197:
mature protein. The free signal peptides are then digested by specific proteases. Moreover, different target locations are aimed by different types of signal peptides. For example, the structure of a target peptide aiming for the mitochondrial environment differs in terms of length and shows an alternating pattern of small positively charged and hydrophobic stretches. Nucleus aiming signal peptides can be found at both the N-terminus and the C-terminus of a protein and are in most cases retained in the mature protein.
313:
transcription or translation of the main protein, and are not part of the final protein sequence. This type of leader peptide primarily refers to a form of gene regulation found in bacteria, although a similar mechanism is used to regulate eukaryotic genes, which is referred to as uORFs (upstream open reading frames).
227:, which is present on the surface of either the plasma membrane (in prokaryotes) or the ER (in eukaryotes). Once membrane-targeting is completed, the signal sequence is inserted into the translocon. Ribosomes are then physically docked onto the cytoplasmic face of the translocon and protein synthesis resumes.
196:
and therefore named cleavage site. This cleavage site is absent from transmembrane-domains that serve as signal peptides, which are sometimes referred to as signal anchor sequences. Signal peptidase may cleave either during or after completion of translocation to generate a free signal peptide and a
270:
that codes for the signal peptide (i.e. the signal sequence coding region, or SSCR) can function as an RNA element with specific activities. SSCRs promote nuclear mRNA export and the proper localization to the surface of the endoplasmic reticulum. In addition SSCRs have specific sequence features:
183:
The core of the signal peptide contains a long stretch of hydrophobic amino acids (about 5–16 residues long) that has a tendency to form a single alpha-helix and is also referred to as the "h-region". In addition, many signal peptides begin with a short positively charged stretch of amino acids,
312:
Signal peptides are not to be confused with the leader peptides sometimes encoded by leader mRNA, although both are sometimes ambiguously referred to as "leader peptides." These other leader peptides are short polypeptides that do not function in protein localization, but instead may regulate
303:
Signal peptides are usually located at the N-terminus of proteins. Some have C-terminal or internal signal peptides (examples: peroxisomal targeting signal and nuclear localisation signal). The structure of these nonclassical signal peptides differs vastly from the N-terminal signal peptides.
241:
ATPase, which in turn pumps the protein through the translocon. Although post-translational translocation is known to occur in eukaryotes, it is poorly understood. It is known that in yeast post-translational translocation requires the translocon and two additional membrane-bound proteins,
171:, where the signal peptide directs the newly synthesized protein to the Sec61 channel, which shares structural and sequence homology with SecYEG, but is present in the endoplasmic reticulum. Both the SecYEG and Sec61 channels are commonly referred to as the
175:, and transit through this channel is known as translocation. While secreted proteins are threaded through the channel, transmembrane domains may diffuse across a lateral gate in the translocon to partition into the surrounding membrane.
593:
291:
Proteins without signal peptides can also be secreted by unconventional mechanisms. E.g. Interleukin, Galectin. The process by which such secretory proteins gain access to the cell exterior is termed
740:
Görlich D, Prehn S, Hartmann E, Kalies KU, Rapoport TA (October 1992). "A mammalian homolog of SEC61p and SECYp is associated with ribosomes and nascent polypeptides during translocation".
258:
Signal peptides are extremely heterogeneous, many prokaryotic and eukaryotic ones are functionally interchangeable within or between species and all determine protein secretion efficiency.
371:
Owji, Hajar; Nezafat, Navid; Negahdaripour, Manica; Hajiebrahimi, Ali; Ghasemi, Younes (August 2018). "A comprehensive review of signal peptides: Structure, roles, and applications".
