536:– the regulation of translation has become a well-studied field. Human translational control is of increasing research interest as it has connotations in a range of diseases. Orthologs of many of the factors involved in human translation are shared by a range of eukaryotic organisms; some of which are used as
544:
eggs upon fertilization, rodent brain and rabbit reticulocytes. Monod and Jacob were among the first to propose that "the synthesis of individual proteins may be provoked or suppressed within a cell, under the influence of specific external agents, and the relative rates at which different proteins
630:(25 kDa), eIF4G (185 kDa) acts as a scaffold for the complex whilst the ATP-dependent RNA helicase eIF4A (46 kDa) processes the secondary structure of the mRNA 5’ UTR to render it more conducive to ribosomal binding and subsequent translation. Together these three proteins are referred to as
696:(2000) revealed that the molecule is approximately 80 Å in length and has a “dumbbell” shape where the proximal section represents an 11 residue (18 Å) linker postulated to confer a degree of flexibility and distension to the molecule in solution. eIF4A is an abundant cytoplasmic protein.
650:
seemed to indicate that eIF4A has a higher binding affinity for ADP than ATP except in the presence of eIF4B, which increased the ATP binding affinity tenfold without affecting ADP affinity. Once bound to the 5’ cap of mRNA, this 48S complex then searches for the (usually) AUG
687:
helicase family, so-called due to their conserved four-residue D-E-A-D sequence. This family of helicases is found in a range of prokaryotic and eukaryotic organisms including humans, wherein they catalyse a variety of processes including embryogenesis and
553:
in eukaryotes is divided into translation initiation, elongation, and termination of these stages; the initiation of translation is the rate limiting step. Within the process of translation initiation; the bottleneck occurs shortly before the
703:
in a ratio of 4:1, respectively. The third isoform; eIF4A III, which shares only 65% similarity to the other isoforms is believed to be a core component of the exon junction complex involved in pre-mRNA splicing.
598:. Before translation can progress to the elongation stage, a number of initiation factors must facilitate the synergy of the ribosome and the mRNA and ensure that the 5’ UTR of the mRNA is sufficiently devoid of
1373:
Holzmann K, Gerner C, Pöltl A, Schäfer R, Obrist P, Ensinger C, Grimm R, Sauermann G (Jan 2000). "A human common nuclear matrix protein homologous to eukaryotic translation initiation factor 4A".
1300:
Jones E, Quinn CM, See CG, Montgomery DS, Ford MJ, Kölble K, Gordon S, Greaves DR (Oct 1998). "The linked human elongation initiation factor 4A1 (EIF4A1) and CD68 genes map to chromosome 17p13".
549:, of which the preceding supposition by Monod and Jacob is an example; contemporary researchers still have much to learn about the modulation of genetic expression. Synthesis of protein from
606:
has implications in the normal regulation of translation as well as the transformation and progression of cancerous cells; as such, it represents an interesting field of research.
1216:
Bi X, Ren J, Goss DJ (May 2000). "Wheat germ translation initiation factor eIF4B affects eIF4A and eIFiso4F helicase activity by increasing the ATP binding affinity of eIF4A".
545:
may be profoundly altered, depending upon external conditions". Almost half a century after the flurry of postulations arising from the revelation of the central dogma of
1338:
Sudo K, Takahashi E, Nakamura Y (1995). "Isolation and mapping of the human EIF4A2 gene homologous to the murine protein synthesis initiation factor 4A-II gene Eif4a2".
362:
201:
52:
867:
Gingras AC, Raught B, Sonenberg N (June 1999). "eIF4 initiation factors: effectors of mRNA recruitment to ribosomes and regulators of translation".
1712:
Bordeleau ME, Matthews J, Wojnar JM, Lindqvist L, Novac O, Jankowsky E, Sonenberg N, Northcote P, Teesdale-Spittle P, Pelletier J (Jul 2005).
902:
Hollams EM, Giles KM, Thomson AM, Leedman PJ (Oct 2002). "MRNA stability and the control of gene expression: implications for human disease".
1776:
1116:
1781:
1107:
Hershey JW Merrick WC (2000). "Pathway and mechanism of initiation of protein synthesis". In
Mathews M, Sonenberg N, Hershey JW (eds.).
386:
225:
76:
764:
1463:"Foot-and-mouth disease virus 3C protease induces cleavage of translation initiation factors eIF4A and eIF4G within infected cells"
1132:
Yao N, Hesson T, Cable M, Hong Z, Kwong AD, Le HV, Weber PC (Jun 1997). "Structure of the hepatitis C virus RNA helicase domain".
