@misc{Sikorski_Michał_M._Struktura_1999,
 author={Sikorski, Michał M. and Biesiadka, Jacek},
 volume={46},
 number={3},
 copyright={Creative Commons Attribution BY-SA 4.0 license},
 journal={Biotechnologia, vol.46, 3 (1999)-.},
 howpublished={online},
 year={1999},
 publisher={Committee on Biotechnology PAS},
 publisher={Institute of Bioorganic Chemistry PAS},
 language={pol},
 abstract={Intracellular Pathogenesis-Related (IPR) Proteins of PRIO class are ubiquitous in the plantkingdom. Their homologues were found in both monocotyledonous and dicotyledonous plants.PRIO proteins are small polypeptides of Mj. 16 000- 18 000, slightly acidic and resistant toproteases. The absence of an apparent signal peptide and their structural properties indicatethat they are cytosolic. PRIO proteins are encoded by small multigene families. They accumulatearound sites of pathogen invasion, wounding and are induced by other environmental stress,suggesting their involvement in a general defence mechanism. The physiological function andany contribution of PRIO proteins to a defence mechanism remains unknown. However, highamino acid sequence homology and the similarity of the expression pattern with that of ginsengribonuclease suggest that an RNase activity associated with these proteins may be involved inthe defence reaction.},
 title={Struktura i organospecyficzna ekspresja genów kodujących roślinne białka klasy PR 10},
 type={Text},
 URL={http://rcin.org.pl/Content/142608/PDF/POZN271_177920_biotechnologia-1999-no3-sikorski.pdf},
 keywords={biotechnology},
}