% IMPORTANT: The following is UTF-8 encoded.  This means that in the presence
% of non-ASCII characters, it will not work with BibTeX 0.99 or older.
% Instead, you should use an up-to-date BibTeX implementation like “bibtex8” or
% “biber”.

@ARTICLE{RootBernstein:842944,
      author       = {Root-Bernstein, Robert and Turke, Miah and Subhramanyam,
                      Udaya and Churchill, Beth and Labahn, Jörg},
      title        = {{A}drenergic {A}gonists {B}ind to
                      {A}drenergic-{R}eceptor-{L}ike {R}egions of the {M}u
                      {O}pioid {R}eceptor, {E}nhancing {M}orphine and
                      {M}ethionine-{E}nkephalin {B}inding: {A} {N}ew {A}pproach to
                      "{B}iased {O}pioids"?},
      journal      = {International journal of molecular sciences},
      volume       = {19},
      number       = {1},
      issn         = {1422-0067},
      address      = {Basel},
      publisher    = {Molecular Diversity Preservation International},
      reportid     = {FZJ-2018-01107},
      pages        = {272},
      year         = {2018},
      abstract     = {Extensive evidence demonstrates functional interactions
                      between the adrenergic and opioid systems in a diversity of
                      tissues and organs. While some effects are due to receptor
                      and second messenger cross-talk, recent research has
                      revealed an extracellular, allosteric opioid binding site on
                      adrenergic receptors that enhances adrenergic activity and
                      its duration. The present research addresses whether opioid
                      receptors may have an equivalent extracellular, allosteric
                      adrenergic binding site that has similar enhancing effects
                      on opioid binding. Comparison of adrenergic and opioid
                      receptor sequences revealed that these receptors share very
                      significant regions of similarity, particularly in some of
                      the extracellular and transmembrane regions associated with
                      adrenergic binding in the adrenergic receptors. Five of
                      these shared regions from the mu opioid receptor (muOPR)
                      were synthesized as peptides and tested for binding to
                      adrenergic, opioid and control compounds using ultraviolet
                      spectroscopy. Adrenergic compounds bound to several of these
                      muOPR peptides with low micromolar affinity while
                      acetylcholine, histamine and various adrenergic antagonists
                      did not. Similar studies were then conducted with purified,
                      intact muOPR with similar results. Combinations of
                      epinephrine with methionine enkephalin or morphine increased
                      the binding of both by about half a log unit. These results
                      suggest that muOPR may be allosterically enhanced by
                      adrenergic agonists. View Full-Text Keywords: biased
                      opioids; morphine; methionine-enkephalin; epinephrine;
                      norepinephrine; enhancement; synergy; allosteric; mu opioid
                      receptor; receptor dimers; dimerization},
      cin          = {ICS-6},
      ddc          = {570},
      cid          = {I:(DE-Juel1)ICS-6-20110106},
      pnm          = {551 - Functional Macromolecules and Complexes (POF3-551)},
      pid          = {G:(DE-HGF)POF3-551},
      typ          = {PUB:(DE-HGF)16},
      UT           = {WOS:000424407200266},
      pubmed       = {pmid:29342106},
      doi          = {10.3390/ijms19010272},
      url          = {https://juser.fz-juelich.de/record/842944},
}