Author

J. E. Mayfield

Listed by name: these papers carry no ORCID for this author, so different people with the same name may be mixed together.

Biology Disciplines

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Biochemistry· 3 Cell Biology· 1

Signature Assays, Organisms & Methods

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Research Focus:chromatin & epigenetic regulation· 3 Approach:experimental assay· 3 Assay:DNA methylation· 2 Organism:human· 2 Assay:proteomics· 2 Approach:statistical model· 2 Research Focus:cell signaling & trafficking· 1 Research Focus:cell type annotation· 1

Frequent Co-Authors

Y. Zhang· 3 shared A. C. Newton· 1 shared A. Chang· 1 shared A. J. Pollak· 1 shared A. McNeilly· 1 shared B. Portz· 1 shared C. A. Worby· 1 shared E. E. Escobar· 1 shared

Activity by Year

2019-2024 · peak 1/yr

Co-Author Collaboration Network

10 top collaborators · 15 mutual co-author links

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3 shared papersBiochemistry

Y. Zhang

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4 papers

Recent·Most cited

Variation of C-terminal domain governs RNA polymerase II genomic locations and alternative splicing in eukaryotic transcription

Q. Zhang, W. Kim, S. Panina, J. E. Mayfield, B. Portz, Y. Zhang

This study shows how phosphorylation of the CTD regulates condensate formation and alternative splicing across species.

bioRxiv · Jan 1, 2024Cell Biology

Ca2+-dependent liquid-liquid phase separation underlies intracellular Ca2+ stores.

J. E. Mayfield, A. J. Pollak, C. A. Worby, J. C. Xu, V. Tandon, M. Bose, A. McNeilly, S. Banerjee, A. C. Newton

The paper identifies Ca2+-dependent liquid-liquid phase separation in CASQ1, a Ca2+ binding protein in skeletal muscle, explaining Ca2+ buffering and storage mechanisms.

bioRxiv · Jul 6, 2021 · PreprintBiochemistry

Kinetic and thermodynamic analysis defines roles for two metal ions in DNA polymerase specificity and catalysis

S. Gong, S. Kirmizialtin, A. Chang, J. E. Mayfield, Y. Zhang, K. A. Johnson

This study analyzes the roles of two Mg2+ ions in DNA polymerase specificity and catalysis using kinetic analysis and molecular dynamics simulations.

bioRxiv · Oct 20, 2020Biochemistry

Tyr1 phosphorylation promotes the phosphorylation of Ser2 on the C-terminal domain of RNA polymerase II by P-TEFb

Y. Zhang, J. E. Mayfield, S. Irani, E. E. Escobar, Z. Zhang, N. T. Burkholder, M. R. Robinson, M. R. Mehaffey, S. N. Sipe, W. Yang, N. A. Prescott, K. Kathuria, Z. Liu, J. Brodbelt

The paper shows Tyr1 phosphorylation directs P-TEFb to phosphorylate Ser2 on RNA polymerase II CTD, altering its specificity and expanding CTD modification coding potential.

bioRxiv · May 28, 2019Biochemistry