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2017-01-01

Carvalho, Wildemar S. P., Wei, Menglian, Ikpo, Nduka, Gao, Yongfeng, Serpe, Michael J.

Reports in the literature on the development of new chemical sensing technologies have been growing steadily in number for years. For example, a Web of Science topic search using the term “Chemical Sensing” revealed that over 8 000 papers were published in 2015–2017, with over 40 000 citations to...

2000

Owttrim, George W., Chamot, Danuta

Expression of the Anabaena sp. strain PCC 7120 RNA helicase gene crhC is induced by cold shock.crhC transcripts are not detectable at 30°C but accumulate at 20°C, and levels remain elevated for the duration of the cold stress. Light-derived metabolic capability, and not light per se, is required...

2006

Owttrim, George W.

RNA helicases function as molecular motors that rearrange RNA secondary structure, potentially performing roles in any cellular process involving RNA metabolism. Although RNA helicase association with a range of cellular functions is well documented, their importance in response to abiotic stress...

2005

Owttrim, George W., Chamot, Danuta, Kujat-Choy, Sonya L., Colvin, Kimberley R.

Rearrangement of RNA secondary structure is crucial for numerous biological processes. RNA helicases participate in these rearrangements through the unwinding of duplex RNA. We report here that the redox-regulated cyanobacterial RNA helicase, CrhR, is a bona fide RNA helicase possessing both...

2009-01-01

Tzeng, Jennifer, Lee, Brian L., Sykes, Brian D., Fliegel, Larry

The Na+/H+ exchanger isoform 1 is a ubiquitously expressed integral membrane protein. It resides on the plasma membrane of cells and regulates intracellular pH in mammals by extruding an intracellular H+ in exchange for one extracellular Na+. We characterized structural and functional aspects of...

2009-01-01

Lee, Brian L., Li, Xiuju J., Liu, Yongsheng, Sykes, Brian D., Fliegel, Larry

The Na+/H+ exchanger isoform 1 is a ubiquitously expressed integral membrane protein that regulates intracellular pH in mammals by extruding an intracellular H+ in exchange for one extracellular Na+. We characterized structural and functional aspects of the critical transmembrane (TM) segment XI...

2005-01-01

Slepkov, Emily R., Rainey, Jan K., Li, Xiuju J., Liu, Yonghsheng S., Cheng, Florence J., Lindhout, Darrin A., Sykes, Brian D., Fliegel, Larry

The Na+/H+ exchanger isoform 1 is a ubiquitously expressed integral membrane protein that regulates intracellular pH in mammals. We characterized the structural and functional aspects of the critical transmembrane (TM) segment IV. Each residue was mutated to cysteine in cysteine-less NHE1. TM IV...

2008-01-01

Reddy, Tyler, Ding, Jie, Li, Xiuju J., Sykes, Brian D., Rainey, Jan K., Fliegel, Larry

The Na+/H+ exchanger isoform 1 (NHE1) is an integral membrane protein that regulates intracellular pH by removing one intracellular H+ in exchange for one extracellular Na+. It has a large N-terminal membrane domain of 12 transmembrane segments and an intracellular C-terminal regulatory domain....

2006-01-01

Ding, Jie, Rainey, Jan K., Xu, Caroline, Sykes, Brian D., Fliegel, Larry

The Na+/H+ exchanger isoform 1 is an integral membrane protein that regulates intracellular pH by exchanging one intracellular H+ for one extracellular Na+. It is composed of an N-terminal membrane domain of 12 transmembrane segments and an intracellular C-terminal regulatory domain. We...

Spring 2016

Cochrane, Stephen A.

The lipopeptides, tridecaptin A1, tridecaptin B1 and cerexin A1 were isolated from Paenibacillus terrae NRRL B-30644, Paenibacillus polymyxa NRRL B-30507 and Bacillus mycoides ATCC 21929, respectively. A combination of chemical synthesis, peptide derivatization, high performance liquid...