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Exact(8)
Histone modifications are catalyzed by a number of enzyme complexes, including the NuRD/Mi2 complex [4].
These modifications are catalyzed by small nucleolar ribonucleoparticles (snoRNPs) through specific base-paring between their RNA component (snoRNA) with the surrounding of the position to be modified.
These modifications are catalyzed by distinct enzymes.
Most of these modifications are catalyzed by specific enzymes that have evolved for their respective tasks.
The snoRNA-dependent modifications are catalyzed by small nucleolar ribonucleoprotein particles (snoRNPs).
Histone modifications are catalyzed by many enzymes such as histone acetyltransferases (HATs), histone deacetylases (HDACs), histone methyltransferases (HMTs), and histone demethylases (HDMs).
Similar(52)
Phosphorylation, one of the more recognizable post-translational modifications, is catalyzed by kinases while the reverse reaction is carried out by phosphatases.
It is recognized that histone modification is catalyzed by several enzymes which modulate the histone markers.
This modification is catalyzed by Clr4, a homolog of the mammalian histone methyltransferase, SUV39H1 (Nakayama et al., 2001b).
The required modification is catalyzed by the ubiquitinating complex, LUBAC; the RLR-activated IRF3 is recruited to LUBAC via TRAF2- and TRAF6-dependent mechanism.
This modification is catalyzed by a family of evolutionarily conserved enzymes called protein arginine methyltransferases (PRMTs).
Related(20)
modifications are facilitated
modifications are mediated
modifications are generated
modifications are created
modifications are preferred
modifications are listed
modifications are explained
modifications are used
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modifications are described
modifications are attenuated
modifications are presented
modifications are needed
modifications are outlined
modifications are required
modifications are proposed
modifications are accompanied
modifications are recommended
modifications are made
modifications are determined
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