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                  <div class="result" id="summary">
                     <div class="searchText">Nat Rev Mol Cell Biol [journal]</div>
                     <div class="searchCount">1453 results</div>
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                  <div class="result">
                     <ul>
                        <li class="author">Minton K&nbsp;</li>
                        <li class="title"><a href="./citation/23756622/Cell_adhesion:_Integrating_the_integrin_response_">Cell adhesion: Integrating the integrin response.<span class="title-pubtype"> [JOURNAL ARTICLE]</span></a></li>
                        <li class="source" title="Nature reviews. Molecular cell biology">Nat Rev Mol Cell Biol 2013&nbsp;Jun&nbsp;12.</li>
                        <li class="links"><span class="fulltext" data-link="http://dx.doi.org/10.1038/nrm3605">Publisher Full Text</span></li>
                     </ul>
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                  <div class="result">
                     <ul>
                        <li class="author">Wrighton KH&nbsp;</li>
                        <li class="title"><a href="./citation/23756621/Autophagy:_Kinase_crosstalk_through_beclin_1_">Autophagy: Kinase crosstalk through beclin 1.<span class="title-pubtype"> [JOURNAL ARTICLE]</span></a></li>
                        <li class="source" title="Nature reviews. Molecular cell biology">Nat Rev Mol Cell Biol 2013&nbsp;Jun&nbsp;12.</li>
                        <li class="links"><span class="fulltext" data-link="http://dx.doi.org/10.1038/nrm3608">Publisher Full Text</span></li>
                     </ul>
                  </div>
                  <div class="result">
                     <ul>
                        <li class="author">Baumann K&nbsp;</li>
                        <li class="title"><a href="./citation/23756620/Cell_adhesion:_Extracellular_bonds_">Cell adhesion: Extracellular bonds.<span class="title-pubtype"> [JOURNAL ARTICLE]</span></a></li>
                        <li class="source" title="Nature reviews. Molecular cell biology">Nat Rev Mol Cell Biol 2013&nbsp;Jun&nbsp;12.</li>
                        <li class="links"><span class="fulltext" data-link="http://dx.doi.org/10.1038/nrm3607">Publisher Full Text</span></li>
                     </ul>
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                  <div class="result">
                     <ul>
                        <li class="author">Schuldt A&nbsp;</li>
                        <li class="title"><a href="./citation/23756619/Development:_PTEN_regulates_junction_dynamics_">Development: PTEN regulates junction dynamics.<span class="title-pubtype"> [JOURNAL ARTICLE]</span></a></li>
                        <li class="source" title="Nature reviews. Molecular cell biology">Nat Rev Mol Cell Biol 2013&nbsp;Jun&nbsp;12.</li>
                        <li class="links"><span class="fulltext" data-link="http://dx.doi.org/10.1038/nrm3610">Publisher Full Text</span></li>
                     </ul>
                  </div>
                  <div class="result">
                     <ul>
                        <li class="author">Hetz C&nbsp;</li>
                        <li class="title"><a href="./citation/23756618/The_biological_meaning_of_the_UPR_">The biological meaning of the UPR.<span class="title-pubtype"> [JOURNAL ARTICLE]</span></a></li>
                        <li class="source" title="Nature reviews. Molecular cell biology">Nat Rev Mol Cell Biol 2013&nbsp;Jun&nbsp;12.</li>
                        <li class="links"><span class="fulltext" data-link="http://dx.doi.org/10.1038/nrm3606">Publisher Full Text</span></li>
                     </ul>
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                  <div class="result">
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                        <li class="author">Du Toit A&nbsp;</li>
                        <li class="title"><a href="./citation/23736682/Meiosis:_A_kinesin_on_foreign_tracks_">Meiosis: A kinesin on foreign tracks.<span class="title-pubtype"> [JOURNAL ARTICLE]</span></a></li>
                        <li class="source" title="Nature reviews. Molecular cell biology">Nat Rev Mol Cell Biol 2013&nbsp;Jun&nbsp;5.</li>
                        <li class="links"><span class="fulltext" data-link="http://dx.doi.org/10.1038/nrm3604">Publisher Full Text</span></li>
                     </ul>
                  </div>
                  <div class="result">
                     <ul>
                        <li class="author">Feijs KL, Forst AH, Verheugd P, et al.&nbsp;</li>
                        <li class="title"><a href="./citation/23736681/Macrodomain_containing_proteins:_regulating_new_intracellular_functions_of_mono_ADP_ribosyl_ation_">Macrodomain-containing proteins: regulating new intracellular functions of mono(ADP-ribosyl)ation.<span class="title-pubtype"> [JOURNAL ARTICLE]</span></a></li>
                        <li class="source" title="Nature reviews. Molecular cell biology">Nat Rev Mol Cell Biol 2013&nbsp;Jun&nbsp;5.</li>
                        <li class="links"><span class="abstractButton">Abstract</span><span class="fulltext" data-link="http://dx.doi.org/10.1038/nrm3601">Publisher Full Text</span></li>
                     </ul>
                     <div class="abstract-wrapper" style="display: none;">
                        <div class="abstract">ADP-ribosylation of proteins was first described in the early 1960's, and today the function and regulation of poly(ADP-ribosyl)ation
                           (PARylation) is partially understood. By contrast, little is known about intracellular mono(ADP-ribosyl)ation (MARylation)
                           by ADP-ribosyl transferase (ART) enzymes, such as ARTD10. Recent findings indicate that MARylation regulates signalling and
                           transcription by modifying key components in these processes. Emerging evidence also suggests that specific macrodomain-containing
                           proteins, including ARTD8, macroD1, macroD2 and C6orf130, which are distinct from those affecting PARylation, interact with
                           MARylation on target proteins to 'read' and 'erase' this modification. Thus, studying macrodomain-containing proteins is key
                           to understanding the function and regulation of MARylation.
