{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,3,29]],"date-time":"2026-03-29T12:07:43Z","timestamp":1774786063238,"version":"3.50.1"},"reference-count":90,"publisher":"Elsevier BV","issue":"2","license":[{"start":{"date-parts":[[1997,5,1]],"date-time":"1997-05-01T00:00:00Z","timestamp":862444800000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Human Immunology"],"published-print":{"date-parts":[[1997,5]]},"DOI":"10.1016\/s0198-8859(97)00081-5","type":"journal-article","created":{"date-parts":[[2002,7,25]],"date-time":"2002-07-25T18:19:25Z","timestamp":1027621165000},"page":"129-136","source":"Crossref","is-referenced-by-count":54,"title":["Delivery of Antigens to the MHC Class I Pathway Using Bacterial Toxins"],"prefix":"10.1016","volume":"54","author":[{"given":"T.J","family":"Goletz","sequence":"first","affiliation":[]},{"given":"K.R","family":"Klimpel","sequence":"additional","affiliation":[]},{"given":"S.H","family":"Leppla","sequence":"additional","affiliation":[]},{"given":"J.M","family":"Keith","sequence":"additional","affiliation":[]},{"given":"J.A","family":"Berzofsky","sequence":"additional","affiliation":[]}],"member":"78","reference":[{"key":"10.1016\/S0198-8859(97)00081-5_BIB1","doi-asserted-by":"crossref","first-page":"81","DOI":"10.1016\/S0092-8674(85)80103-3","article-title":"The T cell receptor","volume":"42","author":"Yague","year":"1985","journal-title":"Cell"},{"key":"10.1016\/S0198-8859(97)00081-5_BIB2","doi-asserted-by":"crossref","first-page":"232","DOI":"10.1038\/320232a0","article-title":"Transfer of specificity by murine alpha and beta T-cell receptor genes","volume":"320","author":"Dembic","year":"1986","journal-title":"Nature"},{"key":"10.1016\/S0198-8859(97)00081-5_BIB3","doi-asserted-by":"crossref","first-page":"125","DOI":"10.1038\/325125a0","article-title":"Specific antigen-Ia activation of transfected human T cells expressing murine Ti d\/b\u2013human T3 receptor complexes","volume":"325","author":"Saito","year":"1987","journal-title":"Nature"},{"key":"10.1016\/S0198-8859(97)00081-5_BIB4","doi-asserted-by":"crossref","first-page":"359","DOI":"10.1038\/317359a0","article-title":"The binding of immunogenic peptides to Ia histocompatibility molecules","volume":"317","author":"Babbitt","year":"1985","journal-title":"Nature"},{"key":"10.1016\/S0198-8859(97)00081-5_BIB5","doi-asserted-by":"crossref","first-page":"1071","DOI":"10.1016\/0092-8674(86)90822-6","article-title":"Isolation and characterization of antigen\u2013Ia complexes involved in T cell recognition","volume":"47","author":"Buus","year":"1986","journal-title":"Cell"},{"key":"10.1016\/S0198-8859(97)00081-5_BIB6","doi-asserted-by":"crossref","first-page":"457","DOI":"10.1016\/0092-8674(85)90103-5","article-title":"Cytotoxic T cells recognize fragments of the influenza nucleoprotein","volume":"42","author":"Townsend","year":"1985","journal-title":"Cell"},{"key":"10.1016\/S0198-8859(97)00081-5_BIB7","doi-asserted-by":"crossref","first-page":"777","DOI":"10.1016\/S0092-8674(88)91043-4","article-title":"Introduction of soluble protein into the class I pathway of antigen processing and presentation","volume":"54","author":"Moore","year":"1988","journal-title":"Cell"},{"key":"10.1016\/S0198-8859(97)00081-5_BIB8","doi-asserted-by":"crossref","first-page":"637","DOI":"10.1126\/science.3257585","article-title":"Cells process exogenous proteins for recognition by cytotoxic T lymphocytes","volume":"239","author":"Yewdell","year":"1988","journal-title":"Science"},{"key":"10.1016\/S0198-8859(97)00081-5_BIB9","doi-asserted-by":"crossref","first-page":"1869","DOI":"10.4049\/jimmunol.127.5.1869","article-title":"Identification of a macrophage antigen-processing event required for I-region-restricted