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Wyszukujesz frazę "methyltransferases" wg kryterium: Temat


Wyświetlanie 1-3 z 3
Tytuł:
Mammalian DNA methyltransferases
Autorzy:
Siedlecki, Pawel
Zielenkiewicz, Piotr
Powiązania:
https://bibliotekanauki.pl/articles/1041231.pdf
Data publikacji:
2006
Wydawca:
Polskie Towarzystwo Biochemiczne
Tematy:
DNA methyltransferases
DNA methylation
Opis:
DNA methylation is an epigenetic process affecting gene expression and chromatin organization. It can heritably silence or activate transcription of genes without any change in their nucleotide sequences, and for a long time was not recognized as an important regulatory mechanism. However, during the recent years it has been shown that improper methylation, especially hypermethylation of promoter regions, is observed in nearly all steps of tumorigenesis. Aberrant methylation is also the cause of several major pathologies including developmental disorders involving chromosome instabilities and mental retardation. A great progress has been made in our understanding of the enzymatic machinery involved in establishing and maintaining methylation patterns. This allowed for the development of new diagnostic tools and epigenetic treatment therapies. The new approaches hold a great potential; several inhibitors of DNA methyltransferases have already shown very promising therapeutic effects.
Źródło:
Acta Biochimica Polonica; 2006, 53, 2; 245-256
0001-527X
Pojawia się w:
Acta Biochimica Polonica
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
Understanding the evolution of restriction-modification systems: Clues from sequence and structure comparisons.
Autorzy:
Bujnicki, Janusz
Powiązania:
https://bibliotekanauki.pl/articles/1044038.pdf
Data publikacji:
2001
Wydawca:
Polskie Towarzystwo Biochemiczne
Tematy:
protein structure
methyltransferases
bioinformatics
molecular evolution
endonucleases
Opis:
Restriction-modification (RM) systems comprise two opposing enzymatic activities: a restriction endonuclease, that targets specific DNA sequences and performs endonucleolytic cleavage, and a modification methyltransferase that renders these sequences resistant to cleavage. Studies on molecular genetics and biochemistry of RM systems have been carried out over the past four decades, laying foundations for modern molecular biology and providing important models for mechanisms of highly specific protein-DNA interactions. Although the number of known, relevant sequences 3D structures of RM proteins is growing steadily, we do not fully understand their functional diversities from an evolutionary perspective and we are not yet able to engineer new sequence specificities based on rational approaches. Recent findings on the evolution of RM systems and on their structures and mechanisms of action have led to a picture in which conserved modules with defined function are shared between different RM proteins and other enzymes involved in nucleic acid biochemistry. On the other hand, it has been realized that some of the modules have been replaced in the evolution by unrelated domains exerting similar function. The aim of this review is to give a survey on the recent progress in the field of structural phylogeny of RM enzymes with special emphasis on studies of sequence-structure-function relationships and emerging potential applications in biotechnology.
Źródło:
Acta Biochimica Polonica; 2001, 48, 4; 935-967
0001-527X
Pojawia się w:
Acta Biochimica Polonica
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
Molecular dynamics and structural comparison approach to understanding the role of knots in proteins
Autorzy:
Perlinska, A. P.
Macnar, J. M.
Sulkowska, J. I.
Powiązania:
https://bibliotekanauki.pl/articles/1938625.pdf
Data publikacji:
2016
Wydawca:
Politechnika Gdańska
Tematy:
knotted proteins
methyltransferases
TrmD
Trm5
TrmJ
Trm7
Opis:
The role of knots in proteins is still unclear. In this short review, we summarize the current knowledge about structural and dynamical differences between knotted and unknotted proteins. We show how the topological difference helps to distinguish the physical properties, characterize the biological activity or identify the biological function of knotted proteins. This knowledge can be used to correctly annotate protein family members and to identify new members.
Źródło:
TASK Quarterly. Scientific Bulletin of Academic Computer Centre in Gdansk; 2016, 20, 4; 373-381
1428-6394
Pojawia się w:
TASK Quarterly. Scientific Bulletin of Academic Computer Centre in Gdansk
Dostawca treści:
Biblioteka Nauki
Artykuł
    Wyświetlanie 1-3 z 3

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