279:
electrons from one reaction to another; the coenzyme exists in two forms: NAD+ (oxidized form) and NADH (reduced form), so that NAD plays a role in the production of energy through the electron transport chain, as well as in the synthesis of nucleic acids. In context of 3α-hydroxysteroid dehydrogenase enzymes, the notion that these enzymes are NAD±specific mean that they require NAD in either its oxidized or reduced form to function properly; still, the activity of these enzymes is almost exclusively oxidative in intact mammalian cells, relying on NAD as a coenzyme for their action, whereas in other (non-mammalian) organisms it can be in reduced form. In humans, the genes for the protein isoforms of the 3α-hydroxysteroid dehydrogenase enzyme share a common gene structure that is characteristic of the
421:(3α-, 3β-, 11β-, 17β-, 20α-, and 20β-positions of the stroid nucleus), and also play a dual role in both the synthesis and deactivation of steroids, and some also participate in the metabolism of a range of non-steroidal molecules. Within target tissues, these dehydrogenases transform inactive steroid hormones into their active counterparts and vice versa, so that these reactions regulates the activation of steroid hormone receptors and influences non-genomic signaling pathways; as such,3α-hydroxysteroid dehydrogenases serve as regulators, enabling the pre-receptor modulation of steroid hormone activities in these organisms.
405:
1328:
1771:
204:(3α-HSD) is an enzyme (1.1.1.50) that plays a role in the metabolism of steroids and non-steroidal compounds in humans and other species, such as bacteria, fungi, plants, and so on. This enzyme catalyzes the chemical reaction of conversion of 3-ketosteroids into 3α-hydroxysteroids. The enzyme has various
420:
In non-human species, 3α-hydroxysteroid dehydrogenases contribute to steroidogenesis as part of the NADPH/NAD±dependent oxidoreductase family; so that these enzymes facilitate the conversion between ketones and their corresponding secondary alcohols across various positions on steroidal substrates
646:
Lee, Hyoung Jae; Nakayasu, Masaru; Akiyama, Ryota; Kobayashi, Midori; Miyachi, Haruka; Sugimoto, Yukihiro; Umemoto, Naoyuki; Saito, Kazuki; Muranaka, Toshiya; Mizutani, Masaharu (March 20, 2019). "Identification of a 3β-Hydroxysteroid
Dehydrogenase/ 3-Ketosteroid Reductase Involved in α-Tomatine
278:
enzymes are almost exclusively oxidative in intact mammalian cells and are nicotinamide adenine dinucleotide (NAD)±specific. NAD is a coenzyme found in all living cells and is required for the metabolic processes that make life possible; specifically, NAD is involved in redox reactions, carrying
849:
Steckelbroeck, Stephan; Watzka, Mathias; Reichelt, Robert; Hans, Volkmar H. J.; Stoffel-Wagner, Birgit; Heidrich, Dagmar D.; Schramm, Johannes; Bidlingmaier, Frank; Klingmüller, Dietrich (March 1, 2001). "Characterization of the 5α-Reductase-3α-Hydroxysteroid
Dehydrogenase Complex in the Human
774:
Matsuura, K.; Shiraishi, H.; Hara, A.; Sato, K.; Deyashiki, Y.; Ninomiya, M.; Sakai, S. (November 1, 1998). "Identification of a
Principal mRNA Species for Human 3 -Hydroxysteroid Dehydrogenase Isoform (AKR1C3) That Exhibits High Prostaglandin D2 11-Ketoreductase Activity".
735:
Ghosh, Debashis; Wawrzak, Zdzislaw; Weeks, Charles M.; Duax, William L.; Erman, Mary (1994). "The refined three-dimensional structure of 3α,20β-hydroxysteroid dehydrogenase and possible roles of the residues conserved in short-chain dehydrogenases".
813:
RižNer, Tea Lanišnik; Lin, Hsueh K.; Peehl, Donna M.; Steckelbroeck, Stephan; Bauman, David R.; Penning, Trevor M. (2003). "Human Type 3 3α-Hydroxysteroid
Dehydrogenase (Aldo-Keto Reductase 1C2) and Androgen Metabolism in Prostate Cells".