antigen presentation to T lymphocytes","volume":"127","author":"Ziegler","year":"1981","journal-title":"J Immunol"},{"key":"10.1016\/S0198-8859(97)00081-5_BIB10","doi-asserted-by":"crossref","first-page":"903","DOI":"10.1084\/jem.163.4.903","article-title":"Differences in antigen presentation to MHC class I and class II-restricted influenza virus specific cytolytic T lymphocyte clones","volume":"163","author":"Morrison","year":"1986","journal-title":"J Exp Med"},{"key":"10.1016\/S0198-8859(97)00081-5_BIB11","doi-asserted-by":"crossref","first-page":"253","DOI":"10.1146\/annurev.bi.59.070190.001345","article-title":"Structure, function, and diversity of class I major histocompatibility complex molecules","volume":"59","author":"Bjorkman","year":"1990","journal-title":"Annu Rev Biochem"},{"key":"10.1016\/S0198-8859(97)00081-5_BIB12","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/0092-8674(84)90068-0","article-title":"The class II molecules of the human and murine major histocompatibility complex","volume":"36","author":"Kaufman","year":"1984","journal-title":"Cell"},{"key":"10.1016\/S0198-8859(97)00081-5_BIB13","doi-asserted-by":"crossref","first-page":"506","DOI":"10.1038\/329506a0","article-title":"Structure of the human class I histocompatibility antigen HLA-A2","volume":"329","author":"Bjorkman","year":"1987","journal-title":"Nature"},{"key":"10.1016\/S0198-8859(97)00081-5_BIB14","doi-asserted-by":"crossref","first-page":"213","DOI":"10.1038\/348213a0","article-title":"Isolation of an endogenously processed immunodominant viral peptide from the class I H-2Kb molecule","volume":"348","author":"Van Bleek","year":"1990","journal-title":"Nature"},{"key":"10.1016\/S0198-8859(97)00081-5_BIB15","doi-asserted-by":"crossref","first-page":"641","DOI":"10.1038\/355641a0","article-title":"Assembly and function of the two ABC transporter proteins encoded in the human major histocompatibility complex","volume":"355","author":"Kelly","year":"1992","journal-title":"Nature"},{"key":"10.1016\/S0198-8859(97)00081-5_BIB16","doi-asserted-by":"crossref","first-page":"647","DOI":"10.1038\/355647a0","article-title":"Ham-2 corrects the class I antigen-processing defect in RMA-S cells","volume":"355","author":"Attaya","year":"1992","journal-title":"Nature"},{"key":"10.1016\/S0198-8859(97)00081-5_BIB17","doi-asserted-by":"crossref","first-page":"323","DOI":"10.1038\/351323a0","article-title":"Restored expression of major histocompatibility class I molecules by gene transfer of a putative peptide transporter","volume":"351","author":"Spies","year":"1991","journal-title":"Nature"},{"key":"10.1016\/S0198-8859(97)00081-5_BIB18","doi-asserted-by":"crossref","first-page":"355","DOI":"10.1038\/353355a0","article-title":"Structural and serological similarity of MHC-linked LMP and proteasome (multicatalytic proteinase) complexes","volume":"353","author":"Brown","year":"1991","journal-title":"Nature"},{"key":"10.1016\/S0198-8859(97)00081-5_BIB19","doi-asserted-by":"crossref","first-page":"664","DOI":"10.1038\/353664a0","article-title":"Homology of proteasome subunits to a major histocompatibility complex-linked LMP gene","volume":"353","author":"Martinez","year":"1991","journal-title":"Nature"},{"key":"10.1016\/S0198-8859(97)00081-5_BIB20","doi-asserted-by":"crossref","first-page":"667","DOI":"10.1038\/353667a0","article-title":"Second proteasome-related gene in the human MHC class II region","volume":"353","author":"Kelly","year":"1991","journal-title":"Nature"},{"key":"10.1016\/S0198-8859(97)00081-5_BIB21","doi-asserted-by":"crossref","first-page":"357","DOI":"10.1038\/353357a0","article-title":"A proteasome-related gene between the two ABC transporter loci in the class II region of the human