699:
Three isoforms of eIF4A exist; I and II share 95% amino acid similarity and have been found simultaneously in rabbit reticulocyte
980:
Vargas R, Castañeda M (Feb 1983). "Age-dependent decrease in the activity of protein-synthesis initiation factors in rat brain".
374:
213:
64:
1714:"Stimulation of mammalian translation initiation factor eIF4A activity by a small molecule inhibitor of eukaryotic translation"
1177:"Interaction between the NH2-terminal domain of eIF4A and the central domain of eIF4G modulates RNA-stimulated ATPase activity"
718:
367:
206:
57:
1624:"Translational control by a small RNA: dendritic BC1 RNA targets the eukaryotic initiation factor 4A helicase mechanism"
713:
667:
has a transcript length of 1741bp, contains 11 exons, and is located on chromosome 17. The genes for human isoforms
558:
binds to the 5’ m7GTP facilitated by a number of proteins; it is at this stage that constrictions born of stress,
810:"Crystal structure of the yeast eIF4A-eIF4G complex: an RNA-helicase controlled by protein-protein interactions"
266:
1786:
614:
The repertoire of compounds involved in eukaryotic translation consists of initiation factor classes 1 – 6;
575:
379:
218:
69:
432:
122:
692:
as well as translation initiation. Crystallographic analysis of yeast eIF4A carried out by
Carruthers
1725:
1572:
945:
Castañeda M (Apr 1969). "The activity of ribosomes of sea urchin eggs in response to fertilization".
821:
550:
283:
1512:"Mutational analysis of a DEAD box RNA helicase: the mammalian translation initiation factor eIF-4A"
532:
are immensely complex; it is therefore unsurprising that regulation occurs at a number of stages of
689:
599:
591:
1025:"Eukaryotic initiation factors 4A (eIF4A) and 4G (eIF4G) mutually interact in a 1:1 ratio in vivo"
1157:
1089:
1005:
927:
782:
1753:
1694:
1653:
1600:
1541:
1492:
1443:
1390:
1355:
1317:
1282:
1233:
1198:
1149:
1112:
1081:
1046:
997:
962:
919:
884:
849:
808:
SchĂĽtz P, Bumann M, Oberholzer AE, Bieniossek C, Trachsel H, Altmann M, Baumann U (Jul 2008).
770:
760:
546:
533:
1743:
1733:
1684:
1643:
1635:
1590:
1580:
1531:
1523:
1482:
1474:
1433:
1425:
1382:
1347:
1309:
1272:
1264:
1225:
1188:
1141:
1073:
1036:
989:
954:
911:
876:
839:
829:
752:
436:
427:
278:
117:
1064:
Jacob F, Monod J (Jun 1961). "Genetic regulatory mechanisms in the synthesis of proteins".
1409:
794:
595:
587:
571:
456:
307:
271:
146:
126:
287:
1729:
1576:
825:
1748:
1713:
1648:
1623:
1527:
1438:
1413:
844:
809:
537:
1689:
1536:
1511:
1487:
1462:
1277:
1252:
1077:
756:
1770:
1595:
1560:
993:
958:
880:
723:
502:
1161:
1093:
1009:
931:
1619:
1478:
403:
242:
93:
1673:"The p46 subunit of eukaryotic initiation factor (eIF)-4F exchanges with eIF-4A"
728:
652:
647:
466:
317:
156:
1718:
Proceedings of the
National Academy of Sciences of the United States of America
1565:
Proceedings of the
National Academy of Sciences of the United States of America
814:
Proceedings of the
National Academy of Sciences of the United States of America
602:. Binding in this way is facilitated by group 4 eukaryotic initiation factors;
915:
579:
559:
541:
410:
249:
100:
1585:
1253:"Nucleotide sequence of human cDNA encoding eukaryotic initiation factor 4AI"
540:
for the investigation of translation initiation and elongation, for example:
1738:
1672:
1268:
834:
529:
1757:
1657:
1604:
1496:
1447:
1394:
1386:
1313:
1237:
1202:
1193:
1176:
1085:
1050:
1041:
1024:
923:
888:
853:
774:
1698:
1561:"Crystal structure of yeast initiation factor 4A, a DEAD-box RNA helicase"
1545:
1359:
1321:
1286:
1153:
1001:
966:
1639:
947:
Biochimica et
Biophysica Acta (BBA) - Nucleic Acids and Protein Synthesis
684:
683:
The 407 residue, 46 kDa, protein eIF4A is the prototypical member of the
555:
513:
509:
415:
254:
105:
1429:
1145:
1111:. Plainview, N.Y: Cold Spring Harbor Laboratory Press. pp. 33–88.
