2394:
40:
623:. The human genome contains 8 genes that share the structure and function with bovine pancreatic ribonuclease, with 5 additional pseudo-genes. The structure and dynamics of these enzymes are related to their diverse biological functions.
634:, a cytotoxin and helminthotoxin with ribonuclease activity; and frog liver ribonuclease and frog sialic acid-binding lectin. The sequence of pancreatic ribonucleases contains four conserved
626:
Other proteins belonging to the pancreatic ribonuclease superfamily include: bovine seminal vesicle and brain ribonucleases; kidney non-secretory ribonucleases; liver-type ribonucleases;
342:
205:
706:(RI), which protects cellular RNA from degradation by pancreatic ribonucleases. Pancreatic ribonucleases that are not inhibited by RI are approximately as toxic as
224:
286:
969:
Hofsteenge J, Matthies R, Stone SR (1989). "Primary structure of a ribonuclease from porcine liver, a new member of the ribonuclease superfamily".
1468:
1715:
1629:
1730:
1724:
1525:
1275:
1573:
1090:"Interaction of human pancreatic ribonuclease with human ribonuclease inhibitor. Generation of inhibitor-resistant cytotoxic variants"
2113:
1684:
1473:
217:
1791:
1679:
1600:
1510:
1463:
600:
168:
144:
2269:
584:
helix by complexing with single-stranded RNA; the complex arises by an extended multi-site cation-anion interaction between
362:
580:
and 3'-phosphooligonucleotides ending in C-P or U-P with 2',3'-cyclic phosphate intermediates. Ribonuclease can unwind the
2022:
1963:
2384:
2067:
1634:
1624:
2027:
1919:
1544:
631:
1613:
1609:
1605:
1521:
1354:
1006:"Human eosinophil cationic protein. Molecular cloning of a cytotoxin and helminthotoxin with ribonuclease activity"
2254:
2370:
2357:
2344:
2331:
2318:
2305:
2292:
1875:
1821:
1781:
1740:
1644:
1483:
1451:
1337:
1301:
742:
2264:
162:
2424:
2218:
2161:
1529:
1378:
1292:
487:
55:
350:
149:
2166:
1398:
1268:
2414:
1954:
1593:
703:
229:
2187:
2106:
1889:
1786:
1578:
1539:
1403:
1325:
912:"Molecular cloning of the human eosinophil-derived neurotoxin: a member of the ribonuclease gene family"
726:
699:
291:
137:
2259:
346:
2072:
1907:
1902:
1835:
1495:
1320:
923:
771:"Comparison of the structure of turtle pancreatic ribonuclease with those of mammalian ribonucleases"
72:
1129:
Saxena, SK; Rybak, SM; Winkler, G; Meade, HM; McGray, P; Youle, RJ; Ackerman, EJ (5 November 1991).
2223:
1927:
1897:
1701:
1696:
1620:
1556:
1342:
165:
67:
89:
2419:
2156:
2060:
1912:
1393:
1383:
1261:
843:
800:
1861:
1806:
1774:
1649:
1368:
1201:
1152:
1111:
1070:
1035:
986:
951:
892:
835:
792:
465:
455:
445:
435:
425:
415:
405:
395:
385:
375:
369:
337:
156:
861:
Narayanan C, Bernard DN, Bafna K, Gagné D, Chennubhotla CS, Doucet N, Agarwal PK (Mar 2018).
603:
is the best-studied member of the family and has served as a model system in work related to
2202:
2197:
2171:
2099:
1937:
1517:
1422:
1417:
1373:
1191:
1183:
1142:
1101:
1062:
1025:
1017:
978:
941:
931:
882:
874:
827:
782:
711:
620:
329:
125:
2249:
2233:
2146:
2039:
1853:
1769:
1764:
1759:
1672:
1667:
1427:
1305:
612:
604:
101:
927:
752:, but the trial did not demonstrate statistical significance against primary endpoints.
