{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,3,16]],"date-time":"2026-03-16T11:23:57Z","timestamp":1773660237974,"version":"3.50.1"},"reference-count":152,"publisher":"Wiley","issue":"4","license":[{"start":{"date-parts":[[2002,7,12]],"date-time":"2002-07-12T00:00:00Z","timestamp":1026432000000},"content-version":"vor","delay-in-days":11,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"funder":[{"name":"Istituto Superiore di Sanit\u00e0, Italy","award":["40C.68"],"award-info":[{"award-number":["40C.68"]}]},{"name":"MURST"},{"name":"PRIN"},{"name":"Progetto di Ricerca di Ateneo (A.L.)"},{"name":"Medical Research Council, UK (H.S.M.)"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Reviews in Medical Virology"],"published-print":{"date-parts":[[2002,7]]},"abstract":"<jats:title>Abstract<\/jats:title><jats:p>Most cellular and viral processes depend on the coordinated formation of protein\u2013protein interactions. With a better understanding of the molecular biology and biochemistry of human viruses it has become possible to screen for and detect inhibitors with activity against specific viral functions and to develop new approaches for the treatment of viral infections. A novel strategy to inhibit viral replication is based on the disruption of viral protein\u2013protein complexes by peptides that mimic either face of the interaction between subunits. Peptides and peptide mimetics capable of dissociating protein\u2013protein interactions have such exquisite specificity that they hold great promise as the next generation of therapeutic agents. This review is focused on recent developments using peptides and small molecules to inhibit protein\u2013protein interactions between cellular and\/or viral proteins with comments on the practicalities of transforming chemical leads into derivatives with the characteristics desired of medicinal compounds. Copyright \u00a9 2002 John Wiley &amp; Sons, Ltd.<\/jats:p>","DOI":"10.1002\/rmv.356","type":"journal-article","created":{"date-parts":[[2002,9,11]],"date-time":"2002-09-11T02:05:28Z","timestamp":1031709928000},"page":"239-262","source":"Crossref","is-referenced-by-count":67,"title":["Protein\u2013protein interactions as targets for antiviral chemotherapy"],"prefix":"10.1002","volume":"12","author":[{"given":"Arianna","family":"Loregian","sequence":"first","affiliation":[]},{"given":"Howard S.","family":"Marsden","sequence":"additional","affiliation":[]},{"given":"Giorgio","family":"Pal\u00f9","sequence":"additional","affiliation":[]}],"member":"311","published-online":{"date-parts":[[2002,7,12]]},"reference":[{"key":"e_1_2_1_2_2","first-page":"67","article-title":"Disruption of protein\u2010subunit interactions","volume":"3","author":"Marsden HS","year":"1992","journal-title":"Semin Virol"},{"key":"e_1_2_1_3_2","doi-asserted-by":"publisher","DOI":"10.1038\/321439a0"},{"key":"e_1_2_1_4_2","doi-asserted-by":"publisher","DOI":"10.1038\/321441a0"},{"key":"e_1_2_1_5_2","doi-asserted-by":"crossref","first-page":"408","DOI":"10.1128\/jvi.9.3.408-418.1972","article-title":"Ribonucleotide reductase activity of synchronized KB cells infected with herpes simplex virus","volume":"9","author":"Cohen GH","year":"1972","journal-title":"J Virol"},{"key":"e_1_2_1_6_2","doi-asserted-by":"publisher","DOI":"10.1099\/0022-1317-64-3-513"},{"key":"e_1_2_1_7_2","doi-asserted-by":"publisher","DOI":"10.1016\/S0021-9258(19)39357-3"},{"key":"e_1_2_1_8_2","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.86.3.1051"},{"key":"e_1_2_1_9_2","doi-asserted-by":"publisher","DOI":"10.1016\/0166-3542(90)90070-N"},{"key":"e_1_2_1_10_2","first-page":"1223","article-title":"Heterocyclic