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These novel diagnostic agents produce high contrast images due to their fast clearance from the bloodstream and healthy tissues, can be evolved to bind a multitude of cancer biomarkers, and are easily functionalized by site-specific bioconjugation methods.
These proteins are able to bind a multitude of different signaling proteins including kinases, phosphatases and transmembrane receptors and play a major role in modulating a wide range of regulatory processes such as mitogenic signal transduction, cell cycle control, ion channel regulation, and apoptosis [36].
HS chains, unique in their ability to bind a multitude of proteins, ensure that a wide variety of bioactive molecules bind to the cell surface and ECM and thereby function in the control of diverse normal and pathological processes [1], [4], [5].
Because RBM44 carries an RNA recognition motif (RRM) and the RRM could potentially bind a multitude of RNA sequences and proteins (reviewed in reference [29]), we suspect that RBM44 may function as an RNA-binding protein required for intercellular bridge function.
A striking feature of the 14-3-3 14-3-3 14-3-3heir ability to bind a multitude of functionally diverse signaling proteins, iscluding kinases, phosphatheir, abilitynsmembrane receptors.
Another way in which p300/CBP is able to respond to signaling pathways is due to the ability of p300/CBP to bind a multitude of different proteins, using its various protein-interacting domains.
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Heparin binds a multitude of growth factors and maintains their bioactivity for an extended period of time.
The c-myc product, Myc, is a transcription factor that binds a multitude of genomic sites, estimated to be over 10 15% of all promoter regions.
Our results show that wt p53 binds a multitude of promoter sequences causing increases in histone H3 and H4 acetylation.
Aptamers are an interesting alternative to antibodies in pharmaceutics and biosensorics, because they are able to bind to a multitude of possible target molecules with high affinity.
Biochemical work studying methyl-CpG binding proteins over the past twenty years has revealed that in addition to specifically associating with methylated CpG dinucleotides, these proteins also bind to a multitude of different chromatin modifying enzymes, including histone deacetylases and histone lysine methyltransferases.
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