60:
2398:
2287:
2228:
2012:
2007:
2002:
1388:
1363:
1359:
1332:
1315:
1196:
1171:
1030:
1005:
887:
863:"Conservation of Dynamics Associated with Biological Function in an Enzyme Superfamily"
862:
745:
678:
653:
635:
608:
200:
1147:
1130:
946:
911:
698:
effects. Mammalian cells are protected from these effects due to their extremely high
180:
2408:
2192:
2151:
1753:
1662:
1412:
1187:
787:
770:
558:
175:
804:
576:
Specifically, the enzymes are involved in endonucleolytic cleavage of 3'-phosphomono
267:
2141:
1880:
1811:
1534:
1455:
847:
749:
707:
646:
616:
325:
1249:
279:
2365:
2300:
2136:
2055:
1826:
1720:
1583:
1549:
1487:
1253:
577:
184:
2393:
1219:
2032:
878:
818:
Marshall GR, Feng JA, Kuster DJ (2008). "Back to the future: ribonuclease A".
734:
660:
627:
554:
17:
2339:
2313:
1945:
1744:
1657:
1284:
936:
730:
695:
1205:
1115:
1106:
1089:
1074:
896:
839:
1156:
1039:
1021:
990:
955:
796:
1990:
1985:
1980:
1801:
1436:
1288:
1245:
589:
570:
562:
274:
1172:"Ribonucleases as novel chemotherapeutics : the ranpirnase example"
982:
490:
113:
1997:
1975:
1970:
1588:
722:
566:
303:
298:
132:
1066:
831:
469:
459:
449:
439:
429:
419:
409:
399:
389:
379:
2352:
2122:
2017:
1950:
1843:
1441:
1349:
1131:"Comparison of RNases and toxins upon injection into Xenopus oocytes"
737:- are not inhibited by RI and show differential cytotoxicity against
682:
674:
670:
666:
585:
357:
212:
108:
96:
84:
39:
2326:
1959:
1710:
1706:
738:
715:
649:
638:
and three amino acid residues involved in the catalytic activity.
630:, which induces vascularisation of normal and malignant tissues;
1691:
1568:
1561:
1505:
1500:
1241:
592:
residues of the enzyme and phosphate groups of the nucleotides.
319:
262:
120:
2095:
1257:
581:
2091:
694:
Some members of the pancreatic ribonuclease family have
1240:
This article incorporates text from the public domain
2382:
2278:
2242:
2211:
2180:
2129:
2048:
1936:
1888:
1874:
1852:
1834:
1820:
1800:
1739:
1643:
1482:
1450:
1300:
551:
ribonucleate 3'-pyrimidino-oligonucleotidohydrolase
368:
356:
336:
318:
313:
297:
285:
273:
261:
253:
248:
243:
223:
211:
199:
194:
174:
155:
143:
131:
119:
107:
95:
83:
78:
66:
54:
49:
32:
1088:Gaur, D; Swaminathan, S; Batra, JK (6 July 2001).
1579:Fructose 6-P,2-kinase:fructose 2,6-bisphosphatase
721:Two pancreatic ribonucleases isolated from the
2107:
1269:
8:
1004:Rosenberg HF, Ackerman SJ, Tenen DG (1989).
910:Rosenberg HF, Tenen DG, Ackerman SJ (1989).
2114:
2100:
2092:
1885:
1831:
1817:
1276:
1262:
1254:
310:
191:
38:
1195:
1146:
1105:
1029:
945:
935:
886:
786:
535:Ceratitis capitata alkaline ribonuclease
2389:
1469:Ubiquitin carboxy-terminal hydrolase L1
761:
240:
29:
2049:either deoxy- or ribo-
769:Beintema JJ, van der Laan JM (1986).
7:
1630:Protein serine/threonine phosphatase
1053:Raines RT (1998). "Ribonuclease A".
