@article{pysz_rinker_shockley_kelly_2001, title={Continuous cultivation of hyperthermophiles}, volume={330}, journal={Hyperthermophilic enzymes. Part A}, publisher={San Diego, Calif.: Academic Press}, author={Pysz, M. A. and Rinker, K. D. and Shockley, K. R. and Kelly, R. M.}, year={2001}, pages={31–40} }
 @article{rinker_han_kelly_1999, title={Continuous culture as a tool for investigating the growth physiology of heterotrophic hyperthermophiles and extreme thermoacidophiles}, volume={85}, number={1999}, journal={Journal of Applied Microbiology}, author={Rinker, K. D. and Han, C. J. and Kelly, R. M.}, year={1999}, pages={118S–127} }
 @article{hicks_rinker_baker_kelly_1998, title={Homomultimeric protease in the hyperthermophilic bacterium Thermotoga maritima has structural and amino acid sequence homology to bacteriocins in mesophilic bacteria}, volume={440}, ISSN={["0014-5793"]}, DOI={10.1016/S0014-5793(98)01451-3}, abstractNote={A novel homomultimeric protease (>669 kDa), based on 31 kDa subunits, was purified from cell extracts of the hyperthermophilic bacterium Thermotoga maritima. This protease exhibits activity toward chymotrypsin and trypsin substrates, optimally at 90°C and pH 7.1, and has a half‐life of 36 min at 95°C. Transmission electron microscopy established that the protease consists of a large globular assembly which appears circular from the front view. The function of this protease in T. maritima remains unclear, although putative homologs include a 29 kDa antigen from Mycobacterium tuberculosis and a 31 kDa monomer of a high molecular weight bacteriocin produced by Brevibacterium linens [Valdes‐Stauber, N. and Scherer, S. (1996) Appl. Environ. Microbiol. 62, 1283–1286]. The relationship of these mesophilic proteins to the T. maritima protease suggests that their antibacterial activity may involve elements of proteolysis, and raises the prospect for anti‐microbial ecological strategies in hyperthermophilic niches.}, number={3}, journal={FEBS LETTERS}, author={Hicks, PM and Rinker, KD and Baker, JR and Kelly, RM}, year={1998}, month={Dec}, pages={393–398} }
 @article{muralidharan_rinker_hirsh_bouwer_kelly_1997, title={Hydrogen transfer between methanogens and fermentative heterotrophs in hyperthermophilic cocultures}, volume={56}, DOI={10.1002/(sici)1097-0290(19971105)56:3<268::aid-bit4>3.0.co;2-h}, abstractNote={Interactions involving hydrogen transfer were studied in a coculture of two hyperthermophilic microorganisms: Thermotoga maritima, an anaerobic heterotroph, and Methanococcus jannaschii, a hydrogenotrophic methanogen. Cell densities of T. maritima increased 10-fold when cocultured with M. jannaschii at 85 degrees C, and the methanogen was able to grow in the absence of externally supplied H(2) and CO(2). The coculture could not be established if the two organisms were physically separated by a dialysis membrane, suggesting the importance of spatial proximity. The significance of spatial proximity was also supported by cell cytometry, where the methanogen was only found in cell sorts at or above 4.5 microm in samples of the coculture in exponential phase. An unstructured mathematical model was used to compare the influence of hydrogen transport and metabolic properties on mesophilic and hyperthermophilic cocultures. Calculations suggest the increases in methanogenesis rates with temperature result from greater interactions between the methanogenic and fermentative organisms, as evidenced by the sharp decline in H(2) concentration in the proximity of a hyperthermophilic methanogen. The experimental and modeling results presented here illustrate the need to consider the interactions within hyperthermophilic consortia when choosing isolation strategies and evaluating biotransformations at elevated temperatures.}, number={3}, journal={Biotechnology and Bioengineering}, author={Muralidharan, V. and Rinker, K. D. and Hirsh, I. S. and Bouwer, E. J. and Kelly, Robert}, year={1997}, pages={268–278} }