dimer

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di·mer

 (dī′mər)
n.
A chemical compound or molecule consisting of two identical simpler molecules.


di·mer′ic (dī-mĕr′ĭk) adj.
American Heritage® Dictionary of the English Language, Fifth Edition. Copyright © 2016 by Houghton Mifflin Harcourt Publishing Company. Published by Houghton Mifflin Harcourt Publishing Company. All rights reserved.

dimer

(ˈdaɪmə)
n
(Chemistry) chem
a. a molecule composed of two identical simpler molecules (monomers)
b. a compound consisting of dimers
[C20: from di-1 + -mer]
Collins English Dictionary – Complete and Unabridged, 12th Edition 2014 © HarperCollins Publishers 1991, 1994, 1998, 2000, 2003, 2006, 2007, 2009, 2011, 2014

di•mer

(ˈdaɪ mər)

n.
1. a molecule composed of two identical, simpler molecules.
2. a polymer derived from two identical monomers.
[1905–10]
di•mer′ic (-ˈmɛr ɪk) adj.
Random House Kernerman Webster's College Dictionary, © 2010 K Dictionaries Ltd. Copyright 2005, 1997, 1991 by Random House, Inc. All rights reserved.

di·mer

(dī′mər)
Any of various chemical compounds made of two smaller, identical molecules (called monomers) that are linked together.
The American Heritage® Student Science Dictionary, Second Edition. Copyright © 2014 by Houghton Mifflin Harcourt Publishing Company. Published by Houghton Mifflin Harcourt Publishing Company. All rights reserved.
ThesaurusAntonymsRelated WordsSynonymsLegend:
Noun1.dimer - a compound whose molecules are composed of two identical monomersdimer - a compound whose molecules are composed of two identical monomers
chemical compound, compound - (chemistry) a substance formed by chemical union of two or more elements or ingredients in definite proportion by weight
Based on WordNet 3.0, Farlex clipart collection. © 2003-2012 Princeton University, Farlex Inc.
Translations
References in periodicals archive ?
As CHRM3 receptors were reported to heterodimerize with CHRM2, it is possible that CHRM3 genes share a few roles as CHRM2 genes and may have similar physiological effects (6).
In mammals, CLOCK and brain and muscle aryl hydrocarbon receptor nuclear translocator-like protein 1 (BMAL1 ; a homolog of CYCLE) heterodimerize and stimulate transcription and translation of PERIOD and a vertebrate, nonphotoreceptive CRYPTOCHROME (NPCRY).
PPARs heterodimerize with the retinoid X receptor and subsequently bind to peroxisome proliferator response elements (PPREs) in the DNA of target genes [2].
Upon blue light irradiation, CRY2 and CIB1 heterodimerize, and the transcriptional activator is recruited to the target locus, activating gene expression.
The protein products of the Per and Cry genes then accumulate in the cytoplasm, where they heterodimerize and reenter the nucleus to inhibit their own transcription.
Upon cytokine binding, IL-1 receptors heterodimerize, which recruit intracellular signaling molecules, including MyD88, IRAK, and TRAF6, then activate NF-[kappa]B, p38, JNK, and/or MAPK transcription factors, leading to transcription of target genes (such as IL-6, IL-5, IL-4, IL-8, mCp-1, and COX-2) [67].
Nrf2, once stabilized, is no longer repressed by Keap1 and becomes free to heterodimerize with members of the Maf family of transcription factors.
The protein is first synthesized as a latent 65 kDa proenzyme that is secreted via vesicles that bud from the Golgi apparatus, which then interacts with cell membrane HSPGs and other receptors, accumulates in endosomes, and undergoes processing at two proteolytic cleavage sites, located at Glu109-Ser110 and Gln157-Lys158, yielding 8- and 50-kDa subunits that heterodimerize to form the active enzyme.
SOHLH1 and SOHLH2 could heterodimerize with each other in vivo, as well as homodimerize.
While C3aR neither homodimerizes nor heterodimerizes, by contrast, C5aR and C5L2 both homo- and heterodimerize [26, 60].
The ARFs are known to bind DNA at auxin response element sequences (AuxREs) and activate or repress gene expression, while the Aux/IAAs heterodimerize with ARFs, preventing them from binding to DNA.