1731:Cyclic nucleotide phosphodiesterase
1725:Clostridium perfringens alpha toxin
1526:Tartrate-resistant acid phosphatase
1135:The Journal of Biological Chemistry
1094:The Journal of Biological Chemistry
741:cells. Ranpirnase was studied in a
543:gene S locus-specific glycoproteins
1574:Pyruvate dehydrogenase phosphatase
652:encoding proteins containing this
25:
1474:4-hydroxybenzoyl-CoA thioesterase
2392:
1188:10.2165/00063030-200822010-00006
547:S-genotype-assocd. glycoproteins
1792:N-acetylglucosamine-6-sulfatase
1680:Sphingomyelin phosphodiesterase
1601:Inositol-phosphate phosphatase
1464:Palmitoyl protein thioesterase
601:Bovine pancreatic ribonuclease
561:found in high quantity in the
484:Pancreatic ribonuclease family
1:
1964:RNA-induced silencing complex
1220:"Alfacell Annual Report 2009"
1148:10.1016/S0021-9258(18)54842-0
748:as a treatment candidate for
314:Available protein structures:
2068:Serratia marcescens nuclease
1635:Dual-specificity phosphatase
1625:Protein tyrosine phosphatase
916:Proc. Natl. Acad. Sci. U.S.A
788:10.1016/0014-5793(86)80113-2
1545:Fructose 1,6-bisphosphatase
632:eosinophil cationic protein
2441:
1239:
1170:Lee JE, Raines RT (2008).
2270:Michaelis–Menten kinetics
1782:Galactosamine-6 sulfatase
1338:6-phosphogluconolactonase
879:10.1016/j.str.2018.01.015
309:
190:
37:
2162:Diffusion-limited enzyme
1530:Purple acid phosphatases
937:10.1073/pnas.86.12.4460
519:ribonucleic phosphatase
244:Pancreatic ribonuclease
33:Pancreatic ribonuclease
1955:Microprocessor complex
1594:Beta-propeller phytase
1107:10.1074/jbc.m102440200
704:ribonuclease inhibitor
596:Notable family members
553:) is a superfamily of
2255:Eadie–Hofstee diagram
2188:Allosteric regulation
1890:Endodeoxyribonuclease
1787:Iduronate-2-sulfatase
1540:Glucose 6-phosphatase
1326:Butyrylcholinesterase
1022:10.1084/jem.170.1.163
727:Northern leopard frog
685:, RNASE7, and RNASE8.
523:alkaline ribonuclease
2265:Lineweaver–Burk plot
2073:Micrococcal nuclease
1908:Deoxyribonuclease IV
1903:Deoxyribonuclease II
1836:Exodeoxyribonuclease
1496:Alkaline phosphatase
1321:Acetylcholinesterase
669:, RNASE10, RNASE12,
531:gene S glycoproteins
44:Structure of RNase A
1928:UvrABC endonuclease
1898:Deoxyribonuclease I
1621:Protein phosphatase
1557:Protein phosphatase
1355:Bile salt-dependent
1343:PAF acetylhydrolase
983:10.1021/bi00451a040
928:1989PNAS...86.4460R
611:formation, protein
2224:Enzyme superfamily
2157:Enzyme promiscuity
2061:Mung bean nuclease
1920:Restriction enzyme
1913:Restriction enzyme
539:SLSG glycoproteins
515:endoribonuclease I
2380:
2379:
2089:
2088:
2085:
2084:
2081:
2080:
1870:
1869:
1862:Oligonucleotidase
1807:deoxyribonuclease
1775:Steroid sulfatase
1650:Phosphodiesterase
1379:Hormone-sensitive
1067:10.1021/cr960427h
977:(25): 9806–9813.
922:(12): 4460–4464.
832:10.1002/bip.20845
481:
480:
477:
476:
363:structure summary
239:
238:
235:
234:
138:metabolic pathway
16:(Redirected from
2432:
2397:
2396:
2388:
2260:Hanes–Woolf plot
2203:Enzyme activator
2198:Enzyme inhibitor
2172:Enzyme catalysis
2116:
2109:
2102:
2093:
1938:Endoribonuclease
1924:
1918:
1886:
1832:
1818:
1518:Acid phosphatase
1399:Monoacylglycerol
1309:ester hydrolases
1278:
1271:
1264:
1255:
1234:
1233:
1231:
1229:
1224:
1216:
1210:
1209:
1199:
1167:
1161:
1160:
1150:
1141:(31): 21208–14.
1126:
1120:
1119:
1109:
1100:(27): 24978–84.
1085:
1079:
1078:
1061:(3): 1045–1066.
