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In the case of rbcL mRNA, it has been shown that the rbcL protein itself has an N-terminal RNA binding domain that could have a role in mediating its own translational arrest by binding its own 5′ UTR [ 60].
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This region, which is known as the tail, might therefore represent an alternative cargo-binding domain that could account for some of the KLC-independent functions of KHC.
While the class C enzymes are methyltransferases, they are thought to utilize a different mechanism than the class A or B enzymes, given that they contain neither a conserved cysteine nor a cobalamin-binding domain that could be used in methyl transfer.
By nested reverse transcription-polymerase chain reaction (RT-PCR) we identified a high number of splice variants including noncoding transcripts and predicted coding ones with different potential protein modifications affecting mainly the transmembrane and ligand-binding domains that could influence their biological function.
Like its T. gondii orthologue (Fang et al., 2006), Plasmodium PI-PLC has a predicted N-terminal Pleckstrin homology (PH) domain presumably required for targeting PI-PLC to the plasma membrane, and a bipartite catalytic domain flanked by Ca2+-binding EF hands and a C2 domain that could be involved in binding to membrane phospholipids in a Ca2+-dependent or independent manner.
Inspection of the structure also indicated significant changes to the conformations of D270 and P329 in the CH2 domain that could negatively impact C1q binding.
Since many BORIS isoproteins possess a ZF DNA binding domain that is highly similar to that of CTCF, their expression in the same cell could interfere with the binding of CTCF to its targets.
BESS domain is a protein binding domain that can interact each other or with other domains.
This was originally proposed to act as a generic mechanism to dislodge KDM4 from chromatin at DNA damage sites, as KDM4 enzymes encode H4K20me-binding Tudor domains that could block efficient occupancy of the damage response protein 53BP1 [ 201], which also recognizes this modification [ 202, 203].
These include the ubiquitin E3 ligase domains with the treble clef fold, such as the B-Box, U-box and different types of RING fingers, the "Little finger", which is a ubiquitin-binding Zn-ribbon, and ubiquitin-like domains that could also bind Ub [ 15, 16].
However, SAF-B has a SAP domain, a non-sequence-specific DNA-binding domain that shows preference for SAR/MAR DNAs[34], and could be recruited to chromatin compartments as a result of direct binding.
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