Zobrazeno 1 - 7
of 7
pro vyhledávání: '"Kevin E. W. Namitz"'
Autor:
Kevin E. W. Namitz, Tongyin Zheng, Ashley J. Canning, Nilda L. Alicea-Velazquez, Carlos A. Castañeda, Michael S. Cosgrove, Steven D. Hanes
Publikováno v:
Communications Biology, Vol 4, Iss 1, Pp 1-14 (2021)
Namitz, Zheng et al. identify a bivalent interaction by the yeast Ess1 with CTD peptides of RNA polymerase II. Their results suggest an anchored mechanism of isomerization, and raise the possibility of eukaryotic parvulin-class prolyl isomerases gain
Externí odkaz:
https://doaj.org/article/cb36b1e1b4ac4118b1cc027bc944f7fe
Publikováno v:
The Journal of Physical Chemistry B. 125:10917-10927
Intrinsically disordered protein (IDP) sequences often contain a high proportion of charged residues in conjunction with their high degree of hydrophilicity and solvation. For high net charge IDPs, long-range electrostatic interactions are thought to
Autor:
Ryan J. Palumbo, Nathan McKean, Erinn Leatherman, Kevin E. W. Namitz, Laurie Connell, Aaron Wolfe, Kelsey Moody, Cene Gostinčar, Nina Gunde-Cimerman, Alaji Bah, Steven D. Hanes
Publikováno v:
Science advances. 8(36)
Most of the world’s biodiversity lives in cold (−2° to 4°C) and hypersaline environments. To understand how cells adapt to such conditions, we isolated two key components of the transcription machinery from fungal species that live in extreme p
Autor:
Steven D. Hanes, Tongyin Zheng, Nilda L. Alicea-Velázquez, Ashley J. Canning, Michael S. Cosgrove, Kevin E. W. Namitz, Carlos A. Castañeda
Publikováno v:
Communications Biology, Vol 4, Iss 1, Pp 1-14 (2021)
Communications Biology
Communications Biology
Accurate gene transcription in eukaryotes depends on isomerization of serine-proline bonds within the carboxy-terminal domain (CTD) of RNA polymerase II. Isomerization is part of the “CTD code” that regulates recruitment of proteins required for
Autor:
Sanim Rahman, Niklas A. Hoffmann, Evan J. Worden, Marissa L. Smith, Kevin E. W. Namitz, Bruce A. Knutson, Michael S. Cosgrove, Cynthia Wolberger
The human Mixed Lineage Leukemia-1 (MLL1) complex orchestrates methylation of histone H3K4 to promote transcription and is stimulated by monoubiquitination of histone H2B. Recent structures of the MLL1-WRAD core complex, which comprises the MLL1 meth
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8ef1f91dd5d3d58410e57b13d8b58590
https://doi.org/10.1101/2022.04.04.486905
https://doi.org/10.1101/2022.04.04.486905
Publikováno v:
Biophysical journal. 120(21)
Post-translational modification (PTM) of proteins is of critical importance to the regulation of many cellular processes in eukaryotic organisms. One of the most well-studied protein PTMs is methylation, wherein an enzyme catalyzes the transfer of a
Autor:
Kevin E. W. Namitz, Ashley J. Canning, Tongyin Zheng, Micheal S. Cosgrove, Nilda L. Alicea-Velázquez, Steven D. Hanes, Carlos A. Castañeda
Publikováno v:
Biophysical Journal. 118:531a