Zobrazeno 1 - 10
of 58
pro vyhledávání: '"Jonathan R. Terman"'
Publikováno v:
Frontiers in Cell and Developmental Biology, Vol 11 (2023)
Actin and its dynamic structural remodelings are involved in multiple cellular functions, including maintaining cell shape and integrity, cytokinesis, motility, navigation, and muscle contraction. Many actin-binding proteins regulate the cytoskeleton
Externí odkaz:
https://doaj.org/article/6873f7124ba74852a37294e33c717c8c
Autor:
Elena E. Grintsevich, Giasuddin Ahmed, Anush A. Ginosyan, Heng Wu, Shannon K. Rich, Emil Reisler, Jonathan R. Terman
Publikováno v:
Nature Communications, Vol 12, Iss 1, Pp 1-18 (2021)
Actin-based structures in cells and tissues are built and maintained through a poorly understood balance between assembly and disassembly. Here, our findings provide insights into how factors known to promote these opposing effects dynamically integr
Externí odkaz:
https://doaj.org/article/d16f206bcaf8453d98be0d77c264773a
Autor:
Elena E. Grintsevich, Peng Ge, Michael R. Sawaya, Hunkar Gizem Yesilyurt, Jonathan R. Terman, Z. Hong Zhou, Emil Reisler
Publikováno v:
Nature Communications, Vol 8, Iss 1, Pp 1-10 (2017)
MICAL Redox enzymes post-translationally modify F-actin to promote its cellular destabilization. Here, the authors present a 3.9Å cryoEM structure of Mical-oxidized F-actin, showing its nucleotide-state dependent dynamic instability and susceptibili
Externí odkaz:
https://doaj.org/article/7ae7d1bd50ae4f3380c5ffcce5f2ab7d
Publikováno v:
Data in Brief, Vol 8, Iss , Pp 1227-1231 (2016)
Bacteria are the predominant source for producing recombinant proteins but while many exogenous proteins are expressed, only a fraction of those are soluble. We have found that a new actin regulatory enzyme Mical is poorly soluble when expressed in b
Externí odkaz:
https://doaj.org/article/b01e4b2765d744218484654ff97c435e
Autor:
Jimok Yoon, Jonathan R. Terman
Publikováno v:
Molecular & Cellular Oncology, Vol 5, Iss 1 (2018)
MICAL Redox enzymes have recently emerged as direct regulators of cell shape and motility – working through specific reversible post-translational oxidation of actin to disassemble and remodel the cytoskeleton. Links are also now emerging between M
Externí odkaz:
https://doaj.org/article/57836f5cfcf84593a8a7c1598108a116
Autor:
Jimok Yoon, Jonathan R. Terman
Publikováno v:
Communicative & Integrative Biology, Vol 11, Iss 1 (2018)
To change their size, shape, and connectivity, cells require actin and tubulin proteins to assemble together into long polymers – and numerous extracellular stimuli have now been identified that alter the assembly and organization of these cytoskel
Externí odkaz:
https://doaj.org/article/9abd4877517142d89ea682f54a34e5c4
Publikováno v:
The FASEB Journal. 36
Publikováno v:
Biophysical Journal. 122:407a
Publikováno v:
Science Advances
Cells shape and remodel themselves using specific transport mechanisms to locally expand their breakdown.
The F-actin cytoskeleton drives cellular form and function. However, how F-actin-based changes occur with spatiotemporal precision and spec
The F-actin cytoskeleton drives cellular form and function. However, how F-actin-based changes occur with spatiotemporal precision and spec
Autor:
Anush A. Ginosyan, Heng Wu, Shannon K. Rich, Elena E. Grintsevich, Giasuddin Ahmed, Emil Reisler, Jonathan R. Terman
Publikováno v:
Nature Communications
Nature communications, vol 12, iss 1
Nature Communications, Vol 12, Iss 1, Pp 1-18 (2021)
Nature communications, vol 12, iss 1
Nature Communications, Vol 12, Iss 1, Pp 1-18 (2021)
Cellular events require the spatiotemporal interplay between actin assembly and actin disassembly. Yet, how different factors promote the integration of these two opposing processes is unclear. In particular, cellular monomeric (G)-actin is complexed