thiosemicarbazones: correlation between structure, inhibition of ribonucleotide reductase, and inhibition of DNA viruses","volume":"131","author":"Brockman RW","year":"1979","journal-title":"Proc Soc Exp Biol Med"},{"key":"e_1_2_1_11_2","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.82.12.4254"},{"key":"e_1_2_1_12_2","doi-asserted-by":"crossref","first-page":"16045","DOI":"10.1016\/S0021-9258(18)37554-9","article-title":"Mechanism of inhibition of herpes simplex virus (HSV) ribonucleotide reductase by a nonapeptide corresponding to the carboxy\u2010terminus of its subunit 2","volume":"263","author":"Paradis H","year":"1988","journal-title":"J Biol Chem"},{"key":"e_1_2_1_13_2","doi-asserted-by":"publisher","DOI":"10.1016\/0042-6822(88)90421-7"},{"key":"e_1_2_1_14_2","doi-asserted-by":"crossref","first-page":"893","DOI":"10.1128\/jvi.41.3.893-900.1982","article-title":"Induction of a new ribonucleotide reductase after infection of mouse L cells with pseudorabies virus","volume":"41","author":"Lankinen H","year":"1982","journal-title":"J Virol"},{"key":"e_1_2_1_15_2","doi-asserted-by":"publisher","DOI":"10.1016\/0042-6822(78)90058-2"},{"key":"e_1_2_1_16_2","doi-asserted-by":"publisher","DOI":"10.1016\/0006-2952(87)90682-4"},{"key":"e_1_2_1_17_2","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.91.19.8994"},{"key":"e_1_2_1_18_2","doi-asserted-by":"publisher","DOI":"10.1038\/372695a0"},{"key":"e_1_2_1_19_2","doi-asserted-by":"crossref","first-page":"1078","DOI":"10.1128\/AAC.40.5.1078","article-title":"Evaluation of a peptidomimetic ribonucleotide reductase inhibitor with a murine model of herpes simplex virus type 1 ocular disease","volume":"40","author":"Brandt CR","year":"1996","journal-title":"Antimicrob Agents Chemother"},{"key":"e_1_2_1_20_2","doi-asserted-by":"publisher","DOI":"10.1021\/jm00072a021"},{"key":"e_1_2_1_21_2","doi-asserted-by":"publisher","DOI":"10.1021\/jm00018a022"},{"key":"e_1_2_1_22_2","doi-asserted-by":"publisher","DOI":"10.1021\/jm950825x"},{"key":"e_1_2_1_23_2","doi-asserted-by":"publisher","DOI":"10.1021\/jm960324r"},{"key":"e_1_2_1_24_2","doi-asserted-by":"crossref","first-page":"1629","DOI":"10.1128\/AAC.42.7.1629","article-title":"Antiviral activity of a selective ribonucleotide reductase inhibitor against acyclovir\u2010resistant herpes simplex virus type 1 in vivo","volume":"42","author":"Duan J","year":"1998","journal-title":"Antimicrob Agents Chemother"},{"key":"e_1_2_1_25_2","doi-asserted-by":"publisher","DOI":"10.1016\/0042-6822(88)90144-4"},{"key":"e_1_2_1_26_2","first-page":"783","article-title":"Resistance of herpes simplex virus type 1 to peptidomimetic ribonucleotide reductase inhibitors: selection and characterisation of mutant isolates","volume":"70","author":"Bonneau A\u2010M","year":"1996","journal-title":"J Virol"},{"key":"e_1_2_1_27_2","first-page":"3","article-title":"Molecular aspects of antiherpesvirus drugs","volume":"3","author":"Coen DM","year":"1992","journal-title":"Semin Virol"},{"key":"e_1_2_1_28_2","doi-asserted-by":"publisher","DOI":"10.1016\/S0195-6701(96)90010-9"},{"key":"e_1_2_1_29_2","doi-asserted-by":"crossref","first-page":"5023","DOI":"10.1128\/jvi.63.12.5023-5029.1989","article-title":"The essential 65\u2010kilodalton DNA\u2010binding protein of herpes simplex virus stimulates the virus\u2010encoded DNA polymerase","volume":"63","author":"Gallo