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pro vyhledávání: '"Donald F, Senear"'
Autor:
Jenaro Soto, Melanie J. Cocco, Colleen L. Moody, Donald F. Senear, Vira Tretyachenko-Ladokhina
The E. coli cytidine repressor (CytR) is a member of the LacR family of bacterial repressors that regulates nine operons with distinct spacing and orientations of recognition sites. Understanding the structural features of the CytR DNA-binding domain
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::5eec4370b16df813cda909974229ebd0
https://doi.org/10.1101/2021.02.28.433298
https://doi.org/10.1101/2021.02.28.433298
Publikováno v:
Biophysical Journal. 120:17a
Autor:
Ying Wang, Vira Tretyachenko-Ladokhina, Hartmut Luecke, Martha Tan, Brad D. Wallentine, Donald F. Senear
Publikováno v:
Acta crystallographica. Section D, Biological crystallography, vol 69, iss Pt 10
To gain insights into the mechanisms by which certain second-site suppressor mutations rescue the function of a significant number of cancer mutations of the tumor suppressor protein p53, X-ray crystallographic structures of four p53 core-domain vari
Autor:
Colleen Moody, Thomas M. Laue, Donald F. Senear, Melanie J. Cocco, Vira Tretyachenko-Ladokhina
Publikováno v:
Biochemistry. 50:6622-6632
The cytidine repressor (CytR) is a member of the LacR family of bacterial repressors with distinct functional features. The Escherichia coli CytR regulon comprises nine operons whose palindromic operators vary in both sequence and, most significantly
Autor:
Yu-Hong Tan, Vira Tretyachenko-Ladokhina, Xiang Ye, Wei Yang, Y. Morris Chen, Qiang Lu, Donald F. Senear, Ray Luo
Publikováno v:
Biophysical Chemistry. 145:37-44
We have utilized both molecular dynamics simulations and solution biophysical measurements to investigate the rescue mechanism of mutation N235K, which plays a key role in the recently identified global suppressor motif of K235/Y239/R240 in the human
Autor:
Laurie M. Franklin, G. Wesley Hatfield, Reuben C. Darlington, Michael L. Opel, Donald F. Senear, J.B. Alexander Ross, Kimberly A. Aeling, Vira Tretyachenko-Ladokhina
Publikováno v:
Senear, Donald F.; Tretyachenko-Ladokhina, Vira; Opel, Michael L.; Aeling, Kimberly A.; Wesley Hatfield, G.; Franklin, Laurie M.; et al.(2007). Pressure dissociation of integration host factor-DNA complexes reveals flexibility-dependent structural variation at the protein-DNA interface. Nucleic Acids Research, 35(6), 1761-1772. UC Irvine: Retrieved from: http://www.escholarship.org/uc/item/6fv9z5d1
Nucleic Acids Research
Nucleic Acids Research
E. coli Integration host factor (IHF) condenses the bacterial nucleoid by wrapping DNA. Previously, we showed that DNA flexibility compensates for structural characteristics of the four consensus recognition elements associated with specific binding
Autor:
M. Johnson, Richard H. Lathrop, Donald F. Senear, Kimberly A. Aeling, N.R. Steffen, G.W. Hatfield
Publikováno v:
IEEE/ACM Transactions on Computational Biology and Bioinformatics. 4:117-125
Proteins that bind to specific locations in genomic DNA control many basic cellular functions. Proteins detect their binding sites using both direct and indirect recognition mechanisms. Deformation energy, which models the energy required to bend DNA
Autor:
Richard H. Lathrop, G. Wesley Hatfield, Michael L. Opel, Vira Tretyachenko-Ladokhina, Kimberly A. Aeling, N.R. Steffen, Donald F. Senear
Publikováno v:
Journal of Biological Chemistry. 281:39236-39248
Integration host factor (IHF) is a bacterial histone-like protein whose primary biological role is to condense the bacterial nucleoid and to constrain DNA supercoils. It does so by binding in a sequence-independent manner throughout the genome. Howev
Publikováno v:
Journal of Molecular Biology. 362:271-286
Interactions between DNA-bound transcription factors CytR and CRP regulate the promoters of the Escherichia coli CytR regulon. A distinctive feature of the palindromic CytR operators is highly variable length central spacers (0−9 bp). Previously we
Publikováno v:
Biochemistry. 42:3812-3825
The unlinked operons that comprise the Escherichia coli CytR regulon are controlled coordinately through interactions between two gene regulatory proteins, the cAMP receptor protein (CRP) and the cytidine repressor (CytR). CytR controls the balance b