416:"Transfer of proteins across membranes. I. Presence of proteolytically processed and unprocessed nascent immunoglobulin light chains on membrane-bound ribosomes of murine myeloma"
230:
The post-translational pathway is initiated after protein synthesis is completed. In prokaryotes, the signal sequence of post-translational substrates is recognized by the
644:"Translocation of proteins across the endoplasmic reticulum. I. Signal recognition protein (SRP) binds to in-vitro-assembled polysomes synthesizing secretory protein"
1204:
2008:
1457:
915:"Comparison of secretory signal peptides for heterologous protein expression in microalgae: Expanding the secretion portfolio for Chlamydomonas reinhardtii"
223:(SRP). SRP then halts further translation (translational arrest only occurs in Eukaryotes) and directs the signal sequence-ribosome-mRNA complex to the
693:"Protein translocation across the endoplasmic reticulum. I. Detection in the microsomal membrane of a receptor for the signal recognition particle"
47:
35:
1867:
192:
it is called the "n-region". At the end of the signal peptide there is typically a stretch of amino acids that is recognized and cleaved by
1197:
618:
1756:
1751:
1726:
1716:
1711:
1701:
1772:
1706:
1190:
463:
Rapoport TA (November 2007). "Protein translocation across the eukaryotic endoplasmic reticulum and bacterial plasma membranes".
2003:
1802:
1109:
Agrawal GK, Jwa NS, Lebrun MH, Job D, Rakwal R (February 2010). "Plant secretome: unlocking secrets of the secreted proteins".
231:
832:
Kober L, Zehe C, Bode J (April 2013). "Optimized signal peptides for the development of high expressing CHO cell lines".
163:, signal peptides direct the newly synthesized protein to the SecYEG protein-conducting channel, which is present in the
136:
129:
2020:
1179:— predicts the presence and location of signal peptide cleavage sites in amino acid sequences from different organisms.
1025:"Genome analysis reveals interplay between 5'UTR introns and nuclear mRNA export for secretory and mitochondrial genes"
1074:
Nickel W, Seedorf M (2008). "Unconventional mechanisms of protein transport to the cell surface of eukaryotic cells".
514:
Käll L, Krogh A, Sonnhammer EL (May 2004). "A combined transmembrane topology and signal peptide prediction method".
292:
1213:
1167:
1413:
785:"Posttranslational protein transport in yeast reconstituted with a purified complex of Sec proteins and Kar2p"
1626:
156:
184:
which may help to enforce proper topology of the polypeptide during translocation by what is known as the
1571:
220:
212:
In both prokaryotes and eukaryotes signal sequences may act co-translationally or post-translationally.
2050:
1023:
Cenik C, Chua HN, Zhang H, Tarnawsky SP, Akef A, Derti A, et al. (April 2011). Snyder M (ed.).
143:, which biochemically resembles a signal sequence except that it is not cleaved. They are a kind of
2045:
1511:
1158:
1836:
139:
and multi-spanning membrane-bound proteins are targeted to the secretory pathway by their first
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1087:
132:
117:
926:
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8:
1221:
930:
476:
351:
Kapp, Katja; Schrempf, Sabrina; Lemberg, Marius K.; Dobberstein, Bernhard (2013-01-01).
200:
It is possible to determine the amino acid sequence of the N-terminal signal peptide by
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The co-translational pathway is initiated when the signal peptide emerges from the
193:
128:), secreted from the cell, or inserted into most cellular membranes. Although most
861:
52:
1226:
1182:
1171:
1041:
990:
972:
Palazzo AF, Springer M, Shibata Y, Lee CS, Dias AP, Rapoport TA (December 2007).
939:
164:
121:
116:. These proteins include those that reside either inside certain organelles (the
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384:
327:
276:
144:
105:
101:
527:
352:
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1906:
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659:
449:
431:
160:
484:
1812:
1240:
189:
172:
168:
97:
1164:
845:
295:(UPS). In plants, even 50% of secreted proteins can be UPS dependent.
1560:
1506:
204:, a cyclic procedure that cleaves off the amino acids one at a time.
125:
370:
1840:
1473:
1465:
974:"The signal sequence coding region promotes nuclear export of mRNA"
783:
Panzner S, Dreier L, Hartmann E, Kostka S, Rapoport TA (May 1995).
216:
109:
1591:
1478:
1438:
1369:
1364:
1359:
1354:
1349:
1304:
272:
93:
16:
Short peptide present at N-terminal of newly synthesized proteins
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782:
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267:
238:
878:(July 1985). "Signal sequences. The limits of variation".
739:
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912:
208:
Co-translational versus post-translational translocation
1022:
913:
Molino JV, de
Carvalho JC, Mayfield SP (2018-02-06).