ML","year":"1989","journal-title":"J Virol"},{"key":"e_1_2_1_30_2","doi-asserted-by":"publisher","DOI":"10.1128\/JVI.64.12.5976-5987.1990"},{"key":"e_1_2_1_31_2","doi-asserted-by":"crossref","first-page":"398","DOI":"10.1128\/jvi.67.1.398-406.1993","article-title":"The extreme C\u2010terminus of herpes simplex virus DNA polymerase is crucial for functional interaction with processivity factor UL42 and for viral replication","volume":"67","author":"Digard P","year":"1993","journal-title":"J Virol"},{"key":"e_1_2_1_32_2","doi-asserted-by":"crossref","first-page":"543","DOI":"10.1128\/jvi.67.1.543-547.1993","article-title":"Mutations in the C terminus of herpes simplex virus type 1 DNA polymerase can affect binding and stimulation by its accessory protein UL42 without affecting basal polymerase activity","volume":"67","author":"Tenney DJ","year":"1993","journal-title":"J Virol"},{"key":"e_1_2_1_33_2","doi-asserted-by":"publisher","DOI":"10.1093\/nar\/21.1.87"},{"key":"e_1_2_1_34_2","doi-asserted-by":"crossref","first-page":"1159","DOI":"10.1128\/jvi.67.3.1159-1168.1993","article-title":"Functional analysis of the herpes simplex virus UL42 protein","volume":"67","author":"Digard P","year":"1993","journal-title":"J Virol"},{"key":"e_1_2_1_35_2","doi-asserted-by":"crossref","first-page":"17393","DOI":"10.1016\/S0021-9258(18)38170-5","article-title":"A novel functional domain of an \u03b1\u2010like DNA polymerase","volume":"265","author":"Digard P","year":"1990","journal-title":"J Biol Chem"},{"key":"e_1_2_1_36_2","doi-asserted-by":"publisher","DOI":"10.1099\/0022-1317-75-11-3127"},{"key":"e_1_2_1_37_2","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.92.5.1456"},{"key":"e_1_2_1_38_2","doi-asserted-by":"publisher","DOI":"10.1074\/jbc.275.1.472"},{"key":"e_1_2_1_39_2","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.96.9.5221"},{"key":"e_1_2_1_40_2","doi-asserted-by":"publisher","DOI":"10.1006\/viro.2000.0390"},{"key":"e_1_2_1_41_2","doi-asserted-by":"publisher","DOI":"10.1016\/S1097-2765(00)80422-0"},{"key":"e_1_2_1_42_2","doi-asserted-by":"publisher","DOI":"10.1128\/JVI.75.11.4990-4998.2001"},{"key":"e_1_2_1_43_2","doi-asserted-by":"crossref","first-page":"501","DOI":"10.1128\/jvi.53.2.501-508.1985","article-title":"DNA\u2010binding protein associated with herpes simplex virus DNA polymerase","volume":"53","author":"Vaughan PJ","year":"1985","journal-title":"J Virol"},{"key":"e_1_2_1_44_2","doi-asserted-by":"crossref","first-page":"4126","DOI":"10.1128\/jvi.66.7.4126-4133.1992","article-title":"Physical and functional interaction of human cytomegalovirus DNA polymerase and its accessory protein (ICP36) expressed in insect cells","volume":"66","author":"Ertl PF","year":"1992","journal-title":"J Virol"},{"key":"e_1_2_1_45_2","doi-asserted-by":"publisher","DOI":"10.1099\/0022-1317-67-9-1759"},{"key":"e_1_2_1_46_2","doi-asserted-by":"crossref","first-page":"1669","DOI":"10.1128\/jvi.69.3.1669-1677.1995","article-title":"Bipartite DNA\u2010binding region of Epstein\u2010Barr virus BRMF1 product essential for DNA polymerase accessory function","volume":"69","author":"Kiehl A","year":"1995","journal-title":"J Virol"},{"key":"e_1_2_1_47_2","doi-asserted-by":"crossref","first-page":"2811","DOI":"10.1128\/jvi.69.5.2811-2818.1995","article-title":"Cloning, sequencing, and functional characterization of the two subunits of the pseudorabies virus DNA polymerase holoenzyme: evidence for specificity of interaction","volume":"69","author":"Berthomme H","year":"1995","journal-title":"J