MHC","volume":"353","author":"Glynne","year":"1991","journal-title":"Nature"},{"key":"10.1016\/S0198-8859(97)00081-5_BIB22","doi-asserted-by":"crossref","first-page":"21","DOI":"10.1007\/BF00990966","article-title":"Molecular biology of proteasomes","volume":"21","author":"Tanaka","year":"1995","journal-title":"Mol Biol Rep"},{"key":"10.1016\/S0198-8859(97)00081-5_BIB23","doi-asserted-by":"crossref","first-page":"13","DOI":"10.1016\/0092-8674(94)90396-4","article-title":"The ubiquitin\u2013proteasome proteolytic pathway","volume":"79","author":"Ciechanover","year":"1994","journal-title":"Cell"},{"key":"10.1016\/S0198-8859(97)00081-5_BIB24","doi-asserted-by":"crossref","first-page":"552","DOI":"10.1038\/363552a0","article-title":"A role for the ubiquitin-dependent proteolytic pathway in MHC class I-restricted antigen presentation","volume":"363","author":"Michalek","year":"1993","journal-title":"Nature"},{"key":"10.1016\/S0198-8859(97)00081-5_BIB25","doi-asserted-by":"crossref","first-page":"1234","DOI":"10.1126\/science.8066463","article-title":"MHC class I expression in mice lacking the proteasome subunit LMP-7","volume":"265","author":"Fehling","year":"1994","journal-title":"Science"},{"key":"10.1016\/S0198-8859(97)00081-5_BIB26","doi-asserted-by":"crossref","first-page":"264","DOI":"10.1038\/365264a0","article-title":"\u03b3-Interferon and expression of MHC genes regulate peptide hydrolysis by proteasomes","volume":"365","author":"Gaczynska","year":"1993","journal-title":"Nature"},{"key":"10.1016\/S0198-8859(97)00081-5_BIB27","doi-asserted-by":"crossref","first-page":"901","DOI":"10.1084\/jem.179.3.901","article-title":"Interferon gamma stimulation modulates the proteolytic activity and cleavage site preference of 20S mouse proteasomes","volume":"179","author":"Boes","year":"1994","journal-title":"J Exp Med"},{"key":"10.1016\/S0198-8859(97)00081-5_BIB28","doi-asserted-by":"crossref","first-page":"1756","DOI":"10.1128\/JVI.63.4.1756-1762.1989","article-title":"HLA class II-restricted presentation of cytoplasmic measles virus antigens to cytotoxic T cells","volume":"63","author":"Jacobson","year":"1989","journal-title":"J Virol"},{"key":"10.1016\/S0198-8859(97)00081-5_BIB29","doi-asserted-by":"crossref","first-page":"1411","DOI":"10.1002\/eji.1830210613","article-title":"Class II-restricted IgG2ab-specific T cells recognize a signal-minus form of the V-CH3b antigen","volume":"21","author":"Bikoff","year":"1991","journal-title":"Eur J Immunol"},{"key":"10.1016\/S0198-8859(97)00081-5_BIB30","doi-asserted-by":"crossref","first-page":"702","DOI":"10.1038\/357702a0","article-title":"Processing pathways for presentation of cytosolic antigen to MHC class II-restricted T cells","volume":"357","author":"Malnati","year":"1992","journal-title":"Nature"},{"key":"10.1016\/S0198-8859(97)00081-5_BIB31","doi-asserted-by":"crossref","first-page":"158","DOI":"10.1007\/BF01923509","article-title":"Autophagy and other vacuolar protein degradation mechanisms","volume":"48","author":"Seglen","year":"1992","journal-title":"Experientia"},{"key":"10.1016\/S0198-8859(97)00081-5_BIB32","doi-asserted-by":"crossref","first-page":"377","DOI":"10.1084\/jem.171.2.377","article-title":"Class I-restricted processing and presentation of exogenous cell-associated antigen in vivo","volume":"171","author":"Carbone","year":"1990","journal-title":"J Exp Med"},{"key":"10.1016\/S0198-8859(97)00081-5_BIB33","doi-asserted-by":"crossref","first-page":"1655","DOI":"10.4049\/jimmunol.126.5.1655","article-title":"The involvement of herpes simplex virus type 1 glycoproteins in cell-mediated immunity","volume":"126","author":"Carter","year":"1981","journal-title":"J Immunol"},{"key":"10.1016\/S0198-8859(97)00081-5_BIB34","doi-asserted-by":"crossref","first-page":"168","DOI":"10.1016\/0167-5699(88)91292-3","article-title":"CD8+ T lymphocytes in intracellular microbial infections","volume":"9","author":"Kaufmann","year":"1988","journal-title":"Immunol Today"},{"key":"10.1016\/S0198-8859(97)00081-5_BIB35","doi-asserted-by":"crossref","first-page":"243","DOI":"10.1126\/science.7809629","article-title":"A phagosome-to-cytosol pathway for exogenous antigens presented on MHC class I molecules","volume":"267","author":"Kovacsovics-Bankowski","year":"1995","journal-title":"Science"},{"key":"10.1016\/S0198-8859(97)00081-5_BIB36","doi-asserted-by":"crossref","first-page":"2795","DOI":"10.4049\/jimmunol.146.8.2795","article-title":"Class I MHC-restricted cytotoxic T lymphocyte recognition of cells infected with human cytomegalovirus does not require endogenous viral gene expression","volume":"146","author":"Riddell","year":"1991","journal-title":"J Immunol"},{"key":"10.1016\/S0198-8859(97)00081-5_BIB37","doi-asserted-by":"crossref","first-page":"873","DOI":"10.1038\/344873a0","article-title":"Induction of CD8+ cytotoxic T cells by immunization with purified HIV-1 envelope protein in ISCOMs","volume":"344","author":"Takahashi","year":"1990","journal-title":"Nature"},{"key":"10.1016\/S0198-8859(97)00081-5_BIB38","doi-asserted-by":"crossref","first-page":"2357","DOI":"10.4049\/jimmunol.148.8.2357","article-title":"Saponin adjuvant induction of ovalbumin-specific CD8+ cytotoxic T lymphocyte responses","volume":"148","author":"Newman","year":"1992","journal-title":"J Immunol"},{"key":"10.1016\/S0198-8859(97)00081-5_BIB39","doi-asserted-by":"crossref","first-page":"1603","DOI":"10.1002\/eji.1830220638","article-title":"Preferred size of peptides that bind to H-2Kb is sequence dependent","volume":"22","author":"Deres","year":"1992","journal-title":"Eur J Immunol"},{"key":"10.1016\/S0198-8859(97)00081-5_BIB40","doi-asserted-by":"crossref","first-page":"3336","DOI":"10.4049\/jimmunol.148.11.3336","article-title":"Processing of exogenous liposome-encapsulated antigens in vivo generates class I MHC-restricted T cell responses","volume":"148","author":"Collins","year":"1992","journal-title":"J Immunol"},{"key":"10.1016\/S0198-8859(97)00081-5_BIB41","doi-asserted-by":"crossref","first-page":"7504","DOI":"10.1016\/S0021-9258(18)34407-7","article-title":"Entry of the toxic proteins abrin, modecin, ricin, and diphtheria toxin into cells. II. Effect of pH, metabolic inhibitors, and ionophores and evidence for toxin penetration from endocytotic vesicles","volume":"257","author":"Sandvig","year":"1982","journal-title":"J Biol Chem"},{"key":"10.1016\/S0198-8859(97)00081-5_BIB42","doi-asserted-by":"crossref","first-page":"145","DOI":"10.1128\/IAI.44.1.145-150.1984","article-title":"Evidence for penetration of diphtheria toxin to the cytosol through a prelysosomal membrane","volume":"44","author":"Marnell","year":"1984","journal-title":"Infect Immun"},{"key":"10.1016\/S0198-8859(97)00081-5_BIB43","doi-asserted-by":"crossref","first-page":"203","DOI":"10.1016\/0092-8674(90)90356-J","article-title":"The binary logic of antigen processing and presentation to T cells","volume":"62","author":"Yewdell","year":"1990","journal-title":"Cell"},{"key":"10.1016\/S0198-8859(97)00081-5_BIB44","doi-asserted-by":"crossref","first-page":"1017","DOI":"10.1016\/0092-8674(91)90325-S","article-title":"Barnase toxin","volume":"64","author":"Prior","journal-title":"Cell"},{"key":"10.1016\/S0198-8859(97)00081-5_BIB45","doi-asserted-by":"crossref","first-page":"1025","DOI":"10.1083\/jcb.113.5.1025","article-title":"Peptides fused to the amino-terminal end of diphtheria toxin are translocated to the cytosol","volume":"113","author":"Stenmark","year":"1991","journal-title":"J Cell