487:
1351:
1229:
672:
668:
664:
498:
494:
490:
398:
347:
332:
237:
186:
171:
88:
37:
22:
700:
639:
635:
631:
627:
615:
603:
623:
583:
391:
230:
81:
586:– this process is regulated by guanine nucleotide exchange and
619:
517:
506:
1671:
Yoder-Hill J, Pause A, Sonenberg N, Merrick WC (Mar 1993).
1414:"eIF4A3 is a novel component of the exon junction complex"
1175:
Korneeva NL, First EA, Benoit CA, Rhoads RE (Jan 2005).
570:
Eukaryotic initiation factor complex 2 (eIF2) forms a
333:
eukaryotic translation initiation factor 4A, isoform 3
172:
eukaryotic translation initiation factor 4A, isoform 2
23:
eukaryotic translation initiation factor 4A, isoform 1
618:
is responsible for the binding of capped mRNA to the
1461:Belsham GJ, McInerney GM, Ross-Smith N (Jan 2000).
1375:
462:
452:
447:
426:
421:
409:
397:
385:
373:
361:
353:
343:
338:
331:
313:
303:
298:
277:
265:
260:
248:
236:
224:
212:
200:
192:
182:
177:
170:
152:
142:
137:
116:
111:
99:
87:
75:
63:
51:
43:
33:
28:
21:
528:The mechanisms governing the basic subsistence of
501:. These factors are required for the binding of
1559:Caruthers JM, Johnson ER, McKay DB (Nov 2000).
1333:
1331:
749:eIF4A: the godfather of the DEAD box helicases
675:reside on chromosomes 3 and 17 respectively.
8:
1408:Chan CC, Dostie J, Diem MD, Feng W, Mann M,
634:. For maximal activity; eIF4A also requires
1251:Kim NS, Kato T, Abe N, Kato S (Apr 1993).
512:subunits. In addition these proteins are
444:
295:
134:
1747:
1737:
1688:
1647:
1594:
1584:
1535:
1486:
1437:
1276:
1192:
1040:
843:
833:
1109:Translational control of gene expression
747:Rogers GW, Komar AA, Merrick WC (2002).
516:that function to unwind double-stranded
1023:Li W, Belsham GJ, Proud CG (Aug 2001).
739:
719:Eukaryotic initiation factor 4F (eIF4F)
486:) family consists of 3 closely related
790:
780:
638:(80 kDa), which itself is enhanced by
328:
167:
18:
7:
982:Mechanisms of Ageing and Development
1677:The Journal of Biological Chemistry
1181:The Journal of Biological Chemistry
1029:The Journal of Biological Chemistry
1528:10.1002/j.1460-2075.1992.tb05330.x
642:(25 kDa). A study conducted by Bi
14:
1510:Pause A, Sonenberg N (Jul 1992).
751:. Vol. 72. pp. 307–31.
881:10.1146/annurev.biochem.68.1.913
480:eukaryotic initiation factor-4A
1628:Molecular and Cellular Biology
1618:Lin D, Pestova TV, Hellen CU,
1340:Cytogenetics and Cell Genetics
1:
1690:10.1016/S0021-9258(18)53358-5
1479:10.1128/JVI.74.1.272-280.2000
1078:10.1016/S0022-2836(61)80072-7
869:Annual Review of Biochemistry
757:10.1016/S0079-6603(02)72073-4
663:In humans, the gene encoding
562:starvation etc. take effect.
1777:Genes on human chromosome 17
1066:Journal of Molecular Biology
994:10.1016/0047-6374(83)90073-8
959:10.1016/0005-2787(69)90046-X
714:Eukaryotic initiation factor
1782:Genes on human chromosome 3
626:. The mRNA cap is bound by
1803:
1412:, Dreyfuss G (Feb 2004).
1134:Nature Structural Biology
443:
294:
133:
1586:10.1073/pnas.97.24.13080
655:and translation begins.