Virol"},{"key":"e_1_2_1_48_2","doi-asserted-by":"crossref","first-page":"6228","DOI":"10.1128\/JVI.72.7.6228-6232.1998","article-title":"Cloning and functional analysis of Kaposi's sarcoma\u2010associated herpesvirus DNA polymerase and its processivity factor","volume":"72","author":"Lin K","year":"1998","journal-title":"J Virol"},{"key":"e_1_2_1_49_2","doi-asserted-by":"publisher","DOI":"10.1128\/JVI.74.23.10920-10929.2000"},{"key":"e_1_2_1_50_2","doi-asserted-by":"crossref","first-page":"2047","DOI":"10.1128\/jvi.69.4.2047-2057.1995","article-title":"Cytomegalovirus\u2010mediated induction of antisense mRNA expression to UL44 inhibits virus replication in astrocytoma cell line: identification of an essential gene","volume":"69","author":"Ripalti A","year":"1995","journal-title":"J Virol"},{"key":"e_1_2_1_51_2","doi-asserted-by":"publisher","DOI":"10.1016\/0042-6822(92)90706-U"},{"key":"e_1_2_1_52_2","doi-asserted-by":"publisher","DOI":"10.1038\/340245a0"},{"key":"e_1_2_1_53_2","doi-asserted-by":"crossref","first-page":"66","DOI":"10.1093\/oso\/9780199637133.003.0003","volume-title":"DNA Virus Replication. Frontiers in Molecular Biology Series","author":"Stow ND","year":"2000"},{"key":"e_1_2_1_54_2","doi-asserted-by":"crossref","first-page":"6390","DOI":"10.1128\/jvi.71.9.6390-6397.1997","article-title":"The catalytic subunit of the DNA polymerase of herpes simplex virus type 1 interacts specifically with the C\u2010terminus of the UL8 component of the viral helicase\u2010primase complex","volume":"71","author":"Marsden HS","year":"1997","journal-title":"J Virol"},{"key":"e_1_2_1_55_2","doi-asserted-by":"publisher","DOI":"10.1099\/0022-1317-75-10-2699"},{"key":"e_1_2_1_56_2","doi-asserted-by":"publisher","DOI":"10.1093\/nar\/13.21.7865"},{"key":"e_1_2_1_57_2","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.82.17.5870"},{"key":"e_1_2_1_58_2","doi-asserted-by":"publisher","DOI":"10.1006\/smvy.1993.1010"},{"key":"e_1_2_1_59_2","doi-asserted-by":"crossref","first-page":"2260","DOI":"10.1128\/jvi.63.5.2260-2269.1989","article-title":"Construction and characterization of a herpes simplex virus type 1 mutant unable to transinduce immediate\u2010early gene expression","volume":"63","author":"Ace CI","year":"1989","journal-title":"J Virol"},{"key":"e_1_2_1_60_2","doi-asserted-by":"publisher","DOI":"10.1038\/335452a0"},{"key":"e_1_2_1_61_2","doi-asserted-by":"publisher","DOI":"10.1038\/344257a0"},{"key":"e_1_2_1_62_2","doi-asserted-by":"crossref","first-page":"852","DOI":"10.1128\/jvi.67.2.852-862.1993","article-title":"Mapping of a major surface\u2010exposed site in herpes simplex virus protein Vmw65 to a region of direct interaction in a transcription complex assembly","volume":"67","author":"Hayes S","year":"1993","journal-title":"J Virol"},{"key":"e_1_2_1_63_2","doi-asserted-by":"publisher","DOI":"10.1128\/MCB.14.5.3484"},{"key":"e_1_2_1_64_2","doi-asserted-by":"crossref","first-page":"3886","DOI":"10.1128\/jvi.71.5.3886-3894.1997","article-title":"Protein interactions in the herpes simplex virus type 1 VP16\u2010induced complex: VP16 peptide inhibition and mutational analysis of host cell factor requirements","volume":"71","author":"Simmen KA","year":"1997","journal-title":"J Virol"},{"key":"e_1_2_1_65_2","doi-asserted-by":"publisher","DOI":"10.1002\/1099-1654(200007\/08)10:4<231::AID-RMV290>3.0.CO;2-P"},{"key":"e_1_2_1_66_2","doi-asserted-by":"publisher","DOI":"10.1126\/science.2548279"},{"key":"e_1_2_1_67_2","doi-asserted-by":"crossref","first-page":"15591","DOI":"10.1016\/S0021-9258(18)98445-0","article-title":"Dissociative