253:
641:
1108:
965:
690:
619:"N-terminal sequencing service - Edman degradation"
513:
1212:
159:the protein, usually to the cellular membrane. In
554:"Topogenic signals in integral membrane proteins"
413:
286:
2037:
642:Walter P, Ibrahimi I, Blobel G (November 1981).
594:"26.6 Peptide Sequencing: The Edman Degradation"
1076:Annual Review of Cell and Developmental Biology
691:Gilmore R, Blobel G, Walter P (November 1982).
548:
542:
1198:
1073:
831:
283:at a frequency that is higher than expected.
155:Signal peptides function to prompt a cell to
825:
261:
868:
776:
354:Post-Targeting Functions of Signal Peptides
150:
1205:
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874:
1157:at the U.S. National Library of Medicine
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1040:
1016:
999:
989:
948:
938:
800:
716:
667:
569:
439:
414:Blobel G, Dobberstein B (December 1975).
298:
108:or internally) of most newly synthesized
1088:10.1146/annurev.cellbio.24.110707.175320
462:
188:. Because of its close location to the
104:(or occasionally nonclassically at the
2038:
279:, and tend to be present in the first
1186:
366:
364:
13:
2021:Prokaryotic ubiquitin-like protein
571:10.1111/j.1432-1033.1988.tb14150.x
275:-content, are enriched in certain
266:In vertebrates, the region of the
254:Secretion efficiency determination
237:that transfers the protein to the
14:
2062:
1148:
361:
834:Biotechnology and Bioengineering
558:European Journal of Biochemistry
373:European Journal of Cell Biology
293:unconventional protein secretion
167:. A homologous system exists in
1102:
1067:
906:
733:
684:
307:
1551:Mitochondrial targeting signal
1214:Posttranslational modification
1165:SPdb (Signal Peptide DataBase)
635:
611:
586:
507:
456:
407:
344:
287:Alternate secretion mechanisms
1:
338:
112:that are destined toward the
1627:Ubiquitin-conjugating enzyme
1042:10.1371/journal.pgen.1001366
991:10.1371/journal.pbio.0050322
940:10.1371/journal.pone.0192433
892:10.1016/0022-2836(85)90046-4
880:Journal of Molecular Biology
802:10.1016/0092-8674(95)90077-2
754:10.1016/0092-8674(92)90517-G
516:Journal of Molecular Biology
178:
7:
1915:E2 SUMO-conjugating enzyme
1572:Ubiquitin-activating enzyme
697:The Journal of Cell Biology
648:The Journal of Cell Biology
420:The Journal of Cell Biology
316:
221:signal-recognition particle
135:have signal peptides, most
10:
2067:
1898:E1 SUMO-activating enzyme
385:10.1016/j.ejcb.2018.06.003
64:(sometimes referred to as
1956:
1887:
1876:
1559:
1536:
1494:
1234:
1220:
528:10.1016/j.jmb.2004.03.016
262:Nucleotide level features
219:and is recognized by the
46:
34:
26:
21:
1512:Survival of motor neuron
1159:Medical Subject Headings
151:Function (translocation)
1878:Ubiquitin-like proteins
1837:Deubiquitinating enzyme
552:, Gavel Y (July 1988).
133:membrane-bound proteins
1123:10.1002/pmic.200900514
299:Nonclassical sequences
118:endoplasmic reticulum
100:long) present at the
78:localization sequence
709:10.1083/jcb.95.2.463
660:10.1083/jcb.91.2.545
598:Chemistry LibreTexts
432:10.1083/jcb.67.3.835
357:. Landes Bioscience.
186:positive-inside rule
141:transmembrane domain
1236:Heat shock proteins
931:2018PLoSO..1392433M
485:10.1038/nature06384
477:2007Natur.450..663R
74:localization signal
1170:2016-01-22 at the
654:(2 Pt 1): 545–50.
333:Topogenic sequence
2051:Protein targeting
2033:
2032:
2029:
2028:
1538:Protein targeting
1532:
1531:
846:10.1002/bit.24776
703:(2 Pt 1): 463–9.
623:www.alphalyse.com
323:Protein targeting
235:chaperone protein
202:Edman degradation
114:secretory pathway
58:
57:
2058:
1885:
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1798:Ubiquitin ligase
1564:(ubiquitylation)
1502:Alpha crystallin
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70:targeting signal
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2046:Gene expression
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1927:E3 SUMO ligase
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1172:Wayback Machine
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1035:(4): e1001366.
