Inside Cover: The Conformational Equilibrium of the Neuropeptide Y2 Receptor in Bilayer Membranes (Angew. Chem. Int. Ed. 52/2020)
NMR spectroscopy sheds light on receptor activation: Molecular switches are conserved motifs of G protein‐coupled receptors that undergo structural changes during activation. Tryptophan residues are often part of these molecular switches and thus provide insights in the activation mechanism of the m...
Gespeichert in:
| Veröffentlicht in: | Angewandte Chemie International Edition 2020-12, Vol.59 (52), p.23346-23346 |
|---|---|
| Hauptverfasser: | , , , , , , , , , , , , |
| Format: | Artikel |
| Sprache: | eng |
| Schlagworte: | |
| Online-Zugang: | Volltext |
| Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
| container_end_page | 23346 |
|---|---|
| container_issue | 52 |
| container_start_page | 23346 |
| container_title | Angewandte Chemie International Edition |
| container_volume | 59 |
| creator | Krug, Ulrike Gloge, Anika Schmidt, Peter Becker‐Baldus, Johanna Bernhard, Frank Kaiser, Anette Montag, Cindy Gauglitz, Marcel Vishnivetskiy, Sergey A. Gurevich, Vsevolod V. Beck‐Sickinger, Annette G. Glaubitz, Clemens Huster, Daniel |
| description | NMR spectroscopy sheds light on receptor activation: Molecular switches are conserved motifs of G protein‐coupled receptors that undergo structural changes during activation. Tryptophan residues are often part of these molecular switches and thus provide insights in the activation mechanism of the molecule. In their Research Article on page 23854, D. Huster and co‐workers use NMR spectroscopy to monitor structural alterations of the neuropeptide Y1 receptor with atomic resolution observable by changes in the chemical shifts of six native tryptophan residues. |
| doi_str_mv | 10.1002/anie.202014454 |
| format | Article |
| fullrecord | <record><control><sourceid>wiley_cross</sourceid><recordid>TN_cdi_crossref_primary_10_1002_anie_202014454</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>ANIE202014454</sourcerecordid><originalsourceid>FETCH-LOGICAL-c1294-7cf7fc8956446d26acb2d239722a9aac337ac0496259328bd401d036645e98023</originalsourceid><addsrcrecordid>eNqFkD1PwzAQhi0EEqWwMnuEIal9dj7MVqIAkUqRUBmYIsdxqFHiFCel6sg_J1ERjEz3nvQ8p9OL0CUlPiUEZtIa7QMBQjkP-BGa0ACox6KIHQ-ZM-ZFcUBP0VnXvQ98HJNwgr4y25lS46T91O4Gr9ZjtFXrGtmb1soapx9bU5vCmW2D2wr3A7HUW9du9KYfzVfAz1oNS-uwsfjW1HKvHX7UTeGk1R2-mts3vfNxstaNjzPb-zgtfRzAbHz2-hydVLLu9MXPnKKXu3SVPHiLp_ssmS88RUFwL1JVVKlYBCHnYQmhVAWUwEQEIIWUirFIKsJFCIFgEBclJ7QkLAx5oEVMgE2Rf7irXNt1Tlf5xplGun1OST4WmI8F5r8FDoI4CDtT6_0_dD5fZumf-w3y0HIz</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype></control><display><type>article</type><title>Inside Cover: The Conformational Equilibrium of the Neuropeptide Y2 Receptor in Bilayer Membranes (Angew. Chem. Int. Ed. 52/2020)</title><source>Wiley Online Library Journals Frontfile Complete</source><creator>Krug, Ulrike ; Gloge, Anika ; Schmidt, Peter ; Becker‐Baldus, Johanna ; Bernhard, Frank ; Kaiser, Anette ; Montag, Cindy ; Gauglitz, Marcel ; Vishnivetskiy, Sergey A. ; Gurevich, Vsevolod V. ; Beck‐Sickinger, Annette G. ; Glaubitz, Clemens ; Huster, Daniel</creator><creatorcontrib>Krug, Ulrike ; Gloge, Anika ; Schmidt, Peter ; Becker‐Baldus, Johanna ; Bernhard, Frank ; Kaiser, Anette ; Montag, Cindy ; Gauglitz, Marcel ; Vishnivetskiy, Sergey A. ; Gurevich, Vsevolod V. ; Beck‐Sickinger, Annette G. ; Glaubitz, Clemens ; Huster, Daniel</creatorcontrib><description>NMR spectroscopy sheds light on receptor activation: Molecular switches are conserved motifs of G protein‐coupled receptors that undergo structural changes during activation. Tryptophan residues are often part of these molecular switches and thus provide insights in the activation mechanism of the molecule. In their Research Article on page 23854, D. Huster and co‐workers use NMR spectroscopy to monitor structural alterations of the neuropeptide Y1 receptor with atomic resolution observable by changes in the chemical shifts of six native tryptophan residues.