inhibition of dimeric enzymes: kinetic characterization of the inhibition of HIV\u20101 protease by its COOH\u2010terminal tetrapeptides","volume":"266","author":"Zhang ZY","year":"1991","journal-title":"J Biol Chem"},{"key":"e_1_2_1_68_2","doi-asserted-by":"publisher","DOI":"10.1002\/pro.5560011003"},{"key":"e_1_2_1_69_2","doi-asserted-by":"publisher","DOI":"10.1016\/0166-3542(96)00940-0"},{"key":"e_1_2_1_70_2","doi-asserted-by":"publisher","DOI":"10.1021\/ja962496j"},{"key":"e_1_2_1_71_2","doi-asserted-by":"publisher","DOI":"10.1021\/jm9803976"},{"key":"e_1_2_1_72_2","doi-asserted-by":"publisher","DOI":"10.1016\/S0166-0934(97)00202-4"},{"key":"e_1_2_1_73_2","doi-asserted-by":"publisher","DOI":"10.1038\/78451"},{"key":"e_1_2_1_74_2","doi-asserted-by":"publisher","DOI":"10.1126\/science.1377403"},{"key":"e_1_2_1_75_2","doi-asserted-by":"publisher","DOI":"10.1016\/S0021-9258(17)36800-X"},{"key":"e_1_2_1_76_2","doi-asserted-by":"publisher","DOI":"10.1074\/jbc.274.35.24941"},{"key":"e_1_2_1_77_2","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.150220297"},{"key":"e_1_2_1_78_2","doi-asserted-by":"publisher","DOI":"10.1111\/j.1432-1033.1996.0765h.x"},{"key":"e_1_2_1_79_2","doi-asserted-by":"publisher","DOI":"10.1046\/j.1432-1327.1999.00130.x"},{"key":"e_1_2_1_80_2","doi-asserted-by":"publisher","DOI":"10.1097\/00002030-199106000-00001"},{"key":"e_1_2_1_81_2","doi-asserted-by":"publisher","DOI":"10.1002\/prot.340130204"},{"key":"e_1_2_1_82_2","doi-asserted-by":"publisher","DOI":"10.1006\/viro.1998.9526"},{"key":"e_1_2_1_83_2","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.91.21.9770"},{"key":"e_1_2_1_84_2","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.94.25.13426"},{"key":"e_1_2_1_85_2","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.95.26.15613"},{"key":"e_1_2_1_86_2","doi-asserted-by":"publisher","DOI":"10.1016\/S0092-8674(00)80205-6"},{"key":"e_1_2_1_87_2","doi-asserted-by":"publisher","DOI":"10.1038\/3293"},{"key":"e_1_2_1_88_2","doi-asserted-by":"publisher","DOI":"10.1126\/science.1057453"},{"key":"e_1_2_1_89_2","doi-asserted-by":"publisher","DOI":"10.1097\/00002030-200100005-00002"},{"key":"e_1_2_1_90_2","doi-asserted-by":"publisher","DOI":"10.1126\/science.2453925"},{"key":"e_1_2_1_91_2","doi-asserted-by":"publisher","DOI":"10.1021\/bi980652o"},{"key":"e_1_2_1_92_2","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.89.13.5872"},{"key":"e_1_2_1_93_2","doi-asserted-by":"publisher","DOI":"10.1016\/S0968-0896(00)82049-0"},{"key":"e_1_2_1_94_2","doi-asserted-by":"crossref","first-page":"5795","DOI":"10.1128\/JVI.73.7.5795-5802.1999","article-title":"Peptide ligands to human immunodeficiency virus type 1 gp120 identified from phage display libraries","volume":"73","author":"Ferrer M","year":"1999","journal-title":"J Virol"},{"key":"e_1_2_1_95_2","first-page":"569","volume-title":"Clinical Virology","author":"Bonnez W","year":"1997"},{"key":"e_1_2_1_96_2","doi-asserted-by":"publisher","DOI":"10.1101\/SQB.1991.056.01.040"},{"key":"e_1_2_1_97_2","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.91.18.8700"},{"key":"e_1_2_1_98_2","doi-asserted-by":"crossref","first-page":"891","DOI":"10.1128\/jvi.71.2.891-899.1997","article-title":"Mapping and characterisation of the interaction domains of the human papillomavirus type 16 E1 and E2 proteins","volume":"71","author":"Yagusi T","year":"1997","journal-title":"J