Francisco Asturias

Affiliations: 
Scripps Research Institute, La Jolla, La Jolla, CA, United States 
Area:
Cell Biology, General Biophysics
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"Francisco Asturias"
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Collaborators

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Joan W. Conaway collaborator (Cell Biology Tree)
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Publications

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Zhao H, Young N, Kalchschmidt J, et al. (2021) Structure of mammalian Mediator complex reveals Tail module architecture and interaction with a conserved core. Nature Communications. 12: 1355
El Khattabi L, Zhao H, Kalchschmidt J, et al. (2019) A Pliable Mediator Acts as a Functional Rather Than an Architectural Bridge between Promoters and Enhancers. Cell
Brignole EJ, Tsai KL, Chittuluru J, et al. (2018) 3.3-Å resolution cryo-EM structure of human ribonucleotide reductase with substrate and allosteric regulators bound. Elife. 7
Tsai KL, Yu X, Gopalan S, et al. (2017) Mediator structure and rearrangements required for holoenzyme formation. Nature
Sato S, Tomomori-Sato C, Tsai KL, et al. (2016) Role for the MED21-MED7 Hinge in Assembly of the Mediator-RNA Polymerase II Holoenzyme. The Journal of Biological Chemistry
Murakami K, Tsai KL, Kalisman N, et al. (2015) Structure of an RNA polymerase II preinitiation complex. Proceedings of the National Academy of Sciences of the United States of America. 112: 13543-8
Tsai KL, Tomomori-Sato C, Sato S, et al. (2014) Subunit Architecture and Functional Modular Rearrangements of the Transcriptional Mediator Complex. Cell. 158: 463
Tsai KL, Tomomori-Sato C, Sato S, et al. (2014) Subunit architecture and functional modular rearrangements of the transcriptional mediator complex. Cell. 157: 1430-44
Tsai KL, Sato S, Tomomori-Sato C, et al. (2013) A conserved Mediator-CDK8 kinase module association regulates Mediator-RNA polymerase II interaction. Nature Structural & Molecular Biology. 20: 611-9
Minnihan EC, Ando N, Brignole EJ, et al. (2013) Generation of a stable, aminotyrosyl radical-induced α2β2 complex of Escherichia coli class Ia ribonucleotide reductase. Proceedings of the National Academy of Sciences of the United States of America. 110: 3835-40
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