{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,4]],"date-time":"2026-09-04T22:03:35Z","timestamp":1788559415613,"version":"build-2803163510"},"reference-count":36,"publisher":"Wiley","issue":"13","license":[{"start":{"date-parts":[[2001,11,1]],"date-time":"2001-11-01T00:00:00Z","timestamp":1004572800000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"},{"start":{"date-parts":[[2001,11,1]],"date-time":"2001-11-01T00:00:00Z","timestamp":1004572800000},"content-version":"tdm","delay-in-days":0,"URL":"http:\/\/doi.wiley.com\/10.1002\/tdm_license_1.1"}],"funder":[{"DOI":"10.13039\/100000002","name":"National Institutes of Health","doi-asserted-by":"publisher","award":["NS-23327"],"award-info":[{"award-number":["NS-23327"]}],"id":[{"id":"10.13039\/100000002","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000002","name":"National Institutes of Health","doi-asserted-by":"publisher","award":["HL-50675"],"award-info":[{"award-number":["HL-50675"]}],"id":[{"id":"10.13039\/100000002","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["faseb.onlinelibrary.wiley.com"],"crossmark-restriction":true},"short-container-title":["The FASEB Journal"],"published-print":{"date-parts":[[2001,11]]},"abstract":"<jats:title>ABSTRACT<\/jats:title>\n                  <jats:p>\n                    Salicylic acid (SA), an endogenous signaling molecule of plants, possesses anti\u2010inflammatory and anti\u2010neoplastic actions in human. Its derivative, aspirin, is the most commonly used anti\u2010inflammatory and analgesic drug. Aspirin and sodium salicylate (sa\u2010licylates) have been reported to have multiple pharmacological actions. However, it is unclear whether they bind to a cellular protein. Here, we report for the first time the purification from human fibroblasts of a ~78 kDa salicylate binding protein with sequence identity to immunoglobulin heavy chain binding protein (BiP). The\n                    <jats:italic>\n                      K\n                      <jats:sub>d<\/jats:sub>\n                    <\/jats:italic>\n                    values of SA binding to crude extract and to recombinant BiP were 45.2 and 54.6 \u03bcM, respectively. BiP is a chaperone protein containing a polypeptide binding site recognizing specific heptapeptide sequence and an ATP binding site. A heptapeptide with the specific sequence displaced SA binding in a concentration\u2010dependent manner whereas a control heptapep\u2010tide did not. Salicylates inhibited ATPase activity stimulated by this specific heptapeptide but did not block ATP binding or induce BiP expression. These results indicate that salicylates bind specifically to the polypep\u2010tide binding site of BiP in human cells that may interfere with folding and transport of proteins important in inflammation.\u2014Deng, W.\u2010G., Ruan, K.\u2010H., Du, M., Saunders, M. A., Wu, K. K. Aspirin and salicylate bind to immunoglobulin heavy chain binding protein (BiP) and inhibit its ATPase activity in human fibroblasts.\n                    <jats:italic>FASEB J<\/jats:italic>\n                    . 15, 2463\u20132470 (2001)\n                  <\/jats:p>","DOI":"10.1096\/fj.01-0259com","type":"journal-article","created":{"date-parts":[[2002,7,26]],"date-time":"2002-07-26T19:03:24Z","timestamp":1027710204000},"page":"2463-2470","update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":33,"title":["Aspirin and salicylate bind to immunoglobulin heavy chain binding protein (BiP) and inhibit its ATPase activity in human fibroblasts"],"prefix":"10.1096","volume":"15","author":[{"given":"WU-GUO","family":"DENG","sequence":"first","affiliation":[{"name":"Vascular Biology Research Center Division of Hematology Department of Internal Medicine University of Texas-Houston Medical School Houston Texas 77030 USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"KE-HE","family":"RUAN","sequence":"additional","affiliation":[{"name":"Vascular Biology Research Center Division of Hematology Department of Internal Medicine University of Texas-Houston Medical School Houston Texas 77030 USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"MIN","family":"DU","sequence":"additional","affiliation":[{"name":"Vascular Biology Research Center Division of Hematology Department of Internal Medicine University of Texas-Houston Medical School Houston Texas 77030 USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"MICHAEL A.","family":"SAUNDERS","sequence":"additional","affiliation":[{"name":"Vascular Biology Research Center Division of Hematology Department of Internal Medicine University of Texas-Houston Medical School Houston Texas 77030 USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"KENNETH K.","family":"WU","sequence":"additional","affiliation":[{"name":"Vascular Biology Research Center Division of Hematology Department of Internal Medicine University of Texas-Houston Medical School Houston Texas 77030 USA"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"311","published-online":{"date-parts":[[2001,11,1]]},"reference":[{"key":"e_1_2_5_2_1","doi-asserted-by":"publisher","DOI":"10.1126\/science.250.4983.1004"},{"key":"e_1_2_5_3_1","doi-asserted-by":"publisher","DOI":"10.1126\/science.250.4983.1002"},{"key":"e_1_2_5_4_1","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.84.5.1417"},{"key":"e_1_2_5_5_1","first-page":"122","article-title":"Aspirin use and risk of fatal cancer","volume":"53","author":"Thun M. 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