Biol"},{"key":"10.1016\/S0198-8859(97)00081-5_BIB46","doi-asserted-by":"crossref","first-page":"1504","DOI":"10.1016\/S0021-9258(19)77001-X","article-title":"Structure and activity of diphtheria toxin II. Attack by trypsin at a specific site within the intact toxin molecule","volume":"246","author":"Drazin","year":"1971","journal-title":"J Biol Chem"},{"key":"10.1016\/S0198-8859(97)00081-5_BIB47","doi-asserted-by":"crossref","first-page":"13449","DOI":"10.1016\/S0021-9258(18)37726-3","article-title":"Requirement of specific receptors for efficient translocation of diphtheria toxin A fragment across the plasma membrane","volume":"263","author":"Stenmark","year":"1988","journal-title":"J Biol Chem"},{"key":"10.1016\/S0198-8859(97)00081-5_BIB48","doi-asserted-by":"crossref","first-page":"6202","DOI":"10.1073\/pnas.89.13.6202","article-title":"pH-dependent insertion of proteins into membranes","volume":"89","author":"O\u2019Keefe","year":"1992","journal-title":"Proc Natl Acad Sci USA"},{"key":"10.1016\/S0198-8859(97)00081-5_BIB49","doi-asserted-by":"crossref","first-page":"9068","DOI":"10.1016\/S0021-9258(19)52509-1","article-title":"Rapid entry of nicked diphtheria toxin into cells at low pH. Characterization of the entry process and effects of low pH on the toxin molecule","volume":"256","author":"Sandvig","year":"1981","journal-title":"J Biol Chem"},{"key":"10.1016\/S0198-8859(97)00081-5_BIB50","doi-asserted-by":"crossref","first-page":"5458","DOI":"10.1021\/bi00341a027","article-title":"Effect of pH on the conformation of diphtheria toxin and its implications for membrane penetration","volume":"24","author":"Blewitt","year":"1985","journal-title":"Biochemistry"},{"key":"10.1016\/S0198-8859(97)00081-5_BIB51","doi-asserted-by":"crossref","first-page":"4928","DOI":"10.1016\/S0021-9258(18)83680-8","article-title":"Secondary structure of diphtheria toxin and its fragments interacting with acidic liposomes studied by polarized infrared spectroscopy","volume":"264","author":"Cabiaux","year":"1989","journal-title":"J Biol Chem"},{"key":"10.1016\/S0198-8859(97)00081-5_BIB52","doi-asserted-by":"crossref","first-page":"17446","DOI":"10.1016\/S0021-9258(19)47393-6","article-title":"Entry of diphtheria toxin\u2013protein A chimeras into cells","volume":"266","author":"Madshus","year":"1991","journal-title":"J Biol Chem"},{"key":"10.1016\/S0198-8859(97)00081-5_BIB53","doi-asserted-by":"crossref","first-page":"3296","DOI":"10.1128\/IAI.60.8.3296-3302.1992","article-title":"Membrane translocation of diphtheria toxin carrying passenger protein domains","volume":"60","author":"Madshus","year":"1992","journal-title":"Infect Immun"},{"key":"10.1016\/S0198-8859(97)00081-5_BIB54","doi-asserted-by":"crossref","first-page":"1647","DOI":"10.1128\/IAI.55.7.1647-1651.1987","article-title":"Expression of a mutant, full-length form of diphtheria toxin in Escherichia coli","volume":"55","author":"Barbieri","year":"1987","journal-title":"Infect Immun"},{"key":"10.1016\/S0198-8859(97)00081-5_BIB55","doi-asserted-by":"crossref","first-page":"2244","DOI":"10.1016\/S0021-9258(18)45869-3","article-title":"Insertional mutagenesis of Bordetella pertussis adenylate cyclase","volume":"267","author":"Ladant","year":"1992","journal-title":"J Biol Chem"},{"key":"10.1016\/S0198-8859(97)00081-5_BIB56","unstructured":"Carbonetti N, Tishon A, Oldstone M, Rappuoli R: Use of pertussis toxin vaccine molecule PT19K\/129G to deliver peptide epitopes for stimulation of a cytotoxic T lymphocyte response. Abstr Annu Meet Am Soc Microbiol 95:295, 1995 [Abstract]."