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Cho, K. C., & Chan, K. K. (1984). Kinetics of cold-induced denaturation of metmyoglobin. Biochimica et Biophysica Acta (BBA) – Protein Structure and Molecular Enzymology, 786(1-2), 103–108.
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Crowell-Davis, S. L., Houpt, K. A., & Carnevale, J. (1985). Feeding and drinking behavior of mares and foals with free access to pasture and water. J. Anim Sci., 60(4), 883–889.
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Hughes, K. L., & Sulaiman, I. (1987). The ecology of Rhodococcus equi and physicochemical influences on growth. Vet Microbiol, 14(3), 241–250.
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Shaw, E. B., Houpt, K. A., & Holmes, D. F. (1988). Body temperature and behaviour of mares during the last two weeks of pregnancy. Equine Vet J, 20(3), 199–202.
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Steinhoff, H. J., Lieutenant, K., & Redhardt, A. (1989). Conformational transition of aquomethemoglobin: intramolecular histidine E7 binding reaction to the heme iron in the temperature range between 220 K and 295 K as seen by EPR and temperature-jump measurements. Biochim Biophys Acta, 996(1-2), 49–56.
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Steinhoff, H. J., Schrader, J., & Schlitter, J. (1992). Temperature-jump studies and polarized absorption spectroscopy of methemoglobin-thiocyanate single crystals. Biochim Biophys Acta, 1121(3), 269–278.
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Ballew, R. M., Sabelko, J., & Gruebele, M. (1996). Direct observation of fast protein folding: the initial collapse of apomyoglobin. Proc. Natl. Acad. Sci. U.S.A., 93(12), 5759–5764.
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Duncan, I. J. H., Widowski, T. M., Malleau, A. E., Lindberg, A. C., & Petherick, J. C. (1998). External factors and causation of dustbathing in domestic hens. Behav. Process., 43(2), 219–228.
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Gilmanshin, R., Callender, R. H., & Dyer, R. B. (1998). The core of apomyoglobin E-form folds at the diffusion limit. Nat Struct Biol, 5(5), 363–365.
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McCutcheon, L. J., & Geor, R. J. (2000). Influence of training on sweating responses during submaximal exercise in horses. J Appl Physiol, 89(6), 2463–2471.
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