1739:10.1073/pnas.0504249102
916:10.1023/A:1020992418511
835:10.1073/pnas.0800418105
590:and serves as the main
1387:10.1006/bbrc.1999.1973
1314:10.1006/geno.1998.5515
1257:Nucleic Acids Research
1194:10.1074/jbc.M406168200
1042:10.1074/jbc.C100284200
904:Neurochemical Research
622:ribosomal subunit via
1269:10.1093/nar/21.8.2012
594:of the bottleneck of
1640:10.1128/MCB.01800-07
551:mature messenger RNA
1730:2005PNAS..10210460B
1577:2000PNAS...9713080C
1467:Journal of Virology
1430:10.1261/rna.5230104
1146:10.1038/nsb0697-463
826:2008PNAS..105.9564S
600:secondary structure
592:regulatory element
578:and the initiator
1352:10.1159/000134145
1230:10.1021/bi992322p
1118:978-0-87969-568-2
547:molecular biology
534:protein synthesis
476:
475:
472:
471:
327:
326:
323:
322:
166:
165:
162:
161:
1794:
1762:
1761:
1751:
1741:
1709:
1703:
1702:
1692:
1668:
1662:
1661:
1651:
1615:
1609:
1608:
1598:
1588:
1556:
1550:
1549:
1539:
1516:The EMBO Journal
1507:
1501:
1500:
1490:
1458:
1452:
1451:
1441:
1405:
1399:
1398:
1370:
1364:
1363:
1335:
1326:
1325:
1297:
1291:
1290:
1280:
1248:
1242:
1241:
1213:
1207:
1206:
1196:
1172:
1166:
1165:
1129:
1123:
1122:
1104:
1098:
1097:
1061:
1055:
1054:
1044:
1020:
1014:
1013:
977:
971:
970:
942:
936:
935:
899:
893:
892:
864:
858:
857:
847:
837:
805:
799:
798:
792:
788:
786:
778:
744:
530:eukaryotic cells
445:
329:
296:
168:
135:
19:
1802:
1801:
1797:
1796:
1795:
1793:
1792:
1791:
1767:
1766:
1765:
1724:(30): 10460–5.
1711:
1710:
1706:
1670:
1669:
1665:
1617:
1616:
1612:
1571:(24): 13080–5.
1558:
1557:
1553:
1509:
1508:
1504:
1460:
1459:
1455:
1407:
1406:
1402:
1372:
1371:
1367:
1337:
1336:
1329:
1299:
1298:
1294:
1250:
1249:
1245:
1224:(19): 5758–65.
1215:
1214:
1210:
1174:
1173:
1169:
1131:
1130:
1126:
1119:
1106:
1105:
1101:
1063:
1062:
1058:
1035:(31): 29111–5.
1022:
1021:
1017:
979:
978:
974:
944:
943:
939:
901:
900:
896:
866:
865:
861:
807:
806:
802:
789:
779:
767:
746:
745:
741:
737:
710:
681:
665:eIF4A isoform I
661:
612:
596:gene expression
588:phosphorylation
572:ternary complex
568:
526:
17:
12:
11:
5:
1800:
1798:
1790:
1789:
1787:Human proteins
1784:
1779:
1769:
1768:
1764:
1763:
1704:
1683:(8): 5566–73.
1663:
1634:(9): 3008–19.
1610:
1551:
1522:(7): 2643–54.
1502:
1453:
1400:
1365:
1327:
1292:
1243:
1208:
1187:(3): 1872–81.
1167:
1124:
1117:
1099:
1056:
1015:
972:
937:
910:(10): 957–80.
894:
859:
820:(28): 9564–9.
800:
791:|journal=
765:
738:
736:
733:
732:
731:
726:
721:
716:
709:
706:
680:
677:
660:
657:
611:
608:
567:
564:
525:
522:
474:
473:
470:
469:
464:
460:
459:
454:
450:
449:
441:
440:
430:
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423:
419:
418:
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407:
406:
401:
395:
394:
389:
383:
382:
377:
371:
370:
365:
359:
358:
355:
351:
350:
345:
341:
340:
336:
335:
325:
324:
321:
320:
315:
311:
310:
305:
301:
300:
292:
291:
281:
275:
274:
269:
263:
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258:
257:
252:
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245:
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216:
210:
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198:
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184:
180:
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164:
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159:
154:
150:
149:
144:
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139:
131:
130:
120:
114:
113:
109:
108:
103:
97:
96:
91:
85:
84:
79:
73:
72:
67:
61:
60:
55:
49:
48:
45:
41:
40:
35:
31:
30:
26:
25:
16:Protein family
15:
13:
10:
9:
6:
4:
3:
2:
1799:
1788:
1785:
1783:
1780:
1778:
1775:
1774:
1772:
1759:
1755:
1750:
1745:
1740:
1735:
1731:
1727:
1723:
1719:
1715:
1708:
1705:
1700:
1696:
1691:
1686:
1682:
1678:
1674:
1667:
1664:
1659:
1655:
1650:
1645:
1641:
1637:
1633:
1629:
1625:
1621:
1614:
1611:
1606:
1602:
1597:
1592:
1587:
1582:
1578:
1574:
1570:
1566:
1562:
1555:
1552:
1547:
1543:
1538:
1533:
1529:
1525:
1521:
1517:
1513:
1506:
1503:
1498:
1494:
1489:
1484:
1480:
1476:
1473:(1): 272–80.