</description><identifier>ISSN: 1433-7851</identifier><identifier>EISSN: 1521-3773</identifier><identifier>DOI: 10.1002/anie.202014454</identifier><language>eng</language><subject>arrestin ; molecular switch ; NMR spectroscopy ; receptors ; structural dynamics</subject><ispartof>Angewandte Chemie International Edition, 2020-12, Vol.59 (52), p.23346-23346</ispartof><rights>2020 Wiley‐VCH GmbH</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><orcidid>0000-0002-3273-0943</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://onlinelibrary.wiley.com/doi/pdf/10.1002%2Fanie.202014454$$EPDF$$P50$$Gwiley$$H</linktopdf><linktohtml>$$Uhttps://onlinelibrary.wiley.com/doi/full/10.1002%2Fanie.202014454$$EHTML$$P50$$Gwiley$$H</linktohtml><link.rule.ids>314,776,780,1411,27903,27904,45553,45554</link.rule.ids></links><search><creatorcontrib>Krug, Ulrike</creatorcontrib><creatorcontrib>Gloge, Anika</creatorcontrib><creatorcontrib>Schmidt, Peter</creatorcontrib><creatorcontrib>Becker‐Baldus, Johanna</creatorcontrib><creatorcontrib>Bernhard, Frank</creatorcontrib><creatorcontrib>Kaiser, Anette</creatorcontrib><creatorcontrib>Montag, Cindy</creatorcontrib><creatorcontrib>Gauglitz, Marcel</creatorcontrib><creatorcontrib>Vishnivetskiy, Sergey A.</creatorcontrib><creatorcontrib>Gurevich, Vsevolod V.</creatorcontrib><creatorcontrib>Beck‐Sickinger, Annette G.</creatorcontrib><creatorcontrib>Glaubitz, Clemens</creatorcontrib><creatorcontrib>Huster, Daniel</creatorcontrib><title>Inside Cover: The Conformational Equilibrium of the Neuropeptide Y2 Receptor in Bilayer Membranes (Angew. Chem. Int. Ed. 52/2020)</title><title>Angewandte Chemie International Edition</title><description>NMR spectroscopy sheds light on receptor activation: Molecular switches are conserved motifs of G protein‐coupled receptors that undergo structural changes during activation. Tryptophan residues are often part of these molecular switches and thus provide insights in the activation mechanism of the molecule. In their Research Article on page 23854, D. Huster and co‐workers use NMR spectroscopy to monitor structural alterations of the neuropeptide Y1 receptor with atomic resolution observable by changes in the chemical shifts of six native tryptophan residues.</description><subject>arrestin</subject><subject>molecular switch</subject><subject>NMR spectroscopy</subject><subject>receptors</subject><subject>structural dynamics</subject><issn>1433-7851</issn><issn>1521-3773</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2020</creationdate><recordtype>article</recordtype><recordid>eNqFkD1PwzAQhi0EEqWwMnuEIal9dj7MVqIAkUqRUBmYIsdxqFHiFCel6sg_J1ERjEz3nvQ8p9OL0CUlPiUEZtIa7QMBQjkP-BGa0ACox6KIHQ-ZM-ZFcUBP0VnXvQ98HJNwgr4y25lS46T91O4Gr9ZjtFXrGtmb1soapx9bU5vCmW2D2wr3A7HUW9du9KYfzVfAz1oNS-uwsfjW1HKvHX7UTeGk1R2-mts3vfNxstaNjzPb-zgtfRzAbHz2-hydVLLu9MXPnKKXu3SVPHiLp_ssmS88RUFwL1JVVKlYBCHnYQmhVAWUwEQEIIWUirFIKsJFCIFgEBclJ7QkLAx5oEVMgE2Rf7irXNt1Tlf5xplGun1OST4WmI8F5r8FDoI4CDtT6_0_dD5fZumf-w3y0HIz</recordid><startdate>20201221</startdate><enddate>20201221</enddate><creator>Krug, Ulrike</creator><creator>Gloge, Anika</creator><creator>Schmidt, Peter</creator><creator>Becker‐Baldus, Johanna</creator><creator>Bernhard, Frank</creator><creator>Kaiser, Anette</creator><creator>Montag, Cindy</creator><creator>Gauglitz, Marcel</creator><creator>Vishnivetskiy, Sergey A.</creator><creator>Gurevich, Vsevolod V.</creator><creator>Beck‐Sickinger, Annette G.