User:Andor J Kiss: Difference between revisions
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<!-- Replace the PubMed ID's ("pmid=#######") below with the PubMed ID's for your publications. You can add or remove lines as needed --> | <!-- Replace the PubMed ID's ("pmid=#######") below with the PubMed ID's for your publications. You can add or remove lines as needed --> | ||
<biblio> | <biblio> | ||
#Paper1 Kiss,A.J. and Cheng,C-H.C. (2008). Molecular diversity and genomic organisation of the α, β and γ eye lens crystallins from the Antarctic toothfish ''Dissostichus mawsoni'' [http://dx.doi.org/10.1016/j.cbd.2008.02.002 doi:10.1016/j.cbd.2008.02.002] | #Paper1 Kiss,A.J. and Cheng,C-H.C. (2008). Molecular diversity and genomic organisation of the α, β and γ eye lens crystallins from the Antarctic toothfish ''Dissostichus mawsoni'' [http://dx.doi.org/10.1016/j.cbd.2008.02.002 doi:10.1016/j.cbd.2008.02.002] | ||
#Paper2 pmid=15579559 | #Paper2 pmid=15579559 | ||
// The above paper was an Editorial feature entitled [http://jeb.biologists.org/cgi/content/full/207/26/iii Blindingly Cold] in the Journal of Experimental Biology | // The above paper was an Editorial feature entitled [http://jeb.biologists.org/cgi/content/full/207/26/iii Blindingly Cold] in the Journal of Experimental Biology | ||
#Book1 isbn=XXXXXXXXXX | #Book1 isbn=XXXXXXXXXX | ||
Revision as of 05:17, 17 December 2008
Contact Info
- Visiting Assistant Professor
- Department of Zoology
- 194 Pearson Hall
- Miami University
- Oxford, OH 45056
I work in collaboration with the Laboratory for Ecophysiological Cryobiology and am a member of the Center for Visual Sciences at Miami University.
Education
- 2005, PhD, University of Illinois at Urbana-Champaign
- 1999, MSc, University of Western Ontario
- 1994, BSc, University of Victoria
Research interests
- My research interests are in the adaptive and evolutionary mechanism of animals. More specifically I am interested in vertebrate animals and their adaptation to extreme cold and heat, and how their physiological systems have evolved to allow them to exploit such niches. The model system that I have been using is that of the proteins in the eye lens. The proteins are called “crystallins” and play an important role in light refraction. Most vertebrates (excluding some birds) have three kinds of crystallins; alpha (α), beta (β) and gamma (γ). Alpha crystallin is also a type of small heat shock (sHSP) protein and comes in at least two flavours (isoforms). One of these α isoforms can be found widely expressed outside the eye lens and has important roles as a stress protein in a number of tissues. The β and γ crystallins are part of the same super-gene family, but presently there are no known non-refractive structure/function roles. Adaptation of ectothermic vertebrate lenses to cold is of interest to me as means of modeling not only lens cataracts, but to modeling globular protein stability. Lens cataract is a rare example of a system that allows investigation into stability of globular non-enzymatic proteins and protein systems.
- Interest 2
- Interest 3
Publications
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Kiss,A.J. and Cheng,C-H.C. (2008). Molecular diversity and genomic organisation of the α, β and γ eye lens crystallins from the Antarctic toothfish Dissostichus mawsoni doi:10.1016/j.cbd.2008.02.002
- Kiss AJ, Mirarefi AY, Ramakrishnan S, Zukoski CF, Devries AL, and Cheng CH. Cold-stable eye lens crystallins of the Antarctic nototheniid toothfish Dissostichus mawsoni Norman. J Exp Biol. 2004 Dec;207(Pt 26):4633-49. DOI:10.1242/jeb.01312 |
The above paper was an Editorial feature entitled Blindingly Cold in the Journal of Experimental Biology
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isbn=XXXXXXXXXX