Virol"},{"key":"e_1_2_1_99_2","doi-asserted-by":"crossref","first-page":"8166","DOI":"10.1128\/JVI.72.10.8166-8173.1998","article-title":"A fifteen\u2010amino\u2010acid peptide inhibits human papilloma E1\u2010E2 interaction and human papillomavirus DNA replication in vitro","volume":"72","author":"Kasukawa H","year":"1998","journal-title":"J Virol"},{"key":"e_1_2_1_100_2","doi-asserted-by":"crossref","first-page":"849","DOI":"10.1128\/jvi.69.2.849-855.1995","article-title":"The N\u2010terminal domain of the Sendai paramyxovirus P protein acts as a chaperone for the NP protein during the nascent chain assembly step of genome replication","volume":"69","author":"Curran J","year":"1995","journal-title":"J Virol"},{"key":"e_1_2_1_101_2","doi-asserted-by":"publisher","DOI":"10.1006\/viro.1993.1366"},{"key":"e_1_2_1_102_2","doi-asserted-by":"publisher","DOI":"10.1006\/viro.2001.1150"},{"key":"e_1_2_1_103_2","doi-asserted-by":"publisher","DOI":"10.1126\/science.282.5394.1669"},{"key":"e_1_2_1_104_2","doi-asserted-by":"publisher","DOI":"10.1038\/13305"},{"key":"e_1_2_1_105_2","doi-asserted-by":"publisher","DOI":"10.1016\/S0969-2126(01)00168-X"},{"key":"e_1_2_1_106_2","doi-asserted-by":"publisher","DOI":"10.1038\/384023a0"},{"key":"e_1_2_1_107_2","doi-asserted-by":"publisher","DOI":"10.1016\/S1367-5931(97)80004-X"},{"key":"e_1_2_1_108_2","doi-asserted-by":"publisher","DOI":"10.1007\/BF00124387"},{"key":"e_1_2_1_109_2","doi-asserted-by":"publisher","DOI":"10.1034\/j.1399-3011.1999.00119.x"},{"key":"e_1_2_1_110_2","doi-asserted-by":"publisher","DOI":"10.1021\/jm950792l"},{"key":"e_1_2_1_111_2","doi-asserted-by":"publisher","DOI":"10.1021\/jm00064a003"},{"key":"e_1_2_1_112_2","doi-asserted-by":"publisher","DOI":"10.1021\/jm00076a016"},{"key":"e_1_2_1_113_2","doi-asserted-by":"publisher","DOI":"10.1021\/ja00092a006"},{"key":"e_1_2_1_114_2","doi-asserted-by":"publisher","DOI":"10.1002\/prot.340110104"},{"key":"e_1_2_1_115_2","doi-asserted-by":"publisher","DOI":"10.1021\/jm00067a013"},{"key":"e_1_2_1_116_2","doi-asserted-by":"publisher","DOI":"10.1023\/A:1008146201260"},{"key":"e_1_2_1_117_2","doi-asserted-by":"publisher","DOI":"10.1016\/S1093-3263(00)00062-0"},{"key":"e_1_2_1_118_2","doi-asserted-by":"publisher","DOI":"10.1007\/978-3-642-60142-2_5"},{"key":"e_1_2_1_119_2","doi-asserted-by":"publisher","DOI":"10.1146\/annurev.biophys.26.1.401"},{"key":"e_1_2_1_120_2","doi-asserted-by":"publisher","DOI":"10.1016\/S1359-6446(00)01501-4"},{"key":"e_1_2_1_121_2","doi-asserted-by":"publisher","DOI":"10.1126\/science.4001944"},{"key":"e_1_2_1_122_2","doi-asserted-by":"publisher","DOI":"10.1038\/nbt0495-378"},{"key":"e_1_2_1_123_2","doi-asserted-by":"publisher","DOI":"10.2174\/1386207013331228"},{"key":"e_1_2_1_124_2","doi-asserted-by":"publisher","DOI":"10.1002\/prot.340080405"},{"key":"e_1_2_1_125_2","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.92.5.1609"},{"key":"e_1_2_1_126_2","doi-asserted-by":"publisher","DOI":"10.1007\/BF01702598"},{"key":"e_1_2_1_127_2","doi-asserted-by":"publisher","DOI":"10.1016\/S1438-4221(00)80004-1"},{"key":"e_1_2_1_128_2","doi-asserted-by":"publisher","DOI":"10.1016\/S1438-4221(00)80119-8"},{"key":"e_1_2_1_129_2","doi-asserted-by":"publisher","DOI":"10.1038\/nbt0697-553"},{"key":"e_1_2_1_130_2","doi-asserted-by":"publisher","DOI":"10.1038\/nbt0195-53"},{"key":"e_1_2_1_131_2","doi-asserted-by":"publisher","DOI":"10.1128\/JVI.69.4.2406-2411.1995"},{"key":"e_1_2_1_132_2","doi-asserted-by":"publisher","DOI":"10.2174\/1386207013331165"},{"key":"e_1_2_1_133_2","volume-title":"The Yeast Two\u2010hybrid