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This phosphorylation, along with modifications of other residues, blocks the p53-Mdm2 interaction, leading to p53 stabilization and an increase in p53 activity [ 56].
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Second, IN is absolutely required for viral replication and mutations in a number of key residues block the viral replication.
Replacement of the Cdc5 phsophorylation sites with phosphomimetic mutants partially bypassed the requirement for Cdc5 in Rho localization and actin ring formation whereas mutation of the phosphorylation sites to nonphosphorylatable residues blocked Rho localization and actin assembly.
Moreover, the O –methylguanine adducts crosslink with the opposite cytosine residues, blocking DNA replication [ 11].
The less restrictive single tyrosine mutant, Vangl2 (Y280A), interacted weakly with μ1-adaptin whereas mutating both tyrosine residues blocked interaction.
These results indicated that the mutation of XRCC1's 518S/519T/523T residues blocked the negative JWA regulation of XRCC1.
Individual modifications of histones may be interdependent, with methylation of certain lysine residues blocking or enhancing the addition of acetyl groups nearby [ 8, 9].
Briefly, 20 μl (55 μg) of each sample was reduced and the cysteine residues blocked with MMTS before digesting each sample with trypsin.
Thymosin alpha1 (T α1) is a heat-stable, acidic polypeptide composed of 28 amino acid residues blocked at the N-terminus by an acetyl group [ 6, 7].
We review diverse roles of TEIIs (removal of aberrant residues blocking the megasynthase, participation in substrate selection, intermediate, and product release) and discuss their application in new biosynthetic systems utilizing PKS and NRPS parts.
Our data showed that the mutation of 518S/519T/523T residues blocked the negative regulation of JWA on XRCC1, indicating the critical role of 518S/519T/523T phosphorylation in negative regulation of XRCC1 by JWA.
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