},{"key":"10.1016\/S0198-8859(97)00081-5_BIB57","doi-asserted-by":"crossref","first-page":"3851","DOI":"10.1128\/IAI.63.10.3851-3857.1995","article-title":"Cell-invasive activity of epitope-tagged adenylate cyclase of Bordetella pertussis allows in vitro presentation of a foreign epitope to CD8+ cytotoxic T cells","volume":"63","author":"Sebo","year":"1995","journal-title":"Infect Immun"},{"key":"10.1016\/S0198-8859(97)00081-5_BIB58","doi-asserted-by":"crossref","first-page":"4697","DOI":"10.4049\/jimmunol.156.12.4697","article-title":"In vivo induction of CTL responses by recombinant adenylate cyclase of Bordetella pertussis carrying viral CD8+ T cell epitopes","volume":"156","author":"Fayolle","year":"1996","journal-title":"J Immunol"},{"key":"10.1016\/S0198-8859(97)00081-5_BIB59","unstructured":"Carbonetti N, Chen C, Irish T, O\u2019Connell C: Development of pertussis and cholera toxins as cytotoxic T lymphocyte vaccine vector molecules. Abstr Annu Meet Am Soc Microbiol 96:277, 1996 [Abstract]."},{"key":"10.1016\/S0198-8859(97)00081-5_BIB60","doi-asserted-by":"crossref","first-page":"20678","DOI":"10.1016\/S0021-9258(17)30557-4","article-title":"Processing of Pseudomonas exotoxin by a cellular protease results in the generation of a 37,000-Da toxin fragment that is translocated to the cytosol","volume":"265","author":"Ogata","year":"1990","journal-title":"J Biol Chem"},{"key":"10.1016\/S0198-8859(97)00081-5_BIB61","doi-asserted-by":"crossref","first-page":"3530","DOI":"10.1073\/pnas.90.8.3530","article-title":"Targeted delivery of peptide epitopes to class I major histocompatibility molecules by a modified Pseudomonas exotoxin","volume":"90","author":"Donnelly","year":"1993","journal-title":"Proc Natl Acad Sci USA"},{"key":"10.1016\/S0198-8859(97)00081-5_BIB62","doi-asserted-by":"crossref","first-page":"881","DOI":"10.1038\/326881a0","article-title":"Cytotoxic T lymphocytes recognize a fragment of influenza virus matrix protein in association with HLA-A2","volume":"326","author":"Gotch","year":"1987","journal-title":"Nature"},{"key":"10.1016\/S0198-8859(97)00081-5_BIB63","doi-asserted-by":"crossref","first-page":"15953","DOI":"10.1016\/S0021-9258(18)71572-X","article-title":"Domain II mutants of Pseudomonas exotoxin deficient in translocation","volume":"264","author":"Jinno","year":"1989","journal-title":"J Biol Chem"},{"key":"10.1016\/S0198-8859(97)00081-5_BIB64","doi-asserted-by":"crossref","first-page":"1590","DOI":"10.1002\/eji.1830240721","article-title":"Presentation of an exogenous antigen by major histocompatibility complex class I molecules","volume":"24","author":"Ulmer","year":"1994","journal-title":"Eur J Immunol"},{"key":"10.1016\/S0198-8859(97)00081-5_BIB65","doi-asserted-by":"crossref","first-page":"17376","DOI":"10.1016\/S0021-9258(19)47383-3","article-title":"Increased cytotoxic activity of Pseudomonas exotoxin and two chimeric toxins ending in KDEL","volume":"266","author":"Seetharam","year":"1991","journal-title":"J Biol Chem"},{"key":"10.1016\/S0198-8859(97)00081-5_BIB66","doi-asserted-by":"crossref","first-page":"308","DOI":"10.1073\/pnas.87.1.308","article-title":"Pseudomonas exotoxin contains a specific sequence at the carboxyl terminus that is required for cytotoxicity","volume":"87","author":"Chaudhary","year":"1997","journal-title":"Proc Natl Acad Sci USA"},{"key":"10.1016\/S0198-8859(97)00081-5_BIB67","doi-asserted-by":"crossref","first-page":"162","DOI":"10.1038\/348162a0","article-title":"A human homologue of yeast HDEL receptor","volume":"348","author":"Lewis","year":"1990","journal-title":"Nature"},{"key":"10.1016\/S0198-8859(97)00081-5_BIB68","doi-asserted-by":"crossref","first-page":"193","DOI":"10.1084\/jem.159.1.193","article-title":"Spontaneous internalization of class I major histocompatibility complex molecules in T lymphoid cells","volume":"159","author":"Tse","year":"1984","journal-title":"J Exp