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471:(7170): 663–9.
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165:plasma membrane
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96:(usually 16-30
86:leader sequence
82:transit peptide
66:signal sequence
62:signal peptide
36:OPM superfamily
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1155:Signal+Peptide
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1149:External links
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1117:(4): 799–827.
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840:(4): 1164–73.
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1400:
1397:
1395:
1392:
1390:
1387:
1385:
1382:
1381:
1380:
1377:
1376:
1371:
1368:
1366:
1363:
1361:
1358:
1356:
1353:
1351:
1348:
1346:
1343:
1341:
1338:
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1333:
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1328:
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1298:
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1278:
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1262:
1260:
1257:
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1247:
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1242:
1237:
1233:
1230:
1228:
1223:
1219:
1215:
1208:
1203:
1201:
1196:
1194:
1189:
1188:
1185:
1178:
1175:
1173:
1169:
1166:
1163:
1160:
1156:
1153:
1152:
1140:
1136:
1132:
1128:
1124:
1120:
1116:
1112:
1105:
1097:
1093:
1089:
1085:
1081:
1077:
1070:
1062:
1058:
1053:
1048:
1043:
1038:
1034:
1030:
1029:PLOS Genetics
1026:
1019:
1011:
1007:
1002:
997:
992:
987:
983:
979:
975:
968:
960:
956:
951:
946:
941:
936:
932:
928:
924:
920:
916:
909:
901:
897:
893:
889:
886:(1): 99–105.
885:
881:
877:
871:
863:
859:
855:
851:
847:
843:
839:
835:
828:
820:
816:
812:
808:
803:
798:
795:(4): 561–70.
794:
790:
786:
779:
771:
767:
763:
759:
755:
751:
747:
743:
736:
728:
724:
719:
714:
710:
706:
702:
698:
694:
687:
679:
675:
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638:
624:
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614:
599:
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589:
581:
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572:
567:
563:
559:
555:
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545:
537:
533:
529:
525:
521:
517:
510:
502:
498:
494:
490:
486:
482:
478:
474:
470:
466:
459:
451:
447:
442:
437:
433:
429:
426:(3): 835–51.
425:
421:
417:
410:
402:
398:
394:
390:
386:
382:
378:
374:
367:
365:
356:
355:
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205:
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138:
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123:
119:
115:
111:
107:
103:
99:
95:
92:) is a short
91:
87:
83:
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75:
71:
67:
63:
54:
51:
49:
45:
42:
39:
37:
33:
29:
25:
20:
1889:SUMO protein
1545:
1114:
1110:
1104:
1079:
1075:
1069:
1032:
1028:
1018:
984:(12): e322.
981:
978:PLOS Biology
977:
967:
922:
918:
908:
883:
879:
876:von Heijne G
870:
837:
833:
827:
792:
788:
778:
745:
741:
735:
700:
696:
686:
651:
647:
637:
626:. Retrieved
622:
613:
602:. Retrieved
600:. 2015-08-26
597:
588:
564:(4): 671–8.
561:
557:
550:von Heijne G
544:
519:
515:
509:
468:
464:
458:
423:
419:
409:
376:
372:
353:
346:
311:
308:Nomenclature
302:
290:
265:
257:
229:
225:SRP receptor
214:
211:
199:
185:
182:
154:
89:
85:
81:
77:
73:
69:
65:
61:
59:
1983:neddylation
1249:Hsp10/GroES
1241:Chaperonins
1082:: 287–308.
