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Nucleoprotein

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430: 295: 86: 27: 434: 433: 435: 300: 299: 296: 301: 432: 298: 383:. Some viruses are simple ribonucleoproteins, containing only one molecule of RNA and a number of identical protein molecules. Others are ribonucleoprotein or deoxyribonucleoprotein complexes containing a number of different proteins, and exceptionally more nucleic acid molecules. Currently, over 2000 RNPs can be found in the RCSB Protein Data Bank (PDB). Furthermore, the 425:
RNPs computationally. Although computational methods of deducing RNP structures are less accurate than experimental methods, they provide a rough model of the structure which allows for predictions of the identity of significant amino acids and nucleotide residues. Such information helps in
431: 297: 247:. Deoxyribonucleoproteins in this kind of complex interact to generate a multiprotein regulatory complex in which the intervening DNA is looped or wound. The deoxyribonucleoproteins participate in regulating DNA replication and transcription. 387:(PRIDB) possesses a collection of information on RNA-protein interfaces based on data drawn from the PDB. Some common features of protein-RNA interfaces were deduced based on known structures. For example, RNP in snRNPs have an RNA-binding 1658:
Tuszynska, Irina; Matelska, Dorota; Magnus, Marcin; Chojnowski, Grzegorz; Kasprzak, Joanna M.; Kozlowski, Lukasz P.; Dunin-Horkawicz, Stanislaw; Bujnicki, Janusz M. (2014-02-01). "Computational modeling of protein-RNA complex structures".
344:. These complexes play an integral part in a number of important biological functions that include transcription, translation and regulating gene expression and regulating the metabolism of RNA. A few examples of RNPs include the 1963: 828:
Albertini, Aurélie A. V.; Wernimont, Amy K.; Muziol, Tadeusz; Ravelli, Raimond B. G.; Clapier, Cedric R.; Schoehn, Guy; Weissenhorn, Winfried; Ruigrok, Rob W. H. (2006-07-21).
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Carter, Stephen D.; Surtees, Rebecca; Walter, Cheryl T.; Ariza, Antonio; Bergeron, Éric; Nichol, Stuart T.; Hiscox, Julian A.; Edwards, Thomas A.; Barr, John N. (2012-10-15).
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and are specific for SLE. The presence of a significant level of anti-U1-RNP also serves a possible indicator of MCTD when detected in conjunction with several other factors.
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when infected. This RNA-nucleolin complex is then safely transported to the cytosol for translation by ribosomes to produce the Interleukin-6 protein, which is involved in
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are therefore little more than an organised collection of nucleoproteins with their binding sites pointing inwards. Structurally characterised viral nucleoproteins include
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Surtees, Rebecca; Ariza, Antonio; Punch, Emma K.; Trinh, Chi H.; Dowall, Stuart D.; Hewson, Roger; Hiscox, Julian A.; Barr, John N.; Edwards, Thomas A. (2015-01-01).
2038: 2058: 1779:"Structure of influenza virus RNP. I. Influenza virus nucleoprotein melts secondary structure in panhandle RNA and exposes the bases to the solvent" 2052: 1069:
Qi, Xiaoxuan; Lan, Shuiyun; Wang, Wenjian; Schelde, Lisa McLay; Dong, Haohao; Wallat, Gregor D.; Ly, Hinh; Liang, Yuying; Dong, Changjiang (2010).
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In the same way, the genomes of negative-strand RNA viruses never exist as free RNA molecule. The ribonucleoproteins protect their genomes from
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and biological functions of many nucleoproteins are understood. Important techniques for determining the structures of nucleoproteins include
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Lukong, Kiven E.; Chang, Kai-wei; Khandjian, Edouard W.; Richard, Stéphane (2008-08-01). "RNA-binding proteins in human genetic disease".
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Ariza, A.; Tanner, S. J.; Walter, C. T.; Dent, K. C.; Shepherd, D. A.; Wu, W.; Matthews, S. V.; Hiscox, J. A.; Green, T. J. (2013-06-01).
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never occur as free RNA molecules in the cell. They always associate with ribonucleoproteins and function as ribonucleoprotein complexes.
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Lewis, Benjamin A.; Walia, Rasna R.; Terribilini, Michael; Ferguson, Jeff; