Publications by authors named "K Prat"
Article Synopsis
- Only a few transcription factors have been identified in the malaria-causing parasite Plasmodium falciparum; this study aims to improve our understanding of its transcription machinery.
- Using advanced sequence analysis methods, the researchers predicted several general transcription factors associated with RNA polymerase II within the P. falciparum genome.
- The findings indicate that more transcription factors may exist in P. falciparum than previously thought, paving the way for future research into transcriptional regulation and the roles of various orphan proteins in this parasite.
Article Synopsis
- The report identifies protein fragments in various proteins that have similarities to the chymosin-sensitive bond found in kappa-caseins.
- This bond is found within a beta-strand structure, consistent with predictions for kappa-caseins.
- The study shows that chymosin can cleave glutamine synthetase at the same Phe-Met bond, indicating a potential resemblance between the glutamine synthetase and kappa-casein interactions with chymosin.
Understanding the formation of metazoan multigene families is a good approach to reconstitute the evolution of the chordate genome. In this attempt, the analysis of the genome of selected species provides valuable information. Ciona intestinalis belongs to the urochordates, whose lineage separated from the chordate lineage that later gave birth to vertebrates.
View Article and Find Full Text PDFStructural features of prions explored by sequence analysis. II. A PrP(Sc) model.
Cell Mol Life Sci
December 2002
Prion diseases are neurodegenerative disorders associated with a conformational conversion of the prion PrP protein, in which the beta strand content increases and that of the a helix decreases. However, the structure of the pathogenous form PrP(Sc), occurring after conformational conversion of the normal cellular form PrP(C), is not yet known. From sequence analysis, we have previously proposed that helix H2 of the prion PrP(C) structure might be a key region for this structural conversion.
View Article and Find Full Text PDFArticle Synopsis
- The study investigates how native alpha-crystallins interact with beta(LOW)- and gamma-crystallins during their denaturation at high temperatures using small angle x-ray scattering (SAXS) and fluorescence energy transfer (FRET).
- SAXS results show that alpha-crystallins undergo significant size and molecular weight changes when exposed to temperatures above 60 degrees C, which are vital for their association with other crystallins.
- FRET experiments reveal that heat-modified alpha-crystallins maintain subunit exchange ability, but the rate of exchange decreases when they associate with different gamma-crystallins and beta(LOW)-, showing variability among gamma-crystallin family members in their interaction with alpha-crystallins.