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.

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]

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.
References in periodicals archive ?
Abbreviations SpCas9: Cas9 from Streptococcus pyogenes SaCas9: Cas9 from Staphylococcus aureus PAM: Protospacer-adjacent motif NLS: Nuclear localization signal CRY2: Light-inducible heterodimerizing cryptochrome 2 CIB1: Calcium- and integrin-binding protein 1 4-HT: 4-Hydroxytamoxifen VPR: Chimeric activation domain composed of the activation domainsVP64, P65, and Rta pdDronpa: Engineered GFP that dimerizes in the dark LOV: Photomodulated dimerizing protein ER-LBD: Ligand-binding domain of the estrogen receptor.
Future studies should be directed to understanding which integrin subunits dimerize as well as to identifying the actual ligands, both in the extracellular matrix and on the sperm surface, for these dimers.
CHOP, a novel developmentally regulated nuclear protein that dimerizes with transcription factors C/EBP and LAP and functions as a dominant-negative inhibitor of gene transcription.
The phosphorylated Stats dimerize, translocate to the nucleus, and drive transcription of their target genes (Figure 1) [2].
Full activation of STAT3 requires phosphorylation at its tyr705 and ser727 residues, which allows it to dimerize and translocate into the nucleus [25, 26].
Because dialkylsilylene 31 is sterically well protected and does not dimerize to the corresponding disilene either in solution or in the solid state, tethering two dialkylsilylene moieties may be possible to give a stable tethered bissilylene.
Less hindered analogs efficiently and rapidly dimerize, at carbon, with concomitant protonation or oxygen-methylation depending on added electrophile.
In the absence of a strong neutral donor, the indium(II) species will obviously dimerize, and this dimer can then disproportionate by halide transfer c.f.
Upon activation by PAMPs or DAMPs, TLR monomers dimerize, and their cytosolic domains subsequently recruit adaptor proteins from the MyD88 family (MyD88, TRIF/TICAM-1, TIRAP/Mal, TIRP/TRAM, and SRAM), thereby initiating downstream signaling pathways [84] (Figure 1).
Under these conditions, some of the fatty acids dimerize, a lesser amount trimerizes, and some isomerizes to monomer.
In general, after expressed the TLRs dimerize and undergo conformational changes to bind to their respective PAMPs through interaction of toll/interleukin 1 (IL-1) receptor domain-containing adaptor molecules such as the myeloid differentiation primary response gene 88 (MyD88) (Yamamoto et al., 2002; Oshiumi et al., 2003).