1472:
1468:
1464:
1457:
1454:
1449:
1445:
1440:
1435:
1431:
1427:
1423:
1419:
1415:
1411:
1404:
1401:
1396:
1392:
1388:
1384:
1381:(1): 339–44.
1380:
1376:
1369:
1366:
1361:
1357:
1353:
1349:
1345:
1341:
1334:
1332:
1328:
1323:
1319:
1315:
1311:
1308:(2): 248–50.
1307:
1303:
1296:
1293:
1288:
1284:
1279:
1274:
1270:
1266:
1262:
1258:
1254:
1247:
1244:
1239:
1235:
1231:
1227:
1223:
1219:
1212:
1209:
1204:
1200:
1195:
1190:
1186:
1182:
1178:
1171:
1168:
1163:
1159:
1155:
1151:
1147:
1143:
1139:
1135:
1128:
1125:
1120:
1114:
1110:
1103:
1100:
1095:
1091:
1087:
1083:
1079:
1075:
1072:(3): 318–56.
1071:
1067:
1060:
1057:
1052:
1048:
1043:
1038:
1034:
1030:
1026:
1019:
1016:
1011:
1007:
1003:
999:
995:
991:
988:(2): 183–91.
987:
983:
976:
973:
968:
964:
960:
956:
952:
948:
941:
938:
933:
929:
925:
921:
917:
913:
909:
905:
898:
895:
890:
886:
882:
878:
875:(1): 913–63.
874:
870:
863:
860:
855:
851:
846:
841:
836:
831:
827:
823:
819:
815:
811:
804:
801:
796:
784:
776:
772:
768:
766:9780125400725
762:
758:
754:
750:
743:
740:
734:
730:
727:
725:
724:Hippuristanol
722:
720:
717:
715:
712:
711:
707:
705:
702:
697:
695:
691:
686:
678:
676:
674:
670:
666:
658:
656:
654:
649:
645:
641:
637:
633:
629:
625:
621:
617:
609:
607:
605:
601:
597:
593:
589:
585:
581:
577:
573:
565:
563:
561:
557:
552:
548:
543:
539:
538:model systems
535:
531:
523:
521:
519:
515:
511:
508:
504:
500:
496:
492:
489:
485:
481:
468:
465:
461:
458:
455:
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446:
442:
439:
438:
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431:
429:
425:
420:
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408:
405:
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381:
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366:
364:
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356:
352:
349:
346:
342:
337:
334:
330:
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285:
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276:
273:
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268:
264:
259:
256:
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199:
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191:
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185:
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145:
141:
136:
132:
129:
128:
124:
121:
119:
115:
110:
107:
104:
102:
98:
95:
92:
90:
86:
83:
80:
78:
74:
71:
68:
66:
62:
59:
56:
54:
50:
46:
42:
39:
36:
32:
27:
24:
20:
1721:
1717:
1707:
1680:
1676:
1666:
1631:
1627:
1622:(May 2008).
1613:
1568:
1564:
1554:
1519:
1515:
1505:
1470:
1466:
1456:
1424:(2): 200–9.
1421:
1417:
1410:Rappsilber J
1403:
1378:
1374:
1368:
1346:(4): 385–8.
1343:
1339:
1305:
1301:
1295:
1260:
1256:
1246:
1221:
1218:Biochemistry
1217:
1211:
1184:
1180:
1170:
1140:(6): 463–7.
1137:
1133:
1127:
1108:
1102:
1069:
1065:
1059:
1032:
1028:
1018:
985:
981:
975:
953:(2): 381–8.
950:
946:
940:
907:
903:
897:
872:
868:
862:
817:
813:
803:
748:
742:
698:
693:
690:RNA splicing
682:
662:
643:
613:
569:
527:
483:
479:
477:
435:
354:Alt. symbols
286:
193:Alt. symbols
125:
44:Alt. symbols
1263:(8): 2012.
