dimer

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Related to Heterodimerize: Homodimer

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.

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]

dimer

/di·mer/ (di´mer)
1. a compound formed by combination of two identical molecules.
2. a capsomer having two structural subunits.

dimer

[dī′mər]
Etymology: Gk, di, twice, meros, parts
a compound formed by the union of two radicals or two molecules of a single simpler compound.

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]

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.

dimer

chemical compound formed by the union of two identical molecules.
References in periodicals archive ?
When activated, PPAR[gamma] heterodimerizes with retinoid X receptor (RXR), binds to specific response elements (PPREs), and promotes the expression of target genes [13].
They also increase insulin secretion and function as ligands for peroxisome proliferator-activated receptor (PPAR)-gamma, which heterodimerizes with retinoic acid receptor.
Platelets and macrophages release most MRP-14, which heterodimerizes with MRP-8.
CHOP heterodimerizes with C/EBP[beta] and by binding to the promoter region of Hsp60 increases its transcription levels [60].
Nuclear factor erythroid 2-related factor 2 (Nrf2), which belongs to the basic leucine zipper (bZIP) transcription factor and heterodimerizes with small Maf proteins, functions as a key player in the redox homeostatic gene regulatory network.
The AhR, on exposure to TCDD, translocates into the nucleus, where it heterodimerizes with the AhR nuclear translocator (ARNT).
As a member of the PER-ARNT-SIM (PAS) domain family of transcriptional regulators, ligand-activated AhR translocates to the nucleus and heterodimerizes with AhR nuclear translocator (ARNT), leading to toxic responses (Bock 1994).