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HMGB1 was initially identified as a widely existing DNA binding protein, which changes the chromatin or DNA configuration and regulates the transcription complex formation [ 6].
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As a result, increased levels of cytoplasmic β-catenin accumulate and become available for nuclear translocation and binding to T-cell factor/lymphoid enhancer factor (TCF/LEF) DNA binding proteins, which change transcription of target genes [17].
This difference is due the binding of cations at four binding sites on the surface of the protein, which changes its net charge thereby increasing repulsive interactions and urate oxidase solubility.
The β-subunit of F1 has a region that is topologically equivalent to the switch II region of guanine-nucleotide binding (G) proteins, which changes the conformation in response to the interconversion of GTP and GDP.
Endoglin, a TGF-beta binding protein which maps to chromosome 9q3, is the gene for HHT1.
Other CDS variations shared by several T. whipplei strains encode either hypothetical proteins (9 cases), membrane proteins (1 case), or FtsE, a cell division ATP-binding protein (which had nucleotide changes in the Dig7, DigADP11, Art1, DigMusc17, and DigNeuro18 strains).
The CRF1 is a G protein-coupled receptor that changes conformation upon CRF binding to promote the coupling of GTP binding proteins, which initiate intracellular signaling cascades [ 51, 112].
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.
This study emphasizes that locally controlled levels of phosphoinositides are important for regulating the function of actin-binding proteins which effect changes in the membrane architecture.
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].
This section will focus on new ways of label-free EC analysis of DNA protein interactions, which play significant roles in nature (such as DNA sequence-specific binding), and in which changes in the protein EC signals are monitored.
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