Zobrazeno 1 - 10
of 313
pro vyhledávání: '"Rohit V, Pappu"'
Publikováno v:
Nature Communications, Vol 15, Iss 1, Pp 1-4 (2024)
Externí odkaz:
https://doaj.org/article/afe1365bd1194edc9c0a34691b9a19d7
Autor:
Mrityunjoy Kar, Laura T. Vogel, Gaurav Chauhan, Suren Felekyan, Hannes Ausserwöger, Timothy J. Welsh, Furqan Dar, Anjana R. Kamath, Tuomas P. J. Knowles, Anthony A. Hyman, Claus A. M. Seidel, Rohit V. Pappu
Publikováno v:
Nature Communications, Vol 15, Iss 1, Pp 1-21 (2024)
Abstract Phase separation and percolation contribute to phase transitions of multivalent macromolecules. Contributions of percolation are evident through the viscoelasticity of condensates and through the formation of heterogeneous distributions of n
Externí odkaz:
https://doaj.org/article/12c6a6e070804665adbd0503a07d444e
Autor:
Furqan Dar, Samuel R. Cohen, Diana M. Mitrea, Aaron H. Phillips, Gergely Nagy, Wellington C. Leite, Christopher B. Stanley, Jeong-Mo Choi, Richard W. Kriwacki, Rohit V. Pappu
Publikováno v:
Nature Communications, Vol 15, Iss 1, Pp 1-17 (2024)
Abstract The functions of biomolecular condensates are thought to be influenced by their material properties, and these will be determined by the internal organization of molecules within condensates. However, structural characterizations of condensa
Externí odkaz:
https://doaj.org/article/c93f7762b30c44859a29f3a08ec49c86
Publikováno v:
Nucleus, Vol 15, Iss 1 (2024)
ABSTRACTIn higher eukaryotes, the nucleolus harbors at least three sub-phases that facilitate multiple functionalities including ribosome biogenesis. The three prominent coexisting sub-phases are the fibrillar center (FC), the dense fibrillar compone
Externí odkaz:
https://doaj.org/article/d1a5e3c5f5074299832f797e96ef7638
Autor:
Andrew Z. Lin, Kiersten M. Ruff, Furqan Dar, Ameya Jalihal, Matthew R. King, Jared M. Lalmansingh, Ammon E. Posey, Nadia A. Erkamp, Ian Seim, Amy S. Gladfelter, Rohit V. Pappu
Publikováno v:
Nature Communications, Vol 14, Iss 1, Pp 1-17 (2023)
Abstract Cellular matter can be organized into compositionally distinct biomolecular condensates. For example, in Ashbya gossypii, the RNA-binding protein Whi3 forms distinct condensates with different RNA molecules. Using criteria derived from a phy
Externí odkaz:
https://doaj.org/article/637a2e86d36b45be88e92a46689153be
Publikováno v:
Nature Communications, Vol 14, Iss 1, Pp 1-16 (2023)
Abstract Prion-like low-complexity domains (PLCDs) are involved in the formation and regulation of distinct biomolecular condensates that form via phase separation coupled to percolation. Intracellular condensates often encompass numerous distinct pr
Externí odkaz:
https://doaj.org/article/6e8bf481cd41441ea01fe4097e787aeb
Publikováno v:
Nature Communications, Vol 13, Iss 1, Pp 1-15 (2022)
Abstract Biomolecular condensates form via coupled associative and segregative phase transitions of multivalent associative macromolecules. Phase separation coupled to percolation is one example of such transitions. Here, we characterize molecular an
Externí odkaz:
https://doaj.org/article/2570f28897ac4bd5a984a99600a308a1
Autor:
Anne Bremer, Ammon E. Posey, Madeleine B. Borgia, Wade M. Borcherds, Mina Farag, Rohit V. Pappu, Tanja Mittag
Publikováno v:
Biomolecules, Vol 12, Iss 10, p 1480 (2022)
Over the last decade, evidence has accumulated to suggest that numerous instances of cellular compartmentalization can be explained by the phenomenon of phase separation. This is a process by which a macromolecular solution separates spontaneously in
Externí odkaz:
https://doaj.org/article/ecb70b4b600f4fbcb19dbfc6dd615c17
Publikováno v:
Nature Communications, Vol 10, Iss 1, Pp 1-10 (2019)
De novo protein nanostructures are typically assembled via top-down approaches. Here, the authors developed a bottom-up approach, using split inteins to ligate multiple copies of a three-helix bundle to create 2D triangular and square-shaped structur
Externí odkaz:
https://doaj.org/article/ec7cdad6dc2045c1b4932d232772c37b
Publikováno v:
APL Materials, Vol 9, Iss 2, Pp 021119-021119-13 (2021)
Many naturally occurring elastomers are intrinsically disordered proteins (IDPs) built up of repeating units, and they can demonstrate two types of thermoresponsive phase behavior. Systems characterized by lower critical solution temperatures (LCSTs)
Externí odkaz:
https://doaj.org/article/c657d67dbca348dcb56a5c9da7c08d21