Med"},{"key":"10.1016\/S0198-8859(97)00081-5_BIB69","doi-asserted-by":"crossref","first-page":"655","DOI":"10.1038\/346655a0","article-title":"Cycling of cell-surface MHC glycoproteins through primaquine-sensitive intracellular compartments","volume":"346","author":"Reid","year":"1990","journal-title":"Nature"},{"key":"10.1016\/S0198-8859(97)00081-5_BIB70","doi-asserted-by":"crossref","first-page":"2688","DOI":"10.1073\/pnas.86.8.2688","article-title":"Constitutive endocytosis of HLA class I antigens requires a specific portion of the intracytoplasmic tail that shares structural features with other endocytosed molecules","volume":"86","author":"Vega","year":"1989","journal-title":"Proc Natl Acad Sci USA"},{"key":"10.1016\/S0198-8859(97)00081-5_BIB71","doi-asserted-by":"crossref","first-page":"1862","DOI":"10.4049\/jimmunol.146.6.1862","article-title":"Endocytosis and dissociation of class I MHC molecules labeled with fluorescent beta-2 microglobulin","volume":"146","author":"Hochman","year":"1989","journal-title":"J Immunol"},{"key":"10.1016\/S0198-8859(97)00081-5_BIB72","doi-asserted-by":"crossref","first-page":"869","DOI":"10.1038\/173869a0","article-title":"Observations on experimental anthrax","volume":"173","author":"Smith","year":"1954","journal-title":"Nature"},{"key":"10.1016\/S0198-8859(97)00081-5_BIB73","doi-asserted-by":"crossref","first-page":"517","DOI":"10.1099\/00221287-29-3-517","article-title":"Purification of the third factor of anthrax toxin","volume":"29","author":"Smith","year":"1962","journal-title":"J Gen Microbiol"},{"key":"10.1016\/S0198-8859(97)00081-5_BIB74","first-page":"1554","article-title":"Anthrax toxic complex","volume":"26","author":"Smith","year":"1967","journal-title":"Fed Proc"},{"key":"10.1016\/S0198-8859(97)00081-5_BIB75","first-page":"543","article-title":"Anthrax toxins","volume":"Vol 8","author":"Leppla","year":"1995"},{"key":"10.1016\/S0198-8859(97)00081-5_BIB76","doi-asserted-by":"crossref","first-page":"7123","DOI":"10.1016\/S0021-9258(17)38364-3","article-title":"Macrophages are sensitive to anthrax lethal toxin through an acid-dependent process","volume":"261","author":"Friedlander","year":"1986","journal-title":"J Biol Chem"},{"key":"10.1016\/S0198-8859(97)00081-5_BIB77","doi-asserted-by":"crossref","first-page":"3162","DOI":"10.1073\/pnas.79.10.3162","article-title":"Anthrax toxin edema factor","volume":"79","author":"Leppla","year":"1982","journal-title":"Proc Natl Acad Sci USA"},{"key":"10.1016\/S0198-8859(97)00081-5_BIB78","series-title":"Molecular Mechanisms of Bacterial Virulence","first-page":"127","article-title":"Anthrax toxin mechanisms of receptor binding and internalization","author":"Leppla","year":"1994"},{"key":"10.1016\/S0198-8859(97)00081-5_BIB79","doi-asserted-by":"crossref","first-page":"10277","DOI":"10.1073\/pnas.89.21.10277","article-title":"Anthrax toxin protective antigen is activated by a cell-surface protease with the sequence specificity and catalytic properties of furin","volume":"89","author":"Klimpel","year":"1992","journal-title":"Proc Natl Acad Sci USA"},{"key":"10.1016\/S0198-8859(97)00081-5_BIB80","doi-asserted-by":"crossref","first-page":"17186","DOI":"10.1016\/S0021-9258(18)41911-4","article-title":"Functional characterization of protease-treated Bacillus anthracis protective antigen","volume":"267","author":"Novak","year":"1992","journal-title":"J Biol Chem"},{"key":"10.1016\/S0198-8859(97)00081-5_BIB81","doi-asserted-by":"crossref","first-page":"2209","DOI":"10.1073\/pnas.86.7.2209","article-title":"Anthrax toxin","volume":"86","author":"Blaustein","year":"1989","journal-title":"Proc Natl Acad Sci USA"},{"key":"10.1016\/S0198-8859(97)00081-5_BIB82","doi-asserted-by":"crossref","first-page":"647","DOI":"10.1111\/j.1365-2958.1993.tb00936.x","article-title":"pH-dependent