dimer

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Related to Dimerizes: Heterodimeric, Dimerisation

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 ?
Thus, Nrf2 translocates to the nucleus where it dimerizes with a small Maf protein and binds to the antioxidant response element (ARE) sequence within regulatory regions of a wide variety of target genes [191, 192].
Binding of TCDD to AHR causes the dissociation of the receptor from the complex and its translocation into the nucleus, where it dimerizes with the AHR nuclear translocator (ARNT).
When activated, the HER2/neu protein dimerizes and activates various signaling pathways to potentiate a variety of cellular functions including promoting cell division while inhibiting apoptosis.
To bind, Nrf2 dimerizes with other basic leucine zipper (bZIP) proteins such as small Maf proteins (Maf G) to form a transactivation complex that binds to AREs [53].
N6AMT1 dimerizes with tRNA methyl transferase 11-2 homolog (TRMT112), which appears to be necessary for proper N6AMT1 function (Figaro et al.
216-218) Phosphorylated STAT3 dimerizes and translocates to the nucleus, where it increases the transcription of antiapoptotic molecules (B-cell lymphoma 2 [BCL2], B-cell lymphoma-extra large [BCL-xL], survivin, myeloid cell leukemia sequence 1 [MCL1]) and cell cycle regulators such as cyclin D3.