dimer

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Related to Homodimers: dimeric, Heterodimerization, Homodimeric

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 intrinsic propensity of HLA-B* 27 heavy chain (B27-HC) allows it to fold slowly in the ER, resulting in the accumulation of misfolded B27-HC and formation of a heavy-chain homodimer, [(B27-HC).sub.2], which is covalently linked by a disulfide bond at Cys-67 [8-10].
A and B chains of 3-phytase B initially form a homodimer (Figure 3) (PDB ID: 1QFX) and its 2D structure corresponds to 38% alpha helices, 12% beta sheets, and 50% random coils.
(2012) Transient GPI-anchored protein homodimers are units for raft organization and function.
In the absence of JH, Met is present as an inactive homodimer. Upon JH binding to the PAS-B domain, Met undergoes a conformational change that liberates Met from the homodimer complex and allows it to bind Taiman [43,45-47].
Two cysteine residues were engineered in the Fos and Jun zipper domains to produce disulfide-stabilized homodimers. This approach usually results in efficient production of stable, secreted homodimers that retain their specificity as assessed in a number of assays.
(39) recently proposed that sRAGE might not only function as a 'decoy' to exert its inhibitory effects on RAGE but also act in a more direct way by binding to the cell surface of RAGE to block the formation of homodimers. Hence, the decreased levels of sRAGE could contribute to enhanced RAGE-mediated pro-inflammatory signaling, thus supporting the possibility of the essential role of RAGE in SLE pathology.
In addition, the extracellular portion of CD4 could form homodimers to enhance immune response (Maekawa et al., 2006).
Among their topics are early-stage and late-stage intermediate folding, structural information involved in interpreting the stepwise protein folding process, using the "fuzzy oil drop" model to identify the complexation area in protein homodimers, misfolded proteins, and other selected ab initio methods for predicting protein structure.
NF-[kappa]B was a transcription factor, which was heterodimers or homodimers consisted of the members of the NF-[kappa]B family.
Schulman et al., "Activation of specific RXR heterodimers by an antagonist of RXR homodimers," Nature, vol.
We also found that the combination of the dual binding pattern of PPARgamma with the promiscuous heterodimerization of RXR with nuclear receptors at other HREbinding sites could contribute to the preserved binding of PPARgamma homodimers to Pal3 at low cellular expression of PPARgamma [20].
Thus, ZHX2 can form homodimers or heterodimers with other ZHX members [16], then interacts with the activation domain of NF-YA, and represses transcription of its regulable gene [17].