1050:
1044:
1043:
1033:
1001:
995:
994:
966:
960:
959:
949:
939:
907:
901:
900:
890:
858:
852:
851:
815:
809:
808:
790:
766:
712:diphtheria toxin
621:protein dynamics
507:pancreatic RNase
472:
462:
452:
442:
432:
422:
412:
402:
392:
382:
311:
241:
192:
42:
30:
27:Class of enzymes
21:
2440:
2439:
2435:
2434:
2433:
2431:
2430:
2429:
2425:Protein domains
2405:
2404:
2403:
2391:
2383:
2381:
2376:
2288:Oxidoreductases
2274:
2250:Enzyme kinetics
2238:
2234:List of enzymes
2207:
2176:
2147:Catalytic triad
2125:
2120:
2090:
2077:
2044:
1932:
1922:
1916:
1879:
1866:
1854:Exoribonuclease
1848:
1825:
1809:
1805:
1796:
1770:Arylsulfatase L
1765:Arylsulfatase B
1760:Arylsulfatase A
1735:
1648:
1639:
1478:
1446:
1308:
1296:
1282:
1252:
1238:
1237:
1227:
1225:
1222:
1218:
1217:
1213:
1169:
1168:
1164:
1128:
1127:
1123:
1087:
1086:
1082:
1052:
1051:
1047:
1003:
1002:
998:
968:
967:
963:
909:
908:
904:
860:
859:
855:
817:
816:
812:
768:
767:
763:
758:
692:
644:
636:disulfide bonds
613:crystallography
605:protein folding
598:
464:
454:
444:
434:
424:
414:
404:
394:
384:
374:
45:
28:
23:
22:
15:
12:
11:
5:
2438:
2436:
2428:
2427:
2422:
2417:
2407:
2406:
2402:
2401:
2378:
2377:
2375:
2374:
2361:
2348:
2335:
2322:
2309:
2296:
2282:
2280:
2276:
2275:
2273:
2272:
2267:
2262:
2257:
2252:
2246:
2244:
2240:
2239:
2237:
2236:
2231:
2226:
2221:
2215:
2213:
2212:Classification
2209:
2208:
2206:
2205:
2200:
2195:
2190:
2184:
2182:
2178:
2177:
2175:
2174:
2169:
2164:
2159:
2154:
2149:
2144:
2139:
2133:
2131:
2127:
2126:
2121:
2119:
2118:
2111:
2104:
2096:
2087:
2086:
2083:
2082:
2079:
2078:
2076:
2075:
2070:
2065:
2064:
2063:
2052:
2050:
2046:
2045:
2043:
2042:
2037:
2036:
2035:
2030:
2025:
2020:
2010:
2005:
2000:
1995:
1994:
1993:
1988:
1983:
1978:
1968:
1967:
1966:
1957:
1942:
1940:
1934:
1933:
1931:
1930:
1925:
1910:
1905:
1900:
1894:
1892:
1883:
1872:
1871:
1868:
1867:
1865:
1864:
1858:
1856:
1850:
1849:
1847:
1846:
1840:
1838:
1829:
1815:
1798:
1797:
1795:
1794:
1789:
1784:
1779:
1778:
1777:
1772:
1767:
1762:
1749:
1747:
1737:
1736:
1734:
1733:
1728:
1718:
1713:
1704:
1699:
1694:
1689:
1688:
1687:
1677:
1676:
1675:
1670:
1660:
1654:
1652:
1641:
1640:
1638:
1637:
1632:
1627:
1618:
1617:
1616:
1598:
1597:
1596:
1586:
1581:
1576:
1571:
1566:
1565:
1564:
1554:
1553:
1552:
1542:
1537:
1532:
1515:
1514:
1513:
1508:
1503:
1492:
1490:
1480:
1479:
1477:
1476:
1471:
1466:
1460:
1458:
1448:
1447:
1445:
1444:
1439:
1433:
1432:
1431:
1430:
1425:
1420:
1409:
1408:
1407:
1406:
1404:Diacylglycerol
1401:
1396:
1391:
1386:
1381:
1376:
1371:
1366:
1357:
1346:
1345:
1340:
1335:
1333:Pectinesterase
1330:
1329:
1328:
1323:
1316:Cholinesterase
1312:
1310:
1298:
1297:
1283:
1281:
1280:
1273:
1266:
1258:
1236:
1235:
1211:
1162:
1121:
1080:
1045:
1016:(1): 163–176.