887:"Human 3α-hydroxysteroid dehydrogenase isoforms (AKR1C1‒AKR1C4) of the aldo-keto reductase superfamily: Functional plasticity and tissue distribution reveals roles in the inactivation and formation of male and female sex hormones"
364:, also known as 3α-androstanediol, and abbreviated as 3α-diol. The activity of this enzyme towards 3α-diol is important not only in the conventional pathways of androgen biosynthesis, but also in the
274:
fractions of rat and human tissues, the membrane-bound proteins which are members of the short-chain dehydrogenase/reductase family. The 3α-hydroxysteroid dehydrogenase activities of these
352:
Regardless of a particular isoform, the 3α-hydroxysteroid dehydrogenase enzyme in humans is known to be necessary for the synthesis of many important endogenous neurosteroids, such as
1121:
Wollam, Joshua; Magner, Daniel B.; Magomedova, Lilia; Rass, Elisabeth; Shen, Yidong; Rottiers, Veerle; Habermann, Bianca; Cummins, Carolyn L.; Antebi, Adam (April 10, 2012).
220:
In humans, 3α-hydroxysteroid dehydrogenase is encoded by the multiple different genes, so that each gene encodes a particular isoform. The most studied isoforms are type 1 (
1086:
Dufort, Isabelle; Labrie, Fernand; Luu-The, Van (February 1, 2001). "Human Types 1 and 3 3α-Hydroxysteroid
Dehydrogenases: Differential Lability and Tissue Distribution1".
1221:
Saleem, Noor; Aziz, Usman; Ali, Muhammad; Liu, Xiangling; Alwutayd, Khairiah
Mubarak; Alshegaihi, Rana M.; Niedbała, Gniewko; Elkelish, Amr; Zhang, Meng (June 15, 2023).
165:
885:
Penning, Trevor M.; Burczynski, Michael E.; Jez, Joseph M.; Hung, Chien-Fu; Lin, Hseuh-Kung; Ma, Haiching; Moore, Margaret; Palackal, Nisha; Ratnam, Kapila (2000).
506:
Kisiela, Michael; Skarka, Adam; Ebert, Bettina; Maser, Edmund (August 22, 2011). "Hydroxysteroid dehydrogenases (HSDS) in bacteria – A bioinformatic perspective".
1309:
246:; although these isoforms are highly similar in their sequence, they exhibit unique reactivity profiles. Albeit other isoforms may also exists in humans; still,
184:
951:
242:
and common properties. They are monomeric soluble proteins consisting of about 320 amino acid residues with molecular weights about 34±37
331:
481:
361:
1490:
177:
1223:"Genome-wide analysis revealed the stepwise origin and functional diversification of HSDS from lower to higher plant species"
448:
144:
120:
1646:
357:
1761:
412:, a prototypical steroid with 32 carbon atoms. Its core ring system (ABCD), composed of 17 carbon atoms, is shown with
1432:"IUPAC-IUB Joint Commission on Biochemical Nomenclature (JCBN). The nomenclature of steroids. Recommendations 1989".
592:
Song, Peng; Zhang, Xue; Feng, Wei; Xu, Wei; Wu, Chaoyun; Xie, Shaoqing; Yu, Sisi; Fu, Rongzhao (February 24, 2023).
262:) is more widely expressed and is found, besides the liver, also in the adrenal glads, testis, brain, prostate, and
723:
human types 1 and 3 3α-HSD, 20α-HSD, and type 5 17β-HSD were named AKR1C4, AKR1C2, AKR1C1, and AKR1C3, respectively
1631:
1747:
1734:
1721:
1708:
1695:
1682:
1669:
369:
365:
1641:
368:. An important emzyme activity in humans is the transformation of the one of the most potent natural androgens,
138:
1595:
1538:
43:
376:. This enzyme in humans, in its various protein isoforms, are also known to be involved in the metabolism of
125:
1543:
478:"Information on EC 1.1.1.50 - 3alpha-hydroxysteroid 3-dehydrogenase (Si-specific) - BRENDA Enzyme Database"
408:
The carbon atom numbering in a hypothetical steroid nucleus can be demonstrated by a structure of 24-ethyl-
693:"Human types 1 and 3 3 alpha-hydroxysteroid dehydrogenases: differential lability and tissue distribution"
967:
Degtiar, W. G.; Kushlinsky, N. E. (2001). "3α-Hydroxysteroid
Dehydrogenase in Animal and Human Tissues".