729:Rocaglamide
653:start codon
457:Swiss-model
339:Identifiers
308:Swiss-model
178:Identifiers
147:Swiss-model
29:Identifiers
1771:Categories
735:References
648:wheat germ
560:amino acid
542:sea urchin
524:Background
453:Structures
448:Search for
422:Other data
304:Structures
299:Search for
261:Other data
143:Structures
138:Search for
112:Other data
793:ignored (
783:cite book
610:Mechanism
514:helicases
510:ribosomal
404:NM_014740
363:NCBI gene
267:EC number
243:NM_001967
202:NCBI gene
94:NM_001416
53:NCBI gene
1758:16030146
1658:18316401
1620:Tiedge H
1605:11087862
1497:10590115
1448:14730019
1395:10623621
1302:Genomics
1238:10801326
1203:15528191
1162:12434586
1094:19804795
1086:13718526
1051:11408474
1010:24826675
932:10737331
924:12462398
889:10872469
854:18606994
775:12206455
708:See also
685:DEAD box
679:Proteins
566:Function
556:ribosome
488:proteins
467:InterPro
318:InterPro
157:InterPro
1749:1176247
1726:Bibcode
1699:8449919
1649:2293081
1573:Bibcode
1546:1378397
1439:1370532
1360:8521730
1322:9790779
1287:8493113
1154:9187654
1002:6865504
967:5814313
845:2474498
822:Bibcode
463:Domains
433:Chr. 17
411:UniProt
314:Domains
272:3.6.1.1
250:UniProt
153:Domains
123:Chr. 17
101:UniProt
1756:
1746:
1697:
1656:
1646:
1603:
1593:
1544:
1537:556740
1534:
1495:
1488:111537
1485:
1446:
1436:
1393:
1358:
1320:
1285:
1278:309447
1275:
1236:
1201:
1160:
1152:
1115:
1092:
1084:
1049:
1008:
1000:
965:
930:
922:
887:
852:
842:
773:
763:
694:et al.
644:et al.
499:EIF4A3
497:, and
495:EIF4A2
491:EIF4A1
416:P38919
399:RefSeq
392:608546
348:EIF4A3
344:Symbol
284:Chr. 3
255:Q14240
238:RefSeq
231:601102
187:EIF4A2
183:Symbol
106:P60842
89:RefSeq
82:602641
38:EIF4A1
34:Symbol
1596:27181
1158:S2CID
1090:S2CID
1006:S2CID
928:S2CID
701:eIF4F
659:Genes
640:eIF4H
636:eIF4B
632:eIF4F
628:eIF4E
616:eIF4F
604:eIF4F
574:with
484:eIF4A
437:q25.3
428:Locus
380:18683
357:DDX48
279:Locus
196:EIF4F
118:Locus
47:EIF4A
1754:PMID
1695:PMID
1654:PMID
1601:PMID
1542:PMID
1493:PMID
1444:PMID
1391:PMID
1356:PMID
1318:PMID
1283:PMID
1234:PMID
1199:PMID
1150:PMID
1113:ISBN
1082:PMID
1047:PMID
998:PMID
963:PMID
920:PMID
885:PMID
850:PMID
795:help
771:PMID
761:ISBN
671:and
624:eIF3
584:tRNA
503:mRNA
478:The
387:OMIM
375:HGNC
368:9775
226:OMIM
219:3284
214:HGNC
207:1974
77:OMIM
70:3282
65:HGNC
58:1973
1744:PMC
1734:doi
1722:102
1685:doi
1681:268
1644:PMC
1636:doi
1591:PMC
1581:doi
1532:PMC
1524:doi
1483:PMC
1475:doi
1434:PMC
1426:doi
1418:RNA
1383:doi
1379:267
1348:doi
1310:doi
1273:PMC
1265:doi
1226:doi
1189:doi
1185:280
1142:doi
1074:doi
1037:doi
1033:276
990:doi
955:doi
951:179
912:doi
877:doi
840:PMC
830:doi
818:105
753:doi
673:III
646:in
620:40S
580:Met
576:GTP
518:RNA
507:40S
505:to
288:q28
127:p13
1773::
1752:.
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1732:.
1720:.
1716:.
1693:.
1679:.
1675:.
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1642:.
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1630:.
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1569:97
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1563:.
1540:.
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1518:.
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1491:.
1481:.
1471:74
1469:.
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1420:.
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482:(
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