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Christopher F Mugler

Researcher at University of California, Berkeley

Publications -  12
Citations -  662

Christopher F Mugler is an academic researcher from University of California, Berkeley. The author has contributed to research in topics: DEAD box & Nuclear pore. The author has an hindex of 7, co-authored 12 publications receiving 451 citations. Previous affiliations of Christopher F Mugler include University of California, Santa Barbara & ETH Zurich.

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Non-invasive measurement of mRNA decay reveals translation initiation as the major determinant of mRNA stability.

TL;DR: Non-invasive transcriptome-wide mRNA production and stability measurements with selective and acute perturbations are combined to demonstrate that mRNA degradation is tightly coupled to the regulation of translation, and that a competition between translation initiation and mRNA decay is the major determinant of mRNA stability in yeast.
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ATPase activity of the DEAD-box protein Dhh1 controls processing body formation

TL;DR: It is shown that in budding yeast, mutations in the DEAD-box ATPase Dhh1 that prevent ATP hydrolysis, or that affect the interaction between DHH1 and Not1, the central scaffold of the CCR4-NOT complex and an activator of the Dhh2 ATPase, prevent PB disassembly in vivo.
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Small and Large Ribosomal Subunit Deficiencies Lead to Distinct Gene Expression Signatures that Reflect Cellular Growth Rate

TL;DR: Two distinct signatures of protein synthesis suggest intriguing and currently mysterious differences in the cellular consequences of deficiency for small and large ribosomal subunits.
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Natively Unfolded FG Repeats Stabilize the Structure of the Nuclear Pore Complex

TL;DR: The results reveal a previously unanticipated structural role for natively unfolded GLFG repeats as Velcro to link NPC subcomplexes and thus add a new layer of connections to current models of the NPC architecture.
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Pat1 promotes processing body assembly by enhancing the phase separation of the DEAD-box ATPase Dhh1 and RNA.

TL;DR: It is shown that the PB component Pat1 antagonizes Not1 and promotes PB assembly via its direct interaction with Dhh1, thereby aiding the assembly of large multivalent mRNP granules that are PBs.