189:
1564:
1483:
275:
267:
113:
1636:
1276:
1600:
280:
141:
404:
65:
1533:
1301:
1458:
3S-1.1. Numbering and ring letters. Steroids are numbered and rings are lettered as in formula 1
17:
1791:
1449:
1414:
1363:
1254:
1203:
1154:
1123:"A Novel 3-Hydroxysteroid Dehydrogenase That Regulates Reproductive Development and Longevity"
1103:
1068:
1019:
984:
947:
916:
867:
831:
792:
753:
714:
664:
625:
574:
523:
373:
239:
132:
396:, thus playing a role in the control of a series of active steroid levels in target tissues.
1579:
1574:
1548:
1476:
1441:
1404:
1394:
1355:
1291:
1244:
1234:
1193:
1185:
1144:
1134:
1095:
1058:
1050:
1011:
976:
939:
906:
898:
859:
823:
784:
745:
704:
656:
615:
605:
564:
554:
515:
353:
477:
101:
1626:
1610:
1523:
1332:
1327:
788:
205:
77:
1331: This article incorporates text from this source, which is available under the
1249:
1222:
48:
1775:
1664:
1605:
1445:
1409:
1382:
1198:
1174:"Structural and Functional Biology of Aldo-Keto Reductase Steroid-Transforming Enzymes"
1173:
1149:
1122:
1063:
1038:
911:
886:
620:
593:
569:
542:
377:
247:
160:
749:
266:
keratinocytes. The 3α-hydroxysteroid dehydrogenase activity has also been detected in
1785:
1569:
1528:
1305:
385:
1172:
Penning, Trevor M.; Wangtrakuldee, Phumvadee; Auchus, Richard J. (August 20, 2018).
1518:
938:. Advances in Experimental Medicine and Biology. Vol. 414. pp. 475–490.
559:
444:
1399:
1139:
943:
1742:
1677:
1513:
902:
519:
330:
aldo-keto reductase family 1 member C3; 3α-hydroxysteroid dehydrogenase type 2;
243:
1770:
1383:"The "backdoor pathway" of androgen synthesis in human male sexual development"
1054:
610:
346:
aldo-keto reductase family 1 member C4; 3α-hydroxysteroid dehydrogenase type 1
318:
aldo-keto reductase family 1 member C2; 3α-hydroxysteroid dehydrogenase type 3
1359:
1239:
980:
393:
381:
1716:
1690:
1296:
1015:
409:
389:
271:
1418:
1367:
1258:
1207:
1158:
1107:
1099:
1072:
1023:
988:
920:
871:
863:
835:
718:
709:
692:
668:
629:
578:
527:
372:
into 3α-diol, a compound having much lower biological activity towards the
283:
family members and contain at least nine conserved exon-intron boundaries.
1453:
1346:
Auchus, Richard J. (2004). "The backdoor pathway to dihydrotestosterone".
1189:
796:
757:
1002:
Verdin, Eric (2015). "NAD in aging, metabolism, and neurodegeneration".
827:
660:
306:
aldo-keto reductase family 1 member C1; 20α-hydroxysteroid dehydrogenase
89:
209:
108:
1729:
1499:
340:
324:
312:
300:
258:
252:
234:
228:
222:
172:
84:
72:
60:
1703:
413:
403:
263:
96:
1472:
543:"Microbial Hydroxysteroid Dehydrogenases: From Alpha to Omega"
1039:"NAD+ metabolism, stemness, the immune response, and cancer"
934:
472:
470:
468:
466:
1468:
936:
Enzymology and
Molecular Biology of Carbonyl Metabolism 6
508:
The
Journal of Steroid Biochemistry and Molecular Biology
256:) is expressed exclusively in the liver, whereas type 3 (
1381:
Miller, Walter L.; Auchus, Richard J. (April 3, 2019).
1088:
The Journal of Clinical Endocrinology & Metabolism
852:
The Journal of Clinical Endocrinology & Metabolism
1759:
1037:
Navas, Lola E.; Carnero, Amancio (January 1, 2021).
1655:
1619:
1588:
1557:
1506:
416:-approved ring lettering and carbon atom numbering.
