dimer

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Related to Homodimerization: dimeric, Homodimers, Heterodimerization

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 ?
2011) Potentiation of Helicobacter pylori CagA protein virulence through homodimerization.
This mechanism involves sequential actions of E2, P4, IFNT, CSH1 and GH1 with biological actions of CSH1 being mediated by homodimerization of the PRLR or heterodimerization of the PRLR and GH1 receptor (Noel et al.
In normal ALK signaling, ligand-induced homodimerization of the extracellular domains brings the tyrosine kinase domains into sufficient proximity to enable transphosphorylation and kinase activity, whereas translocations resulting in pathogenic fusion partners provide dimerization domains that are ligand-independent, leading to unregulated constitutive kinase activity.
Upon ligand binding, receptor homodimerization or heterodimerization occurs, which is followed by autophosphorylation and activation of the tyrosine kinase domains.
After ligand binding, KIT undergoes homodimerization, transphosphorylation of tyrosine residues in its intracellular domain, and subsequent phosphorylation of downstream members of the RAS/RAF/MAPK, JAK/STAT, and PI3K/AKT signaling pathways, thus controlling cell proliferation, apoptosis, chemotaxis, and metabolism.
HER2 does not have a ligand and relies on heterodimerization with another family member or homodimerization with itself when expressed at very high levels to be activated.