dimer

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dimer

 
1. a compound formed by combination of two identical simpler molecules.
2. a capsomer having two structural subunits.
D-dimer a fragment of fibrin that is formed as a result of fibrin degradation. A positive test for its presence in the blood is suggestive of conditions such as thrombotic disease, sickle cell crisis, malignancy, disseminated intravascular coagulation, or recent surgery.
Miller-Keane Encyclopedia and Dictionary of Medicine, Nursing, and Allied Health, Seventh Edition. © 2003 by Saunders, an imprint of Elsevier, Inc. All rights reserved.

di·mer

(dī'mĕr),
A compound or unit produced by the combination of two like molecules; in the strictest sense, this occurs without the loss of atoms (thus, nitrogen tetroxide, N2O4, is the dimer of nitrogen dioxide, NO2), but usually by elimination of H2O or a similar small molecule between the two (for example, a disaccharide), or by simple noncovalent association (as of two identical protein molecules); higher orders of complexity are called trimers, tetramers, oligomers, and polymers.
[G. di-, two, + -mer]
Farlex Partner Medical Dictionary © Farlex 2012

di·mer

(dī'mĕr)
A compound or unit produced by the combination of two like molecules; in the strictest sense, without loss of atoms (thus nitrogen tetroxide, N2O4, is the dimer of nitrogen dioxide, NO2), but usually by elimination of H2O or a similar small molecule between the two (e.g., a disaccharide), or by simple noncovalent association (as of two identical protein molecules); higher orders of complexity are called trimers, tetramers, oligomers, and polymers.
[G. di-, two, + -mer]
Medical Dictionary for the Health Professions and Nursing © Farlex 2012

dimer

a molecule made by the joining of two molecules of the same kind, i.e. two MONOMERS. Ultraviolet light can induce THYMINE DIMERS in DNA.
Collins Dictionary of Biology, 3rd ed. © W. G. Hale, V. A. Saunders, J. P. Margham 2005
References in periodicals archive ?
The UVRAG CCD heterodimerizes with the Beclin 1 CCD, disrupting the Beclin 1 CCD homodimer and increasing autophagy levels in the cell.
Considering that S273 phosphorylation by CDK5 is unique to PPAR[gamma], this event is important for dictating binding to the promoter of potential target genes related to glucose and lipid regulation, since PPAR[gamma] heterodimerizes with DBD region of RXR[alpha] via the [beta]-sheet domain in which S273 resides.
On transforming growth factor [beta]/activin receptor activation, SMAD2 and SMAD3 proteins are phosphorylated and heterodimerize with the SMAD4 protein.
Peroxisome proliferator activated receptorsa (PPAR[gamma]) are ligand-activated nuclear hormone receptors that heterodimerize with the retinoid x receptor and act to control the expression of genes involved in cellular metabolism and differentiation (Desvergne and Whahli, 1999).
Ecdsyteroids, such as ecdysone, exhert their effects through the interaction with the ecdysone receptor (EcR), known to heterodimerize with RXR and to bind to the promoters of ecdysone-regulated genes (LeBlanc 2007; Wang and LeBlanc 2009).
As C5L2 and C5aR heterodimerize [16], the ratio of C5L2/C5aR was evaluated.
Coexpression experiments indicated that survivin can heterodimerize with its splice variants.
PPARs heterodimerize with retinoid-X receptors (RXR) and mediate transcriptional activation by binding to specific DNA promoter sequences in target genes.
After binding with their agonists (natural or synthetic) in cytoplasm, PPARs heterodimerize with the retinoid acid receptor (RNR or NR2B) and translocate to the nucleus, subsequently binding to specific DNA regions termed peroxisome proliferator response elements (PPREs).
Rel family members function as dimers and the five subunits can homodimerize or heterodimerize. All family members share a Rel homology domain, which contains the crucial functional regions for DNA binding, dimerization, nuclear localization, and interactions with the I[kappa]B inhibitory proteins.
Because PPARy and RXRa heterodimerize, organotins stimulate both parts of the heterodimer complex.
Corepressor dissociation allows the receptors to heterodimerize with retinoid X receptors and initiate transcription by binding to specific PPAR response elements in the promoter regions of their target genes [10].