161:prokaryotes
157:translocate
98:amino acids
48:OPM protein
22:Identifiers
2040:Categories
1275:Hsp40/DnaJ
1222:Chaperones
1111:Proteomics
628:2018-09-27
604:2018-09-27
339:References
190:N-terminus
173:translocon
169:eukaryotes
106:C-terminus
102:N-terminus
1561:Ubiquitin
1507:Clusterin
179:Structure
126:endosomes
1841:Ataxin 3
1168:Archived
1139:20647387
1131:19953550
1096:18590485
1061:21533221
1010:18052610
959:29408937
919:PLOS ONE
854:23124363
819:14398668
770:19078317
536:15111065
493:18046402
401:49612506
393:29958716
317:See also
217:ribosome
110:proteins
1764:(CDC34)
1177:SignalP
1052:3077370
1001:2100149
950:5800701
927:Bibcode
900:4032478
811:7758110
762:1423609
727:6292235
718:2112970
678:7309795
669:2111968
580:3134198
501:2497138
473:Bibcode
441:2111658
273:adenine
137:type II
94:peptide
1808:Cullin
1161:(MeSH)
1137:
1129:
1094:
1059:
1049:
1008:
998:
957:
947:
898:
862:449870
860:
852:
817:
809:
768:
760:
725:
715:
676:
666:
578:
534:
499:
491:
465:Nature
450:811671
448:
438:
399:
391:
277:motifs
130:type I
27:Symbol
1999:ATG12
1989:FAT10
1979:NEDD8
1964:ISG15
1957:Other
1946:PIAS4
1941:PIAS3
1936:PIAS2
1931:PIAS1
1881:(UBL)
1863:BIRC6
1823:FANCL
1495:Other
1484:TRAP1
1453:Hsp90
1379:Hsp70
1268:GroEL
1264:HSP60
1259:Hsp47
1254:Hsp27
1135:S2CID
858:S2CID
815:S2CID
766:S2CID
497:S2CID
397:S2CID
248:Sec63
244:Sec62
122:Golgi
2014:UBL5
2004:FUB1
1994:ATG8
1974:UFM1
1969:URM1
1919:UBC9
1907:SAE2
1902:SAE1
1868:UFC1
1858:ATG3
1851:CYLD
1846:USP6
1828:UBR1
1818:MDM2
1617:SAE1
1612:NAE1
1607:ATG7
1602:UBA7
1597:UBA6
1592:UBA5
1587:UBA3
1582:UBA2
1577:UBA1
1522:SMN2
1517:SMN1
1127:PMID
1092:PMID
1057:PMID
1006:PMID
955:PMID
896:PMID
850:PMID
807:PMID
789:Cell
758:PMID
742:Cell
723:PMID
674:PMID
576:PMID
532:PMID
489:PMID
446:PMID
389:PMID
281:exon
268:mRNA
246:and
239:SecA
232:SecB
53:1skh
2009:MUB
1813:CBL
1803:VHL
1796:E3
1625:E2
1570:E1
1439:12A
1370:C19
1365:C14
1360:C13
1355:C11
1350:C10
1305:B11
1119:doi
1084:doi
1047:PMC
1037:doi
996:PMC
986:doi
945:PMC
935:doi
888:doi
884:184
842:doi
838:110
797:doi
750:doi
713:PMC
705:doi
664:PMC
656:doi
566:doi
562:174
524:doi
520:338
481:doi
469:450
436:PMC
428:doi
381:doi
124:or
88:or
41:256
30:N/A
2042::
1839::
1783:V2
1778:V1
1768:R2
1762:R1
1757:Q2
1752:Q1
1732:L6
1727:L4
1722:L3
1717:L2
1712:L1
1702:J2
1697:J1
1682:G2
1677:G1
1672:E3
1667:E2
1662:E1
1657:D3
1652:D2
1647:D1
1479:ER
1444:14
1409:4L
1394:1L
1389:1B
1384:1A
1345:C7
1340:C6
1335:C5
1330:C3
1325:C1
1320:B9
1315:B6
1310:B4
1300:B2
1295:B1
1290:A3
1285:A2
1280:A1
1133:.
1125:.
1115:10
1113:.
1090:.
1080:24
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1031:.
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1004:.
994:.
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953:.
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917:.
894:.
882:.
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813:.
805:.
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787:.
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721:.
711:.
701:95
699:.
695:.
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662:.
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560:.
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530:.
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377:97
375:.
363:^
250:.
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120:,
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60:A
1985:)
1981:(
1788:Z
1773:S
1747:O
1742:N
1737:M
1707:K
1692:I
1687:H
1642:C
1637:B
1632:A
1474:β
1468:2
1466:α
1460:1
1458:α
1434:9
1429:8
1424:7
1419:6
1414:5
1404:4
1399:2
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1238:/
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