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The transcription, translation, processing, and secretion of multiple proteins at high concentration are an intrinsically energy-intensive process.
This allows the simultaneous quantification, by flow cytometry, of multiple proteins at a very low concentration (10 2500 pg/mL) in serum samples.
What these two patterns essentially suggest is that the allelic imbalances of multiple proteins at a single SNP are correlated and have high preference to be skewed toward the same allele.
As tumors typically evade cancer treatment by acquiring secondary mutations on targeted proteins, it appears more difficult for a tumor to escape from miRNA effects, which are directed on multiple proteins at the same time.
In theory, these two innovations may have served to link the cadherin catenin "core" to many other proteins in the cadhesome, thereby integrating multiple proteins at the origin of metazoa.
Third, assembly of multiple proteins at replication origins to form active helicase may be suitable for multiple regulations that sense many signals, not only environmental nutrients but also cell cell interactions etc.
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Applications of concurrent SPRM/SPRF include the ability to monitor the the thickness and physiochemical properties of surface layers simultaneously [13], the detection and quantification of multiple analytes onto a surface [14], [15], and to study reactions between multiple proteins interacting at a surface [16].
CFTR synthesis, processing and destruction are all complex processes [ 3, 14, 15] and a recent review suggest that CFTR binds multiple proteins, perhaps at different times and in different cellular locations creating a plasticity of interactions [ 16].
In fact, flow cytometry allows for testing multiple proteins or peptides at a single time and provides at the same time a quantitative and phenotypic assessment of CD8 and CD4 responding T cells.
However, it is not clearly understood how the expression of these multiple proteins is regulated at gene level and further detailed molecular and proteomic analysis will provide the mechanism on the metabolic role of cell-bound regulatory proteins and the cell-substrate interactions.
Peroxynitrite interacts with and modifies multiple proteins and enzymes at tyrosine residues to form nitrotyrosine. Protein nitrotyrosylation may either up- or down-regulate activities of cellular pathways in a target-dependent manner [8] [10].
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