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The careful annotation of well-described MoRFs in terms of their sequence propensities or interaction interfaces as well as their known binding partners, and integration of these annotations with MoRF predictions, would likely improve the use of these predictions for gaining insight into IDR functionality.
This revealed that the unraveling occurs in a series of steps that correspond well to the known binding modes.
As tension increases from 0 8 pN, the number of wrapped nucleotides decreases in a stepwise manner from 65 to 56 to ∼35 nt, matching very well to the known binding modes.
The MAPs (microtubule-associated proteins) MAP1B and tau are well known for binding to microtubules and stabilizing these structures.
HSA is well known for binding a large variety of molecules, including fatty acids, drugs, hormones, and metal ions [27].
It is well known that binding of PRC2 with the p16 promoter can initiate reversible repression of its transcription through EZH2-mediated trimethylation of histone H3 at lysine 27 (H3K27me3 [10] [12]].
It is well known that binding of miRNAs with their targets is strongly affected by the nucleotides in the 5' end of the miRNA MRE duplex[53], [59], and that, in contrast to the strict requirement for base pairing at the proximal region, nucleotide mismatch at the distal region seems to be highly tolerated.
HSA is well known for binding a large variety of molecules, including fatty acids, drugs, hormones, and metal ions [ 27].
The well known substrate binding differences at the active sites of SULT1A1/1A2 and SULT1A3 (and now SULT1A4) substantiate these findings.
It is well known that binding of SV-40 large-T-antigen to the wild-type p53 completely inactivates its transcription activity [ 41].
Several of the primary-response gene transcripts include those that code for the well known DNA binding transcription factors Eip75B and br as well as vrille which is consistent with the model that primary-response proteins are required for the transcriptional induction of the secondary-response genes.
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