dimerization

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dimerization

[‚dī·mər·ə′zā·shən]
(chemistry)
A chemical reaction in which two identical molecular entities react to form a single dimer.
McGraw-Hill Dictionary of Scientific & Technical Terms, 6E, Copyright © 2003 by The McGraw-Hill Companies, Inc.
References in periodicals archive ?
A recent study explored the photomodulated dimerizing protein domains known as pdDronpa [71], a green fluorescent protein which dimerizes in the dark but dissociates to monomers upon illumination with light at 500 nm [72].
When a cytokine binds to a receptor in the JAK-STAT pathway, the receptor dimerizes and JAKs are activated.
Calcium-sensing receptor dimerizes in the endoplasmic reticulum: biochemical and biophysical characterization of CASR mutants retained intracellularly.
As in any one-dimensional structure with a half-filled electronic band, these stacked radicals are prone to a charge density wave or Peierls instability, i.e., a tendency to dimerize.
In addition, the disease-related mutation DJ-1 L166P shifts its subcellular distribution to the nucleus and decreases its ability to dimerize, whereas BAG1, the first discovered BAG family protein, restores DJ-1 L166P subcellular distribution and dimerization [36].
Activated STATs dimerize and translocate into the nucleus binding to the promoter of target genes and activating their transcription.
The Zwitterion can dimerize to form diperoxide (4) or give a higher peroxide (5).
The starlet sea anemone Nematostella vectensis has at least two [alpha] integrin subunits and four [beta] integrin subunits available to dimerize and bind to the extracellular matrix or mediate sperm-egg interactions.
Gilis, "Modelling and bioinformatics analysis of the dimeric structure of house dust mite allergens from families 5 and 21: der f 5 could dimerize as der p 5," Journal of Biomolecular Structure and Dynamics, vol.
Upon tyrosine phosphorylation, STAT3 proteins dimerize, translocate to the nucleus, and activate certain target genes specifically such as the cis-element IFN-stimulated response element (ISRE), thereby originating transcription of numerous IFN-inducible genes.
Upon accumulation in the cytoplasm to a critical level, the proteins of PER and CRY dimerize and translocate into the nucleus to repress the transcriptional activity of BMAL1:CLOCK/NPAS2 complex, thereby shutting down their own transcription.
In addition to its critical role in regulating ER stress-mediated apoptosis, CHOP10 may dimerize with C/EBP[beta] and C/EBP[alpha] to serve as a transcriptional inhibitor in the regulation of adipogenesis (Ron and Habener 1992).