183:
171:
159:
154:
131:
119:
107:
95:
83:
71:
59:
54:
42:
37:
32:
1275:Masiutin, Maxim; Yadav, Maneesh (April 3, 2023).
238:). Each of these isoforms shares higher than 70%
1270:
1268:
439:
437:
435:
433:
400:3α-Hydroxysteroid dehydrogenase in other species
808:
806:
691:Dufort I, Labrie F, Luu-The V (February 2001).
686:
684:
682:
680:
678:
641:
639:
594:"Biological synthesis of ursodeoxycholic acid"
501:
499:
250:analysis indicates that human type 1 isozyme (
1484:
769:
767:
8:
1491:
1477:
1469:
151:
1408:
1398:
1295:
1248:
1238:
1197:
1148:
1138:
1062:
910:
708:
619:
609:
568:
558:
541:Doden HL, Ridlon JM (February 24, 2021).
216:3α-Hydroxysteroid dehydrogenase in humans
1348:Trends in Endocrinology & Metabolism
1043:Signal Transduction and Targeted Therapy
285:
1766:
429:
29:
1315:from the original on October 24, 2023
789:10.1093/oxfordjournals.jbchem.a022211
7:
1446:10.1111/j.1432-1033.1989.tb15228.x
484:from the original on April 4, 2023
451:from the original on April 5, 2023
25:
1769:
1326:
332:17β-hydroxysteroid dehydrogenase
18:3α-hydroxysteroid oxidoreductase
1277:"Alternative androgen pathways"
202:3α-Hydroxysteroid dehydrogenase
33:3α-Hydroxysteroid dehydrogenase
1:
750:10.1016/S0969-2126(00)00064-2
560:10.3390/microorganisms9030469
358:tetrahydrodeoxycorticosterone
1400:10.1371/journal.pbio.3000198
1140:10.1371/journal.pbio.1001305
944:10.1007/978-1-4615-5871-2_54
520:10.1016/j.jsbmb.2011.08.002
1808:
1227:Frontiers in Plant Science
1055:10.1038/s41392-020-00354-w
611:10.3389/fmicb.2023.1140662
366:androgen backdoor patthway
1647:Michaelis–Menten kinetics
1360:10.1016/j.tem.2004.09.004
1240:10.3389/fpls.2023.1159394
903:10.1042/0264-6021:3510067
649:Plant and Cell Physiology
647:Biosynthesis in Tomato".
598:Frontiers in Microbiology
362:5α-androstane-3α,17β-diol
150:
1539:Diffusion-limited enzyme
1284:WikiJournal of Medicine
1016:10.1126/science.aac4854
981:10.1023/A:1010291527744
777:Journal of Biochemistry
697:J Clin Endocrinol Metab
1100:10.1210/jcem.86.2.7216
864:10.1210/jcem.86.3.7325
710:10.1210/jcem.86.2.7216
417:
370:5α-dihydrotestosterone
276:retinol dehydrogenases
268:retinol dehydrogenases
1632:Eadie–Hofstee diagram
1565:Allosteric regulation
1297:10.15347/WJM/2023.003
1190:10.1210/er.2018-00089
969:Biochemistry (Moscow)
407:
1642:Lineweaver–Burk plot
828:10.1210/en.2002-0032
294:Enzyme Name Aliases
1010:(6265): 1208–1213.
891:Biochemical Journal
287:
281:aldo-keto-reductase
1601:Enzyme superfamily
1534:Enzyme promiscuity
661:10.1093/pcp/pcz049
418:
286:
1757:
1756:
1178:Endocrine Reviews
953:978-1-4615-5871-2
374:androgen receptor
350:
349:
291:HGNC Gene Symbol
240:sequence homology
199:
198:
195:
194:
114:metabolic pathway
16:(Redirected from
1799:
1774:
1773:
1765:
1637:Hanes–Woolf plot
1580:Enzyme activator
1575:Enzyme inhibitor
1549:Enzyme catalysis
1493:
1486:
1479:
1470:
1461:
1460:
1440:(3): 430. 1989.
1429:
1423:
1422:
1412:
1402:
1378:
1372:
1371:
1343:
1337:
1330:
1324:
1322:
1320:
1314:
1299:
1281:
1272:
1263:
1262:
1252:
1242:
1218:
1212:
1211:
1201:
1169:
1163:
1162:
1152:
1142:
1118:
1112:
1111:
1083:
1077:
1076:
1066:
1034:
1028:
1027:
999:
993:
992:
964:
958:
957:
931:
925:
924:
914:
882:
876:
875:
858:(3): 1324–1331.
