{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,5]],"date-time":"2026-10-05T13:11:49Z","timestamp":1791205909243,"version":"4.1.0"},"reference-count":50,"publisher":"Oxford University Press (OUP)","issue":"1","license":[{"start":{"date-parts":[[2000,1,1]],"date-time":"2000-01-01T00:00:00Z","timestamp":946684800000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/academic.oup.com\/pages\/standard-publication-reuse-rights"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[2000,1,1]]},"abstract":"<jats:title>Abstract<\/jats:title>\n                  <jats:p>HLA-F is currently the most enigmatic of the human MHC-encoded class Ib genes. We have investigated the expression of HLA-F using a specific Ab raised against a synthetic peptide corresponding to amino acids 61\u201384 in the \u03b11 domain of the predicted HLA-F protein. HLA-F is expressed as a \u03b22-microglobulin-associated, 42-kDa protein that shows a restricted tissue distribution. To date, we have detected this product only in peripheral blood B cells, B cell lines, and tissues containing B cells, in particular adult tonsil and fetal liver, a major site of B cell development. Thermostability assays suggest that HLA-F is expressed as an empty heterodimer devoid of peptide. Consistent with this, studies using endoglycosidase-H and cell surface immunoprecipitations also indicate that the overwhelming majority of HLA-F contains an immature oligosaccharide component and is expressed inside the cell. We have found that IFN-\u03b3 treatment induces expression of HLA-F mRNA and HLA-F protein, but that this does not result in concomitant cell surface expression. HLA-F associates with at least two components of the conventional class I assembly pathway, calreticulin and TAP. The unusual characteristics of the predicted peptide-binding groove together with the predominantly intracellular localization raise the possibility that HLA-F may be capable of binding only a restricted set of peptides.<\/jats:p>","DOI":"10.4049\/jimmunol.164.1.319","type":"journal-article","created":{"date-parts":[[2014,4,21]],"date-time":"2014-04-21T18:07:57Z","timestamp":1398103677000},"page":"319-328","source":"Crossref","is-referenced-by-count":93,"title":["HLA-F Is a Predominantly Empty, Intracellular, TAP-Associated MHC Class Ib Protein with a Restricted Expression Pattern"],"prefix":"10.1093","volume":"164","author":[{"given":"Shane D","family":"Wainwright","sequence":"first","affiliation":[{"name":"Department of Clinical Medicine, Division of Obstetrics and Gynaecology, University of Bristol, St. Michael\u2019s Hospital , Bristol ,","place":["United Kingdom"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"P Andrew","family":"Biro","sequence":"additional","affiliation":[{"name":"Department of Immunology, St. Bartholomew\u2019s and Royal London School of Medicine and Dentistry, Queen Mary Westfield College , London ,","place":["United Kingdom"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Christopher H","family":"Holmes","sequence":"additional","affiliation":[{"name":"Department of Clinical Medicine, Division of Obstetrics and Gynaecology, University of Bristol, St. Michael\u2019s Hospital , Bristol ,","place":["United Kingdom"]}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"286","published-online":{"date-parts":[[2000,1,1]]},"reference":[{"key":"2026020213141970000_R1","first-page":"469","volume-title":"J. 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