                        </div>
                     </div>
                  </div>
                  <div class="result">
                     <ul>
                        <li class="author">David R&nbsp;</li>
                        <li class="title"><a href="./citation/23736680/DNA_repair:_A_sensor_for_chromatin_damage_">DNA repair: A sensor for chromatin damage.<span class="title-pubtype"> [JOURNAL ARTICLE]</span></a></li>
                        <li class="source" title="Nature reviews. Molecular cell biology">Nat Rev Mol Cell Biol 2013&nbsp;Jun&nbsp;5.</li>
                        <li class="links"><span class="fulltext" data-link="http://dx.doi.org/10.1038/nrm3603">Publisher Full Text</span></li>
                     </ul>
                  </div>
                  <div class="result">
                     <ul>
                        <li class="author">Bouvard D, Pouwels J, De Franceschi N, et al.&nbsp;</li>
                        <li class="title"><a href="./citation/23719537/Integrin_inactivators:_balancing_cellular_functions_in_vitro_and_in_vivo_">Integrin inactivators: balancing cellular functions in vitro and in vivo.<span class="title-pubtype"> [JOURNAL ARTICLE]</span></a></li>
                        <li class="source" title="Nature reviews. Molecular cell biology">Nat Rev Mol Cell Biol 2013&nbsp;May&nbsp;30.</li>
                        <li class="links"><span class="abstractButton">Abstract</span><span class="fulltext" data-link="http://dx.doi.org/10.1038/nrm3599">Publisher Full Text</span></li>
                     </ul>
                     <div class="abstract-wrapper" style="display: none;">
                        <div class="abstract">Integrins mediate cell-matrix and cell-cell interactions and integrate extracellular cues to the cytoskeleton and cellular
                           signalling pathways. Integrin function on the cell surface is regulated by their activity switching such that intracellular
                           proteins interacting with the integrin cytoplasmic domains increase or decrease integrin-ligand binding affinity. It is widely
                           accepted that integrin activation by specific proteins is essential for cell adhesion and integrin linkage to the actin cytoskeleton.
                           However, there is also increasing evidence that integrin-inactivating proteins are crucial for appropriate integrin function
                           in vitro and in vivo and that the regulation of integrin-ligand interactions is a fine-tuned balancing act between inactivation
                           and activation.
                        </div>
                     </div>
                  </div>
                  <div class="result">
                     <ul>
                        <li class="author">Briscoe J, Th&eacute;rond PP&nbsp;</li>
                        <li class="title"><a href="./citation/23719536/The_mechanisms_of_Hedgehog_signalling_and_its_roles_in_development_and_disease_">The mechanisms of Hedgehog signalling and its roles in development and disease.<span class="title-pubtype"> [JOURNAL ARTICLE]</span></a></li>
                        <li class="source" title="Nature reviews. Molecular cell biology">Nat Rev Mol Cell Biol 2013&nbsp;May&nbsp;30.</li>
                        <li class="links"><span class="abstractButton">Abstract</span><span class="fulltext" data-link="http://dx.doi.org/10.1038/nrm3598">Publisher Full Text</span></li>
                     </ul>
                     <div class="abstract-wrapper" style="display: none;">
                        <div class="abstract">The cloning of the founding member of the Hedgehog (HH) family of secreted proteins two decades ago inaugurated a field that
                           has diversified to encompass embryonic development, stem cell biology and tissue homeostasis. Interest in HH signalling increased
                           when the pathway was implicated in several cancers and congenital syndromes. The mechanism of HH signalling is complex and
                           remains incompletely understood. Nevertheless, studies have revealed novel biological insights into this system, including
                           the function of HH lipidation in the secretion and transport of this ligand and details of the signal transduction pathway,
                           which involves Patched 1, Smoothened and GLI proteins (Cubitus interruptus in Drosophila melanogaster), as well as, in vertebrates,
                           primary cilia.
                        </div>
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