846:
840:
839:
822:(7): 2922–2932.
810:
801:
800:
771:
762:
761:
732:
726:
725:
712:
688:
673:
672:
655:(6): 1304–1315.
643:
634:
633:
623:
613:
589:
583:
582:
572:
562:
538:
532:
531:
503:
494:
493:
491:
489:
474:
461:
460:
458:
456:
441:
392:precursors, and
354:allopregnanolone
334:type 5; HSD17B5
288:
206:protein isoforms
152:
30:
21:
1807:
1806:
1802:
1801:
1800:
1798:
1797:
1796:
1782:
1781:
1780:
1768:
1760:
1758:
1753:
1665:Oxidoreductases
1651:
1627:Enzyme kinetics
1615:
1611:List of enzymes
1584:
1553:
1524:Catalytic triad
1502:
1497:
1466:
1464:
1456:. p. 430:
1431:
1430:
1426:
1393:(4): e3000198.
1380:
1379:
1375:
1345:
1344:
1340:
1318:
1316:
1312:
1279:
1274:
1273:
1266:
1220:
1219:
1215:
1171:
1170:
1166:
1133:(4): e1001305.
1120:
1119:
1115:
1085:
1084:
1080:
1036:
1035:
1031:
1001:
1000:
996:
966:
965:
961:
954:
933:
932:
928:
897:(Pt 1): 67–77.
884:
883:
879:
848:
847:
843:
812:
811:
804:
773:
772:
765:
734:
733:
729:
690:
689:
676:
645:
644:
637:
591:
590:
586:
540:
539:
535:
505:
504:
497:
487:
485:
476:
475:
464:
454:
452:
443:
442:
431:
427:
402:
378:glucocorticoids
218:
28:
23:
22:
15:
12:
11:
5:
1805:
1803:
1795:
1794:
1784:
1783:
1779:
1778:
1755:
1754:
1752:
1751:
1738:
1725:
1712:
1699:
1686:
1673:
1659:
1657:
1653:
1652:
1650:
1649:
1644:
1639:
1634:
1629:
1623:
1621:
1617:
1616:
1614:
1613:
1608:
1603:
1598:
1592:
1590:
1589:Classification
1586:
1585:
1583:
1582:
1577:
1572:
1567:
1561:
1559:
1555:
1554:
1552:
1551:
1546:
1541:
1536:
1531:
1526:
1521:
1516:
1510:
1508:
1504:
1503:
1498:
1496:
1495:
1488:
1481:
1473:
1463:
1462:
1424:
1373:
1354:(9): 432–438.
1338:
1264:
1213:
1184:(2): 447–475.
1164:
1113:
1094:(2): 841–846.
1078:
1029:
994:
975:(3): 256–266.
959:
952:
926:
877:
841:
802:
783:(5): 940–946.
763:
744:(7): 629–640.
727:
674:
635:
584:
547:Microorganisms
533:
514:(1–2): 31–46.