</creator><creator>Glaubitz, Clemens</creator><creator>Huster, Daniel</creator><scope>AAYXX</scope><scope>CITATION</scope><orcidid>https://orcid.org/0000-0002-3273-0943</orcidid></search><sort><creationdate>20201221</creationdate><title>Inside Cover: The Conformational Equilibrium of the Neuropeptide Y2 Receptor in Bilayer Membranes (Angew. Chem. Int. Ed. 52/2020)</title><author>Krug, Ulrike ; Gloge, Anika ; Schmidt, Peter ; Becker‐Baldus, Johanna ; Bernhard, Frank ; Kaiser, Anette ; Montag, Cindy ; Gauglitz, Marcel ; Vishnivetskiy, Sergey A. ; Gurevich, Vsevolod V. ; Beck‐Sickinger, Annette G. ; Glaubitz, Clemens ; Huster, Daniel</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c1294-7cf7fc8956446d26acb2d239722a9aac337ac0496259328bd401d036645e98023</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2020</creationdate><topic>arrestin</topic><topic>molecular switch</topic><topic>NMR spectroscopy</topic><topic>receptors</topic><topic>structural dynamics</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Krug, Ulrike</creatorcontrib><creatorcontrib>Gloge, Anika</creatorcontrib><creatorcontrib>Schmidt, Peter</creatorcontrib><creatorcontrib>Becker‐Baldus, Johanna</creatorcontrib><creatorcontrib>Bernhard, Frank</creatorcontrib><creatorcontrib>Kaiser, Anette</creatorcontrib><creatorcontrib>Montag, Cindy</creatorcontrib><creatorcontrib>Gauglitz, Marcel</creatorcontrib><creatorcontrib>Vishnivetskiy, Sergey A.</creatorcontrib><creatorcontrib>Gurevich, Vsevolod V.</creatorcontrib><creatorcontrib>Beck‐Sickinger, Annette G.</creatorcontrib><creatorcontrib>Glaubitz, Clemens</creatorcontrib><creatorcontrib>Huster, Daniel</creatorcontrib><collection>CrossRef</collection><jtitle>Angewandte Chemie International Edition</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Krug, Ulrike</au><au>Gloge, Anika</au><au>Schmidt, Peter</au><au>Becker‐Baldus, Johanna</au><au>Bernhard, Frank</au><au>Kaiser, Anette</au><au>Montag, Cindy</au><au>Gauglitz, Marcel</au><au>Vishnivetskiy, Sergey A.</au><au>Gurevich, Vsevolod V.</au><au>Beck‐Sickinger, Annette G.</au><au>Glaubitz, Clemens</au><au>Huster, Daniel</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Inside Cover: The Conformational Equilibrium of the Neuropeptide Y2 Receptor in Bilayer Membranes (Angew. Chem. Int. Ed. 52/2020)</atitle><jtitle>Angewandte Chemie International Edition</jtitle><date>2020-12-21</date><risdate>2020</risdate><volume>59</volume><issue>52</issue><spage>23346</spage><epage>23346</epage><pages>23346-23346</pages><issn>1433-7851</issn><eissn>1521-3773</eissn><abstract>NMR spectroscopy sheds light on receptor activation: Molecular switches are conserved motifs of G protein‐coupled receptors that undergo structural changes during activation. Tryptophan residues are often part of these molecular switches and thus provide insights in the activation mechanism of the molecule. In their Research Article on page 23854, D. Huster and co‐workers use NMR spectroscopy to monitor structural alterations of the neuropeptide Y1 receptor with atomic resolution observable by changes in the chemical shifts of six native tryptophan residues.</abstract><doi>10.1002/anie.202014454</doi><tpages>1</tpages><orcidid>https://orcid.org/0000-0002-3273-0943</orcidid><oa>free_for_read</oa></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 1433-7851 |
| ispartof | Angewandte Chemie International Edition, 2020-12, Vol.59 (52), p.23346-23346 |
| issn | 1433-7851 1521-3773 |
| language | eng |
| recordid | cdi_crossref_primary_10_1002_anie_202014454 |
| source | Wiley Online Library Journals Frontfile Complete |
| subjects | arrestin molecular switch NMR spectroscopy receptors structural dynamics |
| title | Inside Cover: The Conformational Equilibrium of the Neuropeptide Y2 Receptor in Bilayer Membranes (Angew. Chem. Int. Ed. 52/2020) |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-27T17%3A52%3A46IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-wiley_cross&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Inside%20Cover:%20The%20Conformational%20Equilibrium%20of%20the%20Neuropeptide%20Y2%20Receptor%20in%20Bilayer%20Membranes%20(Angew.%20Chem.%20Int.%20Ed.%2052/2020)&rft.jtitle=Angewandte%20Chemie%20International%20Edition&rft.au=Krug,%20Ulrike&rft.date=2020-12-21&rft.volume=59&rft.issue=52&rft.spage=23346&rft.epage=23346&rft.pages=23346-23346&rft.issn=1433-7851&rft.eissn=1521-3773&rft_id=info:doi/10.1002/anie.202014454&rft_dat=%3Cwiley_cross%3EANIE202014454%3C/wiley_cross%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_id=info:pmid/&rfr_iscdi=true |