Full Text Journal Articles by
Author Michael A Mohan

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The crystal structure of Bacillus subtilis YycI reveals a common fold for two members of an unusual class of sensor histidine kinase regulatory proteins.

Eugenio Santelli, Robert C Liddington, Michael A Mohan, James A Hoch, Hendrik Szurmant,

YycI and YycH are two membrane-anchored periplasmic proteins that regulate the essential Bacillus subtilis YycG histidine kinase through direct interaction. Here we present the crystal structure of YycI at a 2.9-A resolution. YycI forms a dimer, and remarkably the structure resembles that of the two C-terminal domains of YycH despite ... Read more >>

J. Bacteriol. (Journal of bacteriology)
[2007, 189(8):3290-3295]

Cited: 22 times

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YycH and YycI interact to regulate the essential YycFG two-component system in Bacillus subtilis.

Hendrik Szurmant, Michael A Mohan, P Michael Imus, James A Hoch,

The YycFG two-component system is the only signal transduction system in Bacillus subtilis known to be essential for cell viability. This system is highly conserved in low-G+C gram-positive bacteria, regulating important processes such as cell wall homeostasis, cell membrane integrity, and cell division. Four other genes, yycHIJK, are organized within ... Read more >>

J. Bacteriol. (Journal of bacteriology)
[2007, 189(8):3280-3289]

Cited: 74 times

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The crystal structure of YycH involved in the regulation of the essential YycFG two-component system in Bacillus subtilis reveals a novel tertiary structure.

Hendrik Szurmant, Haiyan Zhao, Michael A Mohan, James A Hoch, Kottayil I Varughese,

The Bacillus subtilis YycFG two-component signal transduction system is essential for cell viability, and the YycH protein is part of the regulatory circuit that controls its activity. The crystal structure of YycH was solved by two-wavelength selenium anomalous dispersion data, and was refined using 2.3 A data to an R-factor ... Read more >>

Protein Sci. (Protein science : a publication of the Protein Society)
[2006, 15(4):929-934]

Cited: 17 times

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Two-dimensional diversity: screening human cDNA phage display libraries with a random diversity probe for the display cloning of phosphotyrosine binding domains.

Elizabeth J Videlock, Victor K Chung, Michael A Mohan, Timothy M Strok, David J Austin,

A random phosphopeptide probe (bio-pYZZZ) has been used for the isolation and identification of multiple SH2 domains from human cDNA-displaying phage libraries. In addition, on-phage analysis and quantification of binding affinities for these phage-displayed proteins has shown them to be functional domains, retaining the same characteristics as in their native ... Read more >>

J. Am. Chem. Soc. (Journal of the American Chemical Society)
[2004, 126(12):3730-3731]

Cited: 5 times

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