996:
961:
902:
873:(3): 426–436.
853:
810:
781:(2): 338–343.
760:
759:
757:
754:
746:clinical trial
691:
688:
687:
686:
664:
643:
640:
609:disulfide bond
597:
594:
511:ribonuclease I
479:
478:
475:
474:
372:
366:
365:
360:
354:
353:
340:
334:
333:
323:
316:
315:
307:
306:
301:
295:
294:
289:
283:
282:
277:
271:
270:
265:
259:
258:
255:
251:
250:
246:
245:
237:
236:
233:
232:
227:
221:
220:
215:
209:
208:
203:
197:
196:
188:
187:
178:
172:
171:
160:
153:
152:
147:
141:
140:
135:
129:
128:
123:
117:
116:
111:
105:
104:
99:
93:
92:
87:
81:
80:
76:
75:
70:
64:
63:
58:
52:
51:
47:
46:
43:
35:
34:
26:
24:
18:Ribonuclease A
14:
13:
10:
9:
6:
4:
3:
2:
2437:
2426:
2423:
2421:
2418:
2416:
2415:Ribonucleases
2413:
2412:
2410:
2400:
2395:
2390:
2386:
2372:
2368:
2367:
2362:
2359:
2355:
2354:
2349:
2346:
2342:
2341:
2336:
2333:
2329:
2328:
2323:
2320:
2316:
2315:
2310:
2307:
2303:
2302:
2297:
2294:
2290:
2289:
2284:
2283:
2281:
2277:
2271:
2268:
2266:
2263:
2261:
2258:
2256:
2253:
2251:
2248:
2247:
2245:
2241:
2235:
2232:
2230:
2229:Enzyme family
2227:
2225:
2222:
2220:
2217:
2216:
2214:
2210:
2204:
2201:
2199:
2196:
2194:
2193:Cooperativity
2191:
2189:
2186:
2185:
2183:
2179:
2173:
2170:
2168:
2165:
2163:
2160:
2158:
2155:
2153:
2152:Oxyanion hole
2150:
2148:
2145:
2143:
2140:
2138:
2135:
2134:
2132:
2128:
2124:
2117:
2112:
2110:
2105:
2103:
2098:
2097:
2094:
2074:
2071:
2069:
2066:
2062:
2059:
2058:
2057:
2054:
2053:
2051:
2047:
2041:
2038:
2034:
2031:
2029:
2026:
2024:
2021:
2019:
2016:
2015:
2014:
2011:
2009:
2006:
2004:
2001:
1999:
1996:
1992:
1989:
1987:
1984:
1982:
1979:
1977:
1974:
1973:
1972:
1969:
1965:
1961:
1958:
1956:
1952:
1949:
1948:
1947:
1944:
1943:
1941:
1939:
1935:
1929:
1926:
1921:
1914:
1911:
1909:
1906:
1904:
1901:
1899:
1896:
1895:
1893:
1891:
1887:
1884:
1882:
1877:
1873:
1863:
1860:
1859:
1857:
1855:
1851:
1845:
1842:
1841:
1839:
1837:
1833:
1830:
1828:
1823:
1819:
1816:
1813:
1808:
1803:
1799:
1793:
1790:
1788:
1785:
1783:
1780:
1776:
1773:
1771:
1768:
1766:
1763:
1761:
1758:
1757:
1756:
1755:
1754:arylsulfatase
1751:
1750:
1748:
1746:
1742:
1738:
1732:
1729:
1726:
1722:
1719:
1717:
1714:
1712:
1708:
1705:
1703:
1700:
1698:
1695:
1693:
1690:
1686:
1683:
1682:
1681:
1678:
1674:
1671:
1669:
1666:
1665:
1664:
1663:Phospholipase
1661:
1659:
1656:
1655:
1653:
1651:
1646:
1642:
1636:
1633:
1631:
1628:
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1438:
1435:
1434:
1429:
1426:
1424:
1421:
1419:
1416:
1415:
1414:
1413:Phospholipase
1411:
1410:
1405:
1402:
1400:
1397:
1395:
1392:
1390:
1387:
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1189:
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1173:
1166:
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1144:
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1136:
1132:
1125:
1122:
1117:
1113:
1108:
1103:
1099:
1095:
1091:
1084:
1081:
1076:
1072:
1068:
1064:
1060:
1056:
1049:
1046:
1041:
1037:
1032:
1027:
1023:
1019:
1015:
1011:
1007:
1000:
997:
992:
988:
984:
980:
976:
972:
965:
962:
957:
953:
948:
943:
938:
933:
929:
925:
921:
917:
913:
906:
903:
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894:
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884:
880:
876:
872:
868:
864:
857:
854:
849:
845:
841:
837:
833:
829:
826:(3): 259–77.
