bioRxivBiochemistryPreprint
Structural basis of phosphorylation kinetics in the transcriptional activation domain (TAD) of c-Jun and insight of two new phosphorylation sites Ser58 and Thr62
Abstract
This manuscript has been removed due to unethical behavior by the authors that includes violation of copyright.
- organism: human
- assay: proteomics
- research focus: protein folding & dynamics
- approach: experimental assay
Reproducibility ledger
Nobody has reported trying to reproduce this paper yet. Did you replicate an experiment or run the code? Your report saves the next lab a week.
Sign in to file a reproducibility report.
Related papers
Similarity Map
SelectedSame fieldCross-field
70% semantic matchBiochemistry
- An intrinsic temporal order of c-Jun N-terminal phosphorylation regulates its activity by orchestrating co-factor recruitment
C. A. Waudby, S. Alvarez-Teijeiro, … A. Mylona·bioRxiv·Nov 3, 2021
- Phosphorylation of tyrosine 90 in SH3 domain is a new regulatory switch controlling Src kinase
L. Koudelkova, Z. Bruhova, … D. Rosel·bioRxiv·Aug 23, 2022
- Structural basis of Cdk7 activation by dual T-loop phosphorylation
- PAF1C allosterically activates CDK12/13 kinase during RNAPII transcript elongation
David López Martínez, Izabela Todorovski, … Jesper Qualmann Svejstrup·Molecular CellPeer-reviewed·May 1, 2025
- Tyr1 phosphorylation promotes the phosphorylation of Ser2 on the C-terminal domain of RNA polymerase II by P-TEFb
Y. Zhang, J. E. Mayfield, … J. Brodbelt·bioRxiv·May 28, 2019
- Sequence features of transcriptional activation domains are consistent with the surfactant mechanism of gene activation
Bradley K. Broyles, Tamara Y. Erkina, … Alexandre M. Erkine·bioRxiv·Jun 18, 2023