495:
462:
428:
426:
423:
401:
398:
386:prostaglandins
348:
347:
344:
336:
335:
328:
320:
319:
316:
308:
307:
304:
296:
295:
292:
248:RNA expression
232:) and type 3 (
217:
214:
197:
196:
193:
192:
187:
181:
180:
175:
169:
168:
163:
157:
156:
148:
147:
136:
129:
128:
123:
117:
116:
111:
105:
104:
99:
93:
92:
87:
81:
80:
75:
69:
68:
63:
57:
56:
52:
51:
46:
40:
39:
35:
34:
26:
24:
14:
13:
10:
9:
6:
4:
3:
2:
1804:
1793:
1790:
1789:
1787:
1777:
1772:
1767:
1763:
1749:
1745:
1744:
1739:
1736:
1732:
1731:
1726:
1723:
1719:
1718:
1713:
1710:
1706:
1705:
1700:
1697:
1693:
1692:
1687:
1684:
1680:
1679:
1674:
1671:
1667:
1666:
1661:
1660:
1658:
1654:
1648:
1645:
1643:
1640:
1638:
1635:
1633:
1630:
1628:
1625:
1624:
1622:
1618:
1612:
1609:
1607:
1606:Enzyme family
1604:
1602:
1599:
1597:
1594:
1593:
1591:
1587:
1581:
1578:
1576:
1573:
1571:
1570:Cooperativity
1568:
1566:
1563:
1562:
1560:
1556:
1550:
1547:
1545:
1542:
1540:
1537:
1535:
1532:
1530:
1529:Oxyanion hole
1527:
1525:
1522:
1520:
1517:
1515:
1512:
1511:
1509:
1505:
1501:
1494:
1489:
1487:
1482:
1480:
1475:
1474:
1471:
1467:
1459:
1455:
1451:
1447:
1443:
1439:
1435:
1434:Eur J Biochem
1428:
1425:
1420:
1416:
1411:
1406:
1401:
1396:
1392:
1388:
1384:
1377:
1374:
1369:
1365:
1361:
1357:
1353:
1349:
1342:
1339:
1336:
1334:
1329:
1311:
1307:
1303:
1298:
1293:
1289:
1285:
1278:
1271:
1269:
1265:
1260:
1256:
1251:
1246:
1241:
1236:
1232:
1228:
1224:
1217:
1214:
1209:
1205:
1200:
1195:
1191:
1187:
1183:
1179:
1175:
1168:
1165:
1160:
1156:
1151:
1146:
1141:
1136:
1132:
1128:
1124:
1117:
1114:
1109:
1105:
1101:
1097:
1093:
1089:
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1519:Binding site
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703:(2): 841–6.
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453:. Retrieved
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78:BRENDA entry
1514:Active site
394:xenobiotics
244:kilodaltons
226:), type 2 (
66:IntEnz view
38:Identifiers
1717:Isomerases
1691:Hydrolases
1558:Regulation
553:(3): 469.
425:References
382:progestins
272:microsomal
135:structures
102:KEGG entry
1596:EC number
1333:CC BY 4.0
1306:257943362
738:Structure
410:lanostane
390:bile acid
270:found in
55:Databases
1792:EC 1.1.1
1786:Category
1620:Kinetics
1544:Cofactor
1507:Activity
1419:30943210
1368:15519890
1335:license.
1310:Archived
1259:37396629
1250:10311447
1208:30137266
1159:22505847
1108:11158055
1073:33384409
1049:(1): 2.
1024:26785480
989:11333148
921:10998348
872:11238528
850:Brain".
836:12810547
719:11158055
669:30892648
630:36910199
579:33668351
528:21884790
482:Archived
449:Archived
210:isozymes
190:proteins
178:articles
166:articles
139:RCSB PDB
49:1.1.1.50
1776:Biology
1730:Ligases
1500:Enzymes
1454:2606099
1410:6464227
1319:May 12,
1199:6405412
1150:3323522
1064:7775471
1004:Science
912:1221336
797:9792917
758:7922040
621:9998936
570:7996314
488:May 12,
455:May 12,
126:profile
109:MetaCyc
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301:AKR1C1
259:AKR1C2
253:AKR1C4
235:AKR1C2
229:AKR1C3
223:AKR1C4
173:PubMed
155:Search
145:PDBsum
85:ExPASy
73:BRENDA
61:IntEnz
44:EC no.
27:Enzyme
1656:Types
1313:(PDF)
1302:S2CID
1280:(PDF)
414:IUPAC
264:HaCaT
121:PRIAM
1748:list
1741:EC7
1735:list
1728:EC6
1722:list
1715:EC5
1709:list
1702:EC4
1696:list
1689:EC3
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1676:EC2
1670:list
1663:EC1
1450:PMID
1415:PMID
1364:PMID
1321:2024
1255:PMID
1204:PMID
1155:PMID
1104:PMID
1069:PMID
1020:PMID
985:PMID
948:ISBN
917:PMID
868:PMID
832:PMID
793:PMID
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715:PMID
665:PMID
626:PMID
575:PMID
524:PMID
490:2024
457:2024
185:NCBI
142:PDBe
97:KEGG
1442:doi
1438:186
1405:PMC
1395:doi
1356:doi
1292:doi
1245:PMC
1235:doi
1194:PMC
1186:doi
1145:PMC
1135:doi
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133:PDB
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