Outputs (51)

High-level over-expression, purification, and crystallization of a novel phospholipase C/sphingomyelinase from Pseudomonas aeruginosa (2013)
Journal Article
Truan, D., Vasil, A., Stonehouse, M., Vasil, M., & Pohl, E. (2013). High-level over-expression, purification, and crystallization of a novel phospholipase C/sphingomyelinase from Pseudomonas aeruginosa. Protein Expression and Purification, 90(1), 40-46. https://doi.org/10.1016/j.pep.2012.11.005

The hemolytic phospholipase C/sphingomyelinase PlcH from the opportunistic pathogen Pseudomonas aeruginosa represents the founding member of a growing family of virulence factors identified in a wide range of bacterial and fungal pathogens. In P. aer... Read More about High-level over-expression, purification, and crystallization of a novel phospholipase C/sphingomyelinase from Pseudomonas aeruginosa.

Changes in the quaternary structure and function of MjHSP16.5 attributable to deletion of the I–X–I motif and introduction of the substitution, R107G in the a-crystallin domain (2013)
Journal Article
Quinlan, R., Zhang, Y., Lansbury, A., Williamson, I., Pohl, E., & Sun, F. (2013). Changes in the quaternary structure and function of MjHSP16.5 attributable to deletion of the I–X–I motif and introduction of the substitution, R107G in the a-crystallin domain. Philosophical Transactions of the Royal Society B: Biological Sciences, 368(1617), Article 20120327. https://doi.org/10.1098/rstb.2012.0327

The archael small heat-shock protein (sHSP), MjHSP16.5, forms a 24-subunit oligomer with octahedral symmetry. Here, we demonstrate that the IXI motif present in the C-terminal domain is necessary for the oligomerization of MjHSP16.5. Removal increase... Read More about Changes in the quaternary structure and function of MjHSP16.5 attributable to deletion of the I–X–I motif and introduction of the substitution, R107G in the a-crystallin domain.

A Nucleotide Phosphatase Activity in the Nucleotide Binding Domain of an Orphan Resistance Protein from Rice (2012)
Journal Article
Fenyk, S., de San Eustaquio Campillo, A., Pohl, E., Hussey, P., & Cann, M. (2012). A Nucleotide Phosphatase Activity in the Nucleotide Binding Domain of an Orphan Resistance Protein from Rice. Journal of Biological Chemistry, 287(6), 4023-4032. https://doi.org/10.1074/jbc.m111.314450

Plant resistance proteins (R-proteins) are key components of the plant immune system activated in response to a plethora of different pathogens. R-proteins are P-loop NTPase superfamily members, and current models describe their main function as ATPa... Read More about A Nucleotide Phosphatase Activity in the Nucleotide Binding Domain of an Orphan Resistance Protein from Rice.

Metal-adeninate vertices for the construction of an exceptionally porous metal-organic framework (2012)
Journal Article
An, J., Farha, O. K., Hupp, J. T., Pohl, E., Yeh, J. I., & Rosi, N. L. (2012). Metal-adeninate vertices for the construction of an exceptionally porous metal-organic framework. Nature Communications, 3, Article 604. https://doi.org/10.1038/ncomms1618

Synthesis and molecular structure of a perfluorinated pyridyl carbanion (2012)
Journal Article
Colgin, N., Tatum, N., Pohl, E., Cobb, S., & Sandford, G. (2012). Synthesis and molecular structure of a perfluorinated pyridyl carbanion. Journal of Fluorine Chemistry, 133, 33-37. https://doi.org/10.1016/j.jfluchem.2011.09.013

Reaction of pentafluoropyridine with sodium nitromethanide allowed the isolation and characterisation of the first perfluorinated pyridyl carbanion system, sodium nitrobis(perfluoropyridin-4-yl)methanide, by X-ray crystallography.

The Crystal Structure of Non-Modified and Bipyridine-Modified PNA Duplexes (2010)
Journal Article
Yeh, J. I., Pohl, E., Truan, D., He, W., Sheldrick, G. M., Du, S., & Achim, C. (2010). The Crystal Structure of Non-Modified and Bipyridine-Modified PNA Duplexes. Chemistry - A European Journal, 16(39), 11867-11875. https://doi.org/10.1002/chem.201000392

Crystal Structure of the Caseinolytic Protease Gene Regulator, a Transcriptional Activator in Actinomycetes (2009)
Journal Article
Russo, S., Schweitzer, J., Polen, T., Bott, M., & Pohl, E. (2009). Crystal Structure of the Caseinolytic Protease Gene Regulator, a Transcriptional Activator in Actinomycetes. Journal of Biological Chemistry, 284(8), 5208-5216. https://doi.org/10.1074/jbc.m806591200

Crystallization and preliminary X-ray analysis of the Thermoplasma acidophilum 20S proteasome in complex with protein substrates. (2008)
Journal Article
Felderer, K., Groves, M., Diez, J., Pohl, E., & Witt, S. (2008). Crystallization and preliminary X-ray analysis of the Thermoplasma acidophilum 20S proteasome in complex with protein substrates. Acta crystallographica. Section F, Structural biology and crystallization communications, 64(10), 899-902. https://doi.org/10.1107/s1744309108026791

The Metal-Dependent Regulators FurA and FurB from Mycobacterium Tuberculosis (2008)
Journal Article
Lucarelli, D., Vasil, M., Meyer-Klaucke, W., & Pohl, E. (2008). The Metal-Dependent Regulators FurA and FurB from Mycobacterium Tuberculosis. International Journal of Molecular Sciences, 9(8), 1548-1560. https://doi.org/10.3390/ijms9081548

The ferric uptake regulators (Fur) form a large family of bacterial metalactivated DNA-binding proteins that control a diverse set of genes at the transcriptional level. Mycobacterium tuberculosis, the causative agent of tuberculosis, expresses two m... Read More about The Metal-Dependent Regulators FurA and FurB from Mycobacterium Tuberculosis.

Crystal structure and function of the zinc uptake regulator FurB from Mycobacterium tuberculosis (2007)
Journal Article
Lucarelli, D., Russo, S., Garman, E., Milano, A., Meyer-Klaucke, W., & Pohl, E. (2007). Crystal structure and function of the zinc uptake regulator FurB from Mycobacterium tuberculosis. Journal of Biological Chemistry, 282(13), 9914-9922. https://doi.org/10.1074/jbc.m609974200

Members of the ferric/zinc uptake regulator (Fur/Zur) family are the central metal-dependent regulator proteins in many Gram-negative and -positive bacteria. They are responsible for the control of a wide variety of basic physiological processes and... Read More about Crystal structure and function of the zinc uptake regulator FurB from Mycobacterium tuberculosis.