System","author":"Bartel PL","year":"1997"},{"key":"e_1_2_1_134_2","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.93.19.10315"},{"key":"e_1_2_1_135_2","doi-asserted-by":"publisher","DOI":"10.1093\/nar\/27.4.919"},{"key":"e_1_2_1_136_2","doi-asserted-by":"publisher","DOI":"10.1016\/S0167-7799(99)01338-4"},{"key":"e_1_2_1_137_2","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.93.24.13896"},{"key":"e_1_2_1_138_2","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.94.25.13396"},{"key":"e_1_2_1_139_2","doi-asserted-by":"publisher","DOI":"10.1038\/nbt1098-946"},{"key":"e_1_2_1_140_2","doi-asserted-by":"publisher","DOI":"10.1016\/S0021-9258(18)53325-1"},{"key":"e_1_2_1_141_2","doi-asserted-by":"publisher","DOI":"10.1006\/abio.1996.0429"},{"key":"e_1_2_1_142_2","doi-asserted-by":"publisher","DOI":"10.1016\/S0969-2126(01)00176-9"},{"key":"e_1_2_1_143_2","doi-asserted-by":"publisher","DOI":"10.1006\/immu.1994.1021"},{"key":"e_1_2_1_144_2","doi-asserted-by":"publisher","DOI":"10.1006\/bbrc.1994.2222"},{"key":"e_1_2_1_145_2","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.93.16.8437"},{"key":"e_1_2_1_146_2","doi-asserted-by":"crossref","first-page":"4309","DOI":"10.1016\/S0021-9258(20)64323-X","article-title":"Uptake and concentration of bioactive macromolecules by K562 cells via the transferrin cycle utilizing an acid\u2010labile transferrin","volume":"266","author":"Wellhoner HH","year":"1991","journal-title":"J Biol Chem"},{"key":"e_1_2_1_147_2","doi-asserted-by":"publisher","DOI":"10.1083\/jcb.113.5.1025"},{"key":"e_1_2_1_148_2","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.90.8.3530"},{"key":"e_1_2_1_149_2","doi-asserted-by":"publisher","DOI":"10.1016\/S0092-8674(00)81843-7"},{"key":"e_1_2_1_150_2","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.91.2.664"},{"key":"e_1_2_1_151_2","doi-asserted-by":"crossref","first-page":"596","DOI":"10.1128\/mr.47.4.596-620.1983","article-title":"Membrane receptor for bacterial toxins","volume":"47","author":"Eidels L","year":"1983","journal-title":"Microbiol Rev"},{"key":"e_1_2_1_152_2","doi-asserted-by":"crossref","first-page":"8764","DOI":"10.1016\/S0021-9258(19)87394-5","article-title":"Crystal structure of the B subunit of Escherichia coli heat\u2010labile enterotoxin carrying peptides with anti\u2010herpes simplex virus type 1 activity","volume":"274","author":"Matkovic\u2010Calovica D","year":"1999","journal-title":"J Biol Chem"},{"key":"e_1_2_1_153_2","doi-asserted-by":"publisher","DOI":"10.1128\/MMBR.56.4.622-647.1992"}],"container-title":["Reviews in Medical Virology"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.wiley.com\/onlinelibrary\/tdm\/v1\/articles\/10.1002%2Frmv.356","content-type":"unspecified","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/onlinelibrary.wiley.com\/doi\/pdf\/10.1002\/rmv.356","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2023,11,18]],"date-time":"2023-11-18T08:15:46Z","timestamp":1700295346000},"score":1,"resource":{"primary":{"URL":"https:\/\/onlinelibrary.wiley.com\/doi\/10.1002\/rmv.356"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2002,7]]},"references-count":152,"journal-issue":{"issue":"4","published-print":{"date-parts":[[2002,7]]}},"alternative-id":["10.1002\/rmv.356"],"URL":"https:\/\/doi.org\/10.1002\/rmv.356","archive":["Portico"],"relation":{},"ISSN":["1052-9276","1099-1654"],"issn-type":[{"value":"1052-9276","type":"print"},{"value":"1099-1654","type":"electronic"}],"subject":[],"published":{"date-parts":[[2002,7]]}}}