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Dimer
[[Biochemistry]] ====See Also==== In chemistry, a dimer refers to a molecule composed of two similar . . . halogen bonding. Its more common usage refers to dimers as certain types of sugar: sucrose, for example, . . . is a dimer of a glucose molecule and a fructose molecule. . . . particularly molecular and cellular biology, dimers are most often observed in signaling. They are . . . in biochemistry as well. In this case, a dimer is a protein complex made up of two subunits . . .
3K - last updated 2006-05-05 10:51 UTC by PeterDAdamo
G-protein-coupled receptors
[[Biochemistry]] ====See Also==== * [[Ligand]] * [[Receptor]] * [[Receptor antagonist]] * [[Second messengers]] . . . receptors can form homo- and/or hetero-dimers and possibly more complex oligomeric structures. . . . it is presently unproven that true hetero-dimers exist. Present bio-chemical and physical techniques . . . to differentiate between distinct homo-dimers assembled into an oligomer or true 1:1 hetero-dimers. . . . receptors can form homo- and/or heterodimers and possibly more complex oligomeric structures, . . .
10K - last updated 2006-07-08 10:41 UTC by PeterDAdamo
Histone
[[Genomics]] ====See Also==== * [[Allele]] * [[Chromatin]] * [[Chromosome]] * [[Deoxyribonucleic acid . . . The nucleosome core is formed of two H2A-H2B dimers and two H3-H4 dimers, forming two nearly symmetrical . . . image of the other). The H2A-H2B and H3-H4 dimers themselves also show pseudodyad symmetry. The . . . helix turn helix' motif (which allows the easy dimerisation). They also share the feature of long . . .
8K - last updated 2006-07-07 10:26 UTC by PeterDAdamo
Ornithine decarboxylase
[[Biochemistry]] ====See Also==== * [[Polyamines]] * [[Putrescine]] ====Description==== Ornithine decarboxylase . . . (ODC) is a homodimer of 461 amino acids (in humans, at least) that . . .
3K - last updated 2006-08-10 07:06 UTC by AlanGoldenberg
STAT3 signal transducer and activator of transcription 3 (acute-phase response factor)
[[Genomics]] ====See Also==== * [[G Quartet oligonucleotides]] * [[Interleukin-6 (IL-6)]] * [[Transcription . . . associated kinases, and then form homo- or heterodimers that translocate to the cell nucleus where they . . .
3K - last updated 2006-05-31 18:22 UTC by PeterDAdamo
STAT Protein
[[Genomics]] ====See Also==== * [[Cytokines]] * [[Janus kinase (JAK)]] * [[Transcription factors]] * . . . STAT4, STAT5a, STAT5b and STAT6. STAT1 homodimers are involved in type II interferon signalling, . . . type I interferon signalling, STAT1-STAT2 heterodimer combines with IRF9 (Interferon Response Factor) . . . residue in the STAT protein which promotes the dimerization of STAT monomers via their SH2 domain. . . . The phosphorylated dimer is then actively transported in the nucleus via . . .
3K - last updated 2006-06-26 11:09 UTC by PeterDAdamo
Signal transduction
[[Physiology]] ====See Also==== * [[Nitric Oxide]] * [[Proteasome]] * [[Second messengers]] ====Description==== . . . domain. The latter is also responsible for dimerization of most nuclearic receptors prior to DNA . . .
21K - last updated 2006-07-07 11:58 UTC by PeterDAdamo
Toll-like receptors (TLRs)
[[Immunology]] ====See Also==== * [[Interleukin-1 (IL-1)]] * [[Interleukin-6 (IL-6)]] * [[Interleukin-8 . . . a matter of semantics. TLRs function as a [[dimer]]. Though most TLRs appear to function as homodimers, . . . TLR2 forms heterodimers with TLR1 or TLR6, each dimer having a different . . . Each Toll-like receptor forms either a homodimer or heterodimer in the recognition of a specific . . .
8K - last updated 2006-05-23 07:33 UTC by AlanGoldenberg
Von Willebrand factor (vWF)
[[Biochemistry]] ====See Also==== * [[Factor VIII]] * [[Clotting factors]] ====Description==== <b>Von . . . [[Glycans|N-glycosylated]], arranged into [[Dimer|dimers]] in the endoplasmic reticulum and into . . .
6K - last updated 2007-05-29 03:53 UTC by AlanGoldenberg
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