825:
821:
814:
811:
806:
802:
798:
794:
789:
784:
780:
776:
772:
765:
762:
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747:
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736:
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724:
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629:
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614:
610:
606:
602:
595:
593:
591:
587:
583:
579:
574:
572:
568:
564:
560:
559:endonucleases
556:
552:
548:
544:
540:
536:
532:
528:
524:
520:
516:
512:
508:
504:
500:
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471:
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300:
296:
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219:
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210:
207:
204:
202:
198:
193:
189:
186:
182:
179:
177:
176:Gene Ontology
173:
170:
167:
164:
161:
158:
154:
151:
148:
146:
142:
139:
136:
134:
130:
127:
124:
122:
118:
115:
114:NiceZyme view
112:
110:
106:
103:
100:
98:
94:
91:
88:
86:
82:
77:
74:
71:
69:
65:
62:
59:
57:
53:
48:
41:
36:
31:
19:
2366:Translocases
2363:
2350:
2337:
2324:
2311:
2301:Transferases
2298:
2285:
2142:Binding site
1923:}}
1917:{{
1881:Endonuclease
1812:ribonuclease
1752:
1535:Nucleotidase
1456:Thioesterase
1226:. Retrieved
1214:
1182:(1): 53–58.
1179:
1175:
1165:
1138:
1134:
1124:
1097:
1093:
1083:
1058:
1054:
1048:
1013:
1009:
999:
974:
971:Biochemistry
970:
964:
919:
915:
905:
870:
866:
856:
823:
819:
813:
778:
774:
764:
750:mesothelioma
720:
708:alpha-sarcin
693:
690:Cytotoxicity
645:
625:
617:spectroscopy
599:
575:
569:and of some
550:
546:
542:
538:
534:
530:
527:ribonuclease
526:
522:
518:
514:
510:
506:
502:
498:
494:
483:
482:
102:BRENDA entry
2137:Active site
2056:Nuclease S1
1827:Exonuclease
1721:Lecithinase
1550:Calcineurin
1488:Phosphatase
1394:Lipoprotein
1384:Endothelial
1010:J. Exp. Med
820:Biopolymers
642:Human genes
578:nucleotides
565:of certain
249:Identifiers
90:IntEnz view
50:Identifiers
2409:Categories
2340:Isomerases
2314:Hydrolases
2181:Regulation
1369:Pancreatic
1306:Carboxylic
1228:2 February
756:References
735:ranpirnase
628:angiogenin
557:-specific
555:pyrimidine
326:structures
159:structures
126:KEGG entry
73:9001-99-4
2420:EC 3.1.27
2219:EC number
1946:RNase III
1804:(includes
1745:Sulfatase
1658:Autotaxin
1522:Prostatic
1374:Lysosomal
1289:esterases
1285:Hydrolase
1250:IPR001427
1055:Chem. Rev
867:Structure
775:FEBS Lett
743:Phase III
731:amphinase
696:cytotoxic
656:include:
304:PDOC00118
280:IPR001427
79:Databases
2243:Kinetics
2167:Cofactor
2130:Activity
2040:RNase T1
1802:Nuclease
1437:Cutinase
1246:InterPro
1206:18215091
1176:BioDrugs
1116:11342552
1075:11848924
897:29478822
840:17868092
805:21907373
700:affinity
590:arginine
571:reptiles
563:pancreas
491:4.6.1.18
463:
453:
443:
433:
423:
413:
403:
393:
383:
343:RCSB PDB
275:InterPro
230:proteins
218:articles
206:articles
163:RCSB PDB
61:4.6.1.18
2399:Biology
2353:Ligases
2123:Enzymes
2013:RNase E
2008:RNase Z
2003:RNase A
1998:RNase P
1971:RNase H
1589:Phytase
1389:Hepatic
1364:Lingual
1360:Gastric
1197:2802594
1157:1939163
1040:2473157
1031:2189377
991:2611266
956:2734298
924:Bibcode
888:5842143
848:2905312
797:3940901
725:of the
723:oocytes
567:mammals
503:RNase A
499:RNase I
473:
299:PROSITE
292:SM00092
268:PF00074
185:QuickGO
150:profile
133:MetaCyc
68:CAS no.
