{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,2,25]],"date-time":"2026-02-25T18:21:46Z","timestamp":1772043706311,"version":"3.50.1"},"reference-count":12,"publisher":"Oxford University Press (OUP)","issue":"14","content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[2013,7,15]]},"abstract":"<jats:title>Abstract<\/jats:title>\n               <jats:p>Summary: Dynamics governing the function of biomolecule is usually described as exchange processes and can be monitored at atomic resolution with nuclear magnetic resonance (NMR) relaxation dispersion data. Here, we present a new tool for the analysis of CPMG relaxation dispersion profiles (ShereKhan). The web interface to ShereKhan provides a user-friendly environment for the analysis.<\/jats:p>\n               <jats:p>Availability: A stable version of ShereKhan, the web application and documentation are available at http:\/\/sherekhan.bionmr.org.<\/jats:p>\n               <jats:p>Contact: \u00a0dole@nmr.mpibpc.mpg.de or mako@nmr.mpibpc.mpg.de<\/jats:p>","DOI":"10.1093\/bioinformatics\/btt286","type":"journal-article","created":{"date-parts":[[2013,5,23]],"date-time":"2013-05-23T00:16:52Z","timestamp":1369268212000},"page":"1819-1820","source":"Crossref","is-referenced-by-count":22,"title":["ShereKhan\u2014calculating exchange parameters in relaxation dispersion data from CPMG experiments"],"prefix":"10.1093","volume":"29","author":[{"given":"Adam","family":"Mazur","sequence":"first","affiliation":[{"name":"Department of NMR-based Structural Biology, Max-Planck-Institute for Biophysical Chemistry, Am Fassberg 11, 37077 G\u00f6ttingen, Germany"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Bj\u00f6rn","family":"Hammesfahr","sequence":"additional","affiliation":[{"name":"Department of NMR-based Structural Biology, Max-Planck-Institute for Biophysical Chemistry, Am Fassberg 11, 37077 G\u00f6ttingen, Germany"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Christian","family":"Griesinger","sequence":"additional","affiliation":[{"name":"Department of NMR-based Structural Biology, Max-Planck-Institute for Biophysical Chemistry, Am Fassberg 11, 37077 G\u00f6ttingen, Germany"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Donghan","family":"Lee","sequence":"additional","affiliation":[{"name":"Department of NMR-based Structural Biology, Max-Planck-Institute for Biophysical Chemistry, Am Fassberg 11, 37077 G\u00f6ttingen, Germany"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Martin","family":"Kollmar","sequence":"additional","affiliation":[{"name":"Department of NMR-based Structural Biology, Max-Planck-Institute for Biophysical Chemistry, Am Fassberg 11, 37077 G\u00f6ttingen, Germany"}],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"286","published-online":{"date-parts":[[2013,5,21]]},"reference":[{"key":"2023012810452780300_btt286-B12","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/j.jmr.2012.05.005","article-title":"Exceeding the limit of dynamics studies on biomolecules using high spin-lock field strengths with a cryogenically cooled probehead","volume":"221","author":"Ban","year":"2012","journal-title":"J. Magn. Reson."},{"key":"2023012810452780300_btt286-B1","doi-asserted-by":"crossref","first-page":"421","DOI":"10.1186\/1471-2105-12-421","article-title":"Automated NMR relaxation dispersion data analysis using NESSY","volume":"12","author":"Bieri","year":"2011","journal-title":"BMC Bioinformatics"},{"key":"2023012810452780300_btt286-B2","doi-asserted-by":"crossref","first-page":"1121","DOI":"10.1109\/TVCG.2009.174","article-title":"Protovis: a graphical toolkit for visualization","volume":"15","author":"Bostock","year":"2009","journal-title":"IEEE Trans. Vis. Comput. Graph."},{"key":"2023012810452780300_btt286-B3","first-page":"89","article-title":"General 2-site solution for chemical exchange produced dependence of T2 upon Carr\u2013Purcell pulse separation","volume":"6","author":"Carver","year":"1972","journal-title":"J. Magn. Reson."},{"key":"2023012810452780300_btt286-B4","doi-asserted-by":"crossref","first-page":"266","DOI":"10.1006\/jmrb.1994.1084","article-title":"Direct measurements of the dissociation-rate constant for inhibitor-enzyme complexes via the T1 rho and T2 (CPMG) methods","volume":"104","author":"Davis","year":"1994","journal-title":"J. Magn. Reson. B"},{"key":"2023012810452780300_btt286-B5","doi-asserted-by":"crossref","first-page":"11","DOI":"10.1007\/s10858-011-9589-y","article-title":"GUARDD: user-friendly MATLAB software for rigorous analysis of CPMG RD NMR data","volume":"52","author":"Kleckner","year":"2012","journal-title":"J. Biomol. NMR"},{"key":"2023012810452780300_btt286-B6","doi-asserted-by":"crossref","first-page":"366","DOI":"10.1063\/1.1734254","article-title":"Nuclear magnetic resonance study of the protolysis of trimethylammonium ion in aqueous solution\u2014order of the reaction with respect to solvent","volume":"39","author":"Luz","year":"1963","journal-title":"J. Chem. Phys."},{"key":"2023012810452780300_btt286-B7","doi-asserted-by":"crossref","first-page":"430","DOI":"10.1063\/1.1744152","article-title":"Reaction rates by nuclear magnetic resonance","volume":"28","author":"McConnell","year":"1958","journal-title":"J. Chem. Phys."},{"key":"2023012810452780300_btt286-B8","doi-asserted-by":"crossref","first-page":"2867","DOI":"10.1021\/ja993511y","article-title":"The static magnetic field dependence of chemical exchange linebroadening defines the NMR chemical shift time scale","volume":"122","author":"Millet","year":"2000","journal-title":"J. Am. Chem. 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