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FN is known to bind several receptors of the integrin family [ 22, 28], and 120-kDa FN-f, which contains the cell-binding RGD sequence, may bind to and stimulate the α5β1 integrin receptor, subsequently increasing cytokine and chemokine expression through p38 or JNK mitogen-activated protein kinase (MAPK) activation and the NF-κB-dependent pathway [ 29, 30].
Y-box protein 2 (Ybx2) is an RNA-binding protein in germ cells but also has the ability to bind to and stimulate transcription of the mouse protamine-2 promoter [ 60].
It is noteworthy that all of these proinflammatory mediators bind to and stimulate specific receptors expressed in the peripheral terminals of nociceptors (pain-mediating sensory nerve fibers) [ 4].
However, soluble forms of E-cadherin have also been shown to directly bind to and stimulate the growth factor receptors, epidermal growth factor receptor (EGFR), Her2, and Her3 [ 22, 23, 28], activating cell signaling pathways.
These studies were extended to show that haptenated DNA could bind to and stimulate TLR9 in B cell expressing hapten-specific receptors [ 22], further clarifying that autoantigens bound by the B-cell receptor can be delivered to the proper intracellular compartment to trigger TLR9 activation.
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For example, Fowler et al. [ 24, 25] demonstrated that increased ERα expression in MCF7 cells resulted in activation of ER-responsive gene even in the absence of estrogen, that proves the ability of unliganded ER dimers to bind to ERE and stimulate transcription.
Its secondary role is linked to innate immunity because some surfactant proteins bind to pathogens and stimulate their phagocytosis and lysis.
Microtubule-associated proteins (MAPs) are primarily recognized as cytosolic proteins that bind to tubulin and stimulate their polymerization.
VEGFR1-specific ligands such as PlGF and VEGF-B bind to monocytes and stimulate intracellular signalling events including ERK1/2 (extracellular signal-regulated kinase 1/2), Akt and p38 MAPK pathways [ 91].
For example, MYC [ 6] and the MAP kinase ERK [ 7] bind to TFIIIB and stimulate its activity, whereas an array of tumor suppressors inhibit TFIIIB activity [ 8], either directly or indirectly, including BRCA1 [ 9], PTEN [ 10, 11], p53 [ 12], and the RB family [ 13].
Rather, HLA-G binds to and stimulates signaling via the leukocyte immunoglobulin-like receptors (LILRB1/ILT2/CD85j) as well as LILRB2/ILT4/CD85d) and KIR2DL4 (CD158d) [25].
More suggestions(17)
bind to and colonize
bind to and help
bind to and affect
bind to and kill
bind to and release
bind to and stabilize
bind to and uptake
bind to and facilitate
bind to and internalize
bind to and respond
bind to and enter
bind to and promote
bind to and regulate
bind to and integrate
bind to and move
bind to and oxidize
bind to and induce
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