permeabilization of the plasma membrane of mammalian cells by anthrax protective antigen","volume":"10","author":"Milne","year":"1993","journal-title":"Mol Microbiol"},{"key":"10.1016\/S0198-8859(97)00081-5_BIB83","doi-asserted-by":"crossref","first-page":"20607","DOI":"10.1016\/S0021-9258(17)32036-7","article-title":"Anthrax protective antigen forms oligomers during intoxication of mammalian cells","volume":"269","author":"Milne","year":"1994","journal-title":"J Biol Chem"},{"key":"10.1016\/S0198-8859(97)00081-5_BIB84","doi-asserted-by":"crossref","first-page":"661","DOI":"10.1111\/j.1365-2958.1995.tb02375.x","article-title":"Protective antigen-binding domain of anthrax lethal factor mediates translocation of a heterologous protein fused to its amino- or carboxy-terminus","volume":"15","author":"Milne","year":"1995","journal-title":"Mol Microbiol"},{"key":"10.1016\/S0198-8859(97)00081-5_BIB85","doi-asserted-by":"crossref","first-page":"15542","DOI":"10.1016\/S0021-9258(19)49569-0","article-title":"Fusions of anthrax toxin lethal factor to the ADP-ribosylation domain of Pseudomonas exotoxin A are potent cytotoxins which are translocated to the cytosol of mammalian cells","volume":"267","author":"Arora","year":"1992","journal-title":"J Biol Chem"},{"key":"10.1016\/S0198-8859(97)00081-5_BIB86","doi-asserted-by":"crossref","first-page":"4955","DOI":"10.1128\/IAI.62.11.4955-4961.1994","article-title":"Fusions of anthrax toxin lethal factor with shiga toxin and diphtheria toxin enzymatic domains are toxic to mammalian cells","volume":"62","author":"Arora","year":"1994","journal-title":"Infect Immun"},{"key":"10.1016\/S0198-8859(97)00081-5_BIB87","doi-asserted-by":"crossref","first-page":"26165","DOI":"10.1016\/S0021-9258(18)47173-6","article-title":"Cytotoxic effects of a chimeric protein consisting of tetanus toxin light chain and anthrax toxin lethal factor in non-neuronal cells","volume":"269","author":"Arora","year":"1994","journal-title":"J Biol Chem"},{"key":"10.1016\/S0198-8859(97)00081-5_BIB88","doi-asserted-by":"crossref","first-page":"3334","DOI":"10.1016\/S0021-9258(18)53698-X","article-title":"Residues 1\u2013254 of anthrax toxin lethal factor are sufficient to cause cellular uptake of fused polypeptides","volume":"268","author":"Arora","year":"1993","journal-title":"J Biol Chem"},{"key":"10.1016\/S0198-8859(97)00081-5_BIB89","doi-asserted-by":"crossref","first-page":"12531","DOI":"10.1073\/pnas.93.22.12531","article-title":"Anthrax toxin-mediated delivery of a cytotoxic T-cell epitope in vivo","volume":"93","author":"Ballard","year":"1996","journal-title":"Proc Natl Acad Sci USA"},{"key":"10.1016\/S0198-8859(97)00081-5_BIB90","doi-asserted-by":"crossref","first-page":"726","DOI":"10.1126\/science.7732382","article-title":"Inhibition of proteasome activities and subunit-specific amino-terminal threonine modification by lactacystin","volume":"268","author":"Fenteany","year":"1995","journal-title":"Science"}],"container-title":["Human Immunology"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0198885997000815?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0198885997000815?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2023,4,11]],"date-time":"2023-04-11T18:59:10Z","timestamp":1681239550000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0198885997000815"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[1997,5]]},"references-count":90,"journal-issue":{"issue":"2","published-print":{"date-parts":[[1997,5]]}},"alternative-id":["S0198885997000815"],"URL":"https:\/\/doi.org\/10.1016\/s0198-8859(97)00081-5","relation":{},"ISSN":["0198-8859"],"issn-type":[{"value":"0198-8859","type":"print"}],"subject":[],"published":{"date-parts":[[1997,5]]}}}