2385:Portal
2327:Lyases
1951:Drosha
1876:3.1.21
1844:RecBCD
1822:3.1.11
1442:PETase
1350:Lipase
1204:
1194:
1155:
1114:
1073:
1038:
1028:
989:
954:
947:287289
944:
895:
885:
846:
838:
803:
795:
683:RNASE6
679:RNASE4
675:RNASE3
671:RNASE2
667:RNASE1
654:domain
619:, and
586:lysine
358:PDBsum
332:
322:
257:RNaseA
254:Symbol
213:PubMed
195:Search
181:AmiGO
169:PDBsum
109:ExPASy
97:BRENDA
85:IntEnz
56:EC no.
2279:Types
1960:Dicer
1915:;see
1741:3.1.6
1711:PDE4B
1707:PDE4A
1645:3.1.4
1614:IMPA3
1610:IMPA2
1606:IMPA1
1484:3.1.3
1452:3.1.2
1302:3.1.1
1223:(PDF)
844:S2CID
801:S2CID
739:tumor
716:ricin
714:, or
650:genes
647:Human
495:RNase
287:SMART
145:PRIAM
2371:list
2364:EC7
2358:list
2351:EC6
2345:list
2338:EC5
2332:list
2325:EC4
2319:list
2312:EC3
2306:list
2299:EC2
2293:list
2286:EC1
1878:-31:
1824:-16:
1810:and
1716:PDE5
1702:PDE3
1697:PDE2
1692:PDE1
1584:PTEN
1569:OCRL
1562:PP2A
1511:ALPP
1506:ALPL
1501:ALPI
1295:3.1)
1244:and
1242:Pfam
1230:2015
1202:PMID
1153:PMID
1112:PMID
1071:PMID
1036:PMID
987:PMID
952:PMID
893:PMID
836:PMID
793:PMID
733:and
702:for
615:and
588:and
470:1agi
460:1afu
450:1afl
440:1afk
430:1a5q
420:1a5p
410:1a4y
400:1a2w
390:11bg
380:11ba
351:PDBj
347:PDBe
330:ECOD
320:Pfam
263:Pfam
225:NCBI
166:PDBe
121:KEGG
2033:4/5
1192:PMC
1184:doi
1143:doi
1139:266
1102:doi
1098:276
1063:doi
1026:PMC
1018:doi
1014:170
979:doi
942:PMC
932:doi
883:PMC
875:doi
828:doi
783:doi
779:194
661:ANG
582:RNA
466:PDB
456:PDB
446:PDB
436:PDB
426:PDB
416:PDB
406:PDB
396:PDB
386:PDB
376:PDB
370:PDB
338:PDB
201:PMC
157:PDB
2411::
1991:2C
1986:2B
1981:2A
1962::
1953::
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1423:A2
1418:A1
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1293:EC
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1200:.
1190:.
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1012:.
1008:.
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950:.
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930:.
920:86
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881:.
871:26
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729:-
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710:,
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509:,
505:,
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488:EC
468::
458::
448::
438::
428::
418::
408::
398::
388::
378::
349:;
345:;
328:/
183:/
2387::
2373:)
2369:(
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2356:(
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2343:(
2334:)
2330:(
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2317:(
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2304:(
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486:(
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