Ezra Feldman, Jingxian Li, Tobin R. Sosnick, Minglei Zhao, Kelly R. Monk, Demet Araç
Publikováno v:
Nature Communications, Vol 11, Iss 1, Pp 1-14 (2020)
The extracellular regions (ECRs) of adhesion GPCRs have diverse biological functions, but their structures and mechanisms of action remain unclear. Here, the authors solve the ECR structure of the Gpr126 receptor and show that ECR conformation and si
Externí odkaz:
https://doaj.org/article/e5359c615ebc4086814c00727386b7d8
Autor:
Daniel S. W. Lee, Chang-Hyun Choi, David W. Sanders, Lien Beckers, Joshua A. Riback, Clifford P. Brangwynne, Ned S. Wingreen
Publikováno v:
Nature Physics. 19:586-596
Phase separation of biomolecules into condensates has emerged as a mechanism for intracellular organization and affects many intracellular processes, including reaction pathways through the clustering of enzymes and pathway intermediates. Precise and
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::f73b43b2702070ce75a707c5c887b355
https://doi.org/10.1038/s41567-022-01917-0
https://doi.org/10.1038/s41567-022-01917-0
Autor:
Ruofan Chen, Darren Kahan, Julia Shangguan, Joseph R. Sachleben, Joshua A. Riback, D. Allan Drummond, Tobin R. Sosnick
Eukaryotic cells form biomolecular condensates to sense and adapt to their environment1,2. Poly(A)-binding protein (Pab1), a canonical stress granule marker3,4, condenses upon heat shock or starvation, promoting adaptation5. The molecular basis of co
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::d5780b6267f1d7e342688f7a50514afe
https://doi.org/10.1101/2022.09.21.508844
https://doi.org/10.1101/2022.09.21.508844
Autor:
Daniel S.W. Lee, Chang-Hyun Choi, David W. Sanders, Lien Beckers, Joshua A. Riback, Clifford P. Brangwynne, Ned S. Wingreen
Phase separation of biomolecules into condensates has emerged as a ubiquitous mechanism for intracellular organization and impacts many intracellular processes, including reaction pathways through clustering of enzymes and their intermediates. Precis
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::5ace3980d5ce541227af3a912e5eb05f
https://doi.org/10.1101/2022.03.08.483545
https://doi.org/10.1101/2022.03.08.483545
Autor:
Ming-Tzo Wei, Diana M. Mitrea, Joshua A. Riback, Michele Tolbert, Richard W. Kriwacki, David W. Sanders, Clifford P. Brangwynne, Mylene C. Ferrolino, Lian Zhu
Publikováno v:
Nature
Intracellular bodies such as nucleoli, Cajal bodies and various signalling assemblies represent membraneless organelles, or condensates, that form via liquid–liquid phase separation (LLPS)1,2. Biomolecular interactions—particularly homotypic inte
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::43090c72cbb95bd763b1acd029a4c7b6
https://doi.org/10.1038/s41586-020-2256-2
https://doi.org/10.1038/s41586-020-2256-2
Autor:
Joshua A. Riback, Jorine M. Eeftens, Daniel S. W. Lee, Sofia A. Quinodoz, Lien Beckers, Lindsay A. Becker, Clifford P. Brangwynne
The nucleolus facilitates transcription, processing, and assembly of ribosomal RNA (rRNA), the most abundant RNA in cells. Nucleolar function is facilitated by its multiphase liquid properties, but nucleolar fluidity and its connection to ribosome bi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::85d6b39199f2dbd50ca36188952859da
https://doi.org/10.1101/2021.12.31.474660
https://doi.org/10.1101/2021.12.31.474660
Publikováno v:
Biophysical Journal. 122:295a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::cbd69e06de3770cc898893841d789841
https://doi.org/10.1016/j.bpj.2022.11.1671
https://doi.org/10.1016/j.bpj.2022.11.1671
Autor:
Gandhar K. Datar, Archish Anand, Marwa Sadek, Christina Dollinger, English Laserna, Lorenzo Brunetti, Nidhi Sahni, Margaret Goodell, Joshua A. Riback
Publikováno v:
Biophysical Journal. 122:442a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::978c8f26d0dbdb7e824a81c70c95aff7
https://doi.org/10.1016/j.bpj.2022.11.2386
https://doi.org/10.1016/j.bpj.2022.11.2386
Autor:
Micayla A. Bowman, Adam M. Zmyslowski, Joshua A. Riback, Tobin R. Sosnick, Kevin W. Plaxco, Patricia L. Clark
Publikováno v:
Proceedings of the National Academy of Sciences of the United States of America, vol 116, iss 18
The dimensions that unfolded proteins, including intrinsically disordered proteins (IDPs), adopt in the absence of denaturant remain controversial. We developed an analysis procedure for small-angle X-ray scattering (SAXS) profiles and used it to dem
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f44dc130c65218e954185813d9c00818
https://doi.org/10.1073/pnas.1813038116
https://doi.org/10.1073/pnas.1813038116
Autor:
Joshua A. Riback, Anabel Rodriguez, Micayla A. Bowman, Hongyu Guo, Tobin R. Sosnick, Jun Li, Patricia L. Clark
Publikováno v:
Proc Natl Acad Sci U S A
Much attention is being paid to conformational biases in the ensembles of intrinsically disordered proteins. However, it is currently unknown whether or how conformational biases within the disordered ensembles of foldable proteins affect function in
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5c68b5dd12f441791a4375931b7931e3
https://pubmed.ncbi.nlm.nih.gov/32879005
https://pubmed.ncbi.nlm.nih.gov/32879005