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Actin dynamic behavior is regulated by a large number of binding proteins, which drive intracellular and extracellular signaling pathways.
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Most of these transporters belong to the superfamily of ATP-binding cassette (ABC) proteins, which drive the cellular extrusion of many therapeutic drugs with different structures and clinical uses.
ATP-binding cassette (ABC) transporters are membrane proteins which drive the transport of compounds over the biological membranes.
The researchers focused on a class of bacterial proteins called periplasmic binding proteins, which have the unusual characteristic of closing up, like a Venus flytrap, when they bind to a particular chemical.
In the murine 3T3-L1 preadipocell cell model, adipogenic signals induce the differentiation markers PPARγ and C/EBPα (CCAAT/enhancer-binding protein α), which drive terminal adipocyte differentiation and lipid accumulation [ 28– 31].
In this context, ERK1, ERK2, cAMP and CaMKIV function as synapse-to-nucleus communicators to trigger the activation of the cAMP response element-binding protein (CREB), which drives the expression of a variety of pain-related proteins, such as COX-2, TRPV1 and Ca2+ channels, among others (see Poster, panel D) (Kawasaki et al., 2004).
These effects are coupled to the activation of the actin-binding protein moesin, which drives actin fibers to the cell membrane, increasing the formation of specialized membrane structures which interact with the extracellular matrix and with nearby cells, thus allowing the cells to achieve locomotion.
Endoglin, a TGF-beta binding protein which maps to chromosome 9q3, is the gene for HHT1.
Calcium-dependent regulator protein is a low molecular weight (17,000), thermostable, calcium binding protein which is structurally homologous to skeletal muscle troponin C.
The v-myb oncogene and its cellular homolog c-myb encode sequence-specific DNA-binding proteins which regulate transcription from promoters containing Myb-binding sites in animal cells.
This Gram-positive bacterium possesses specific surface proteins such as fibronectin-binding proteins, collagen-binding proteins, and fibrinogen-binding proteins, which have been implicated as mediators in specific bacterial binding to the extracellular matrix and subsequent biofilm development [1, 5 7].
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