Zobrazeno 1 - 10
of 392
pro vyhledávání: '"Eugene I. Shakhnovich"'
Publikováno v:
Nature Communications, Vol 15, Iss 1, Pp 1-13 (2024)
Abstract The existence of multiple biomolecular condensates inside living cells is a peculiar phenomenon not compatible with the predictions of equilibrium statistical mechanics. In this work, we address the problem of multiple condensates state (MCS
Externí odkaz:
https://doaj.org/article/9ffe34df61cb4ceb90892704ea5d0ade
Autor:
Sourav Chowdhury, Daniel C. Zielinski, Christopher Dalldorf, Joao V. Rodrigues, Bernhard O. Palsson, Eugene I. Shakhnovich
Publikováno v:
Nature Communications, Vol 14, Iss 1, Pp 1-14 (2023)
Abstract Elucidating intracellular drug targets is a difficult problem. While machine learning analysis of omics data has been a promising approach, going from large-scale trends to specific targets remains a challenge. Here, we develop a hierarchic
Externí odkaz:
https://doaj.org/article/487eb402d5bc4afe9dded197f9fac91e
Autor:
Michael Manhart, Eugene I. Shakhnovich
Publikováno v:
Nature Communications, Vol 9, Iss 1, Pp 1-9 (2018)
Higher-order interactions occur when one species mediates the interaction between two others. Here, the authors model microbial growth and competition to show that higher-order interactions can arise from tradeoffs in growth traits, leading to neutra
Externí odkaz:
https://doaj.org/article/50e1e4d748d04ccaa7d646a805e19fce
Autor:
Stéphanie Valleau, Romain A. Studer, Florian Häse, Christoph Kreisbeck, Rafael G. Saer, Robert E. Blankenship, Eugene I. Shakhnovich, Alán Aspuru-Guzik
Publikováno v:
ACS Central Science, Vol 3, Iss 10, Pp 1086-1095 (2017)
Externí odkaz:
https://doaj.org/article/f8326317a735443895ae6134b5b39f2a
Autor:
Rui J. S. Loureiro, Diogo Vila-Viçosa, Miguel Machuqueiro, Eugene I. Shakhnovich, Patrícia F. N. Faísca
Publikováno v:
Biomolecules, Vol 9, Iss 8, p 366 (2019)
Human β2-microglobulin (b2m) protein is classically associated with dialysis-related amyloidosis (DRA). Recently, the single point mutant D76N was identified as the causative agent of a hereditary systemic amyloidosis affecting visceral organs. To g
Externí odkaz:
https://doaj.org/article/cee126a759844428a39df9012d64fb01
Publikováno v:
Cell Reports, Vol 2, Iss 2, Pp 249-256 (2012)
The consistent observation across all kingdoms of life that highly abundant proteins evolve slowly demonstrates that cellular abundance is a key determinant of protein evolutionary rate. However, other empirical findings, such as the broad distributi
Externí odkaz:
https://doaj.org/article/2b3f4742b6a44d7a8d673eb38ad16235
Autor:
David Scheerer, Bharat V. Adkar, Sanchari Bhattacharyya, Dorit Levy, Marija Iljina, Inbal Riven, Orly Dym, Gilad Haran, Eugene I. Shakhnovich
Publikováno v:
Proceedings of the National Academy of Sciences. 120
Enzymes play a vital role in life processes; they control chemical reactions and allow functional cycles to be synchronized. Many enzymes harness large-scale motions of their domains to achieve tremendous catalytic prowess and high selectivity for sp
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::41cfeeaa33fb3d750532f195cdc6fbb7
https://doi.org/10.1073/pnas.2219855120
https://doi.org/10.1073/pnas.2219855120
Protein space is a rich analogy for genotype-phenotype maps, where amino acid sequence is organized into a high-dimensional space that highlights the connectivity between protein variants. It is a useful abstraction for understanding the process of e
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::fa6e74f0b0ced5ce94ebafed3fb7bbdd
https://doi.org/10.1101/2023.04.09.535490
https://doi.org/10.1101/2023.04.09.535490
Publikováno v:
Biophys J
To what degree are individual structural elements within proteins modular such that similar structures from unrelated proteins can be interchanged? We study subdomain modularity by creating 20 chimeras of an enzyme, Escherichia coli dihydrofolate red
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8380cbc9c1f777986f3b97e1b6d0ba18
https://doi.org/10.1016/j.bpj.2021.09.032
https://doi.org/10.1016/j.bpj.2021.09.032
Publikováno v:
bioRxiv
Many secreted proteins contain multiple disulfide bonds. How disulfide formation is coupled to protein folding in the cell remains poorly understood at the molecular level. Here, we combine experiment and simulation to address this question as it per
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ae19551b11ac37d4471cdf8035fd84a7
https://doi.org/10.1101/2022.11.10.516025
https://doi.org/10.1101/2022.11.10.516025