{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,4,7]],"date-time":"2026-04-07T09:16:54Z","timestamp":1775553414341,"version":"3.50.1"},"reference-count":11,"publisher":"Oxford University Press (OUP)","issue":"22","license":[{"start":{"date-parts":[[2017,8,3]],"date-time":"2017-08-03T00:00:00Z","timestamp":1501718400000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/academic.oup.com\/journals\/pages\/about_us\/legal\/notices"}],"funder":[{"DOI":"10.13039\/100000002","name":"National Institutes of Health","doi-asserted-by":"publisher","award":["R01GM093937"],"award-info":[{"award-number":["R01GM093937"]}],"id":[{"id":"10.13039\/100000002","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[2017,11,15]]},"abstract":"<jats:title>Abstract<\/jats:title>\n               <jats:sec>\n                  <jats:title>Summary<\/jats:title>\n                  <jats:p>Electrostatic force is an essential component of the total force acting between atoms and macromolecules. Therefore, accurate calculations of electrostatic forces are crucial for revealing the mechanisms of many biological processes. We developed a DelPhiForce web server to calculate and visualize the electrostatic forces at molecular level. DelPhiForce web server enables modeling of electrostatic forces on individual atoms, residues, domains and molecules, and generates an output that can be visualized by VMD software. Here we demonstrate the usage of the server for various biological problems including protein\u2013cofactor, domain\u2013domain, protein\u2013protein, protein\u2013DNA and protein\u2013RNA interactions.<\/jats:p>\n               <\/jats:sec>\n               <jats:sec>\n                  <jats:title>Availability and implementation<\/jats:title>\n                  <jats:p>The DelPhiForce web server is available at: http:\/\/compbio.clemson.edu\/delphi-force.<\/jats:p>\n               <\/jats:sec>\n               <jats:sec>\n                  <jats:title>Supplementary information<\/jats:title>\n                  <jats:p>Supplementary data are available at Bioinformatics online.<\/jats:p>\n               <\/jats:sec>","DOI":"10.1093\/bioinformatics\/btx495","type":"journal-article","created":{"date-parts":[[2017,8,1]],"date-time":"2017-08-01T19:16:32Z","timestamp":1501614992000},"page":"3661-3663","source":"Crossref","is-referenced-by-count":48,"title":["DelPhiForce web server: electrostatic forces and energy calculations and visualization"],"prefix":"10.1093","volume":"33","author":[{"given":"Lin","family":"Li","sequence":"first","affiliation":[{"name":"Department of Physics, Clemson University, Clemson, SC, USA"}]},{"given":"Zhe","family":"Jia","sequence":"additional","affiliation":[{"name":"Department of Physics, Clemson University, Clemson, SC, USA"}]},{"given":"Yunhui","family":"Peng","sequence":"additional","affiliation":[{"name":"Department of Physics, Clemson University, Clemson, SC, USA"}]},{"given":"Arghya","family":"Chakravorty","sequence":"additional","affiliation":[{"name":"Department of Physics, Clemson University, Clemson, SC, USA"}]},{"given":"Lexuan","family":"Sun","sequence":"additional","affiliation":[{"name":"Department of Physics, Clemson University, Clemson, SC, USA"}]},{"given":"Emil","family":"Alexov","sequence":"additional","affiliation":[{"name":"Department of Physics, Clemson University, Clemson, SC, USA"}]}],"member":"286","published-online":{"date-parts":[[2017,8,3]]},"reference":[{"key":"2023051308380764400_btx495-B1","doi-asserted-by":"crossref","first-page":"8368","DOI":"10.1093\/nar\/gkt584","article-title":"Structure of p53 binding to the BAX response element reveals DNA unwinding and compression to accommodate base-pair insertion","volume":"41","author":"Chen","year":"2013","journal-title":"Nucleic Acids Res"},{"key":"2023051308380764400_btx495-B2","doi-asserted-by":"crossref","first-page":"10795","DOI":"10.1093\/nar\/gku743","article-title":"Structure analysis of free and bound states of an RNA aptamer against ribosomal protein S8 from Bacillus anthracis","volume":"42","author":"Davlieva","year":"2014","journal-title":"Nucleic Acids Res"},{"key":"2023051308380764400_btx495-B3","doi-asserted-by":"crossref","first-page":"e20930","DOI":"10.7554\/eLife.20930","article-title":"\u03b3-Protocadherin structural diversity and functional implications","volume":"5","author":"Goodman","year":"2016","journal-title":"Elife"},{"key":"2023051308380764400_btx495-B4","doi-asserted-by":"crossref","first-page":"225","DOI":"10.1007\/s00249-006-0123-1","article-title":"Electrostatic control of the overall shape of calmodulin: numerical calculations","volume":"36","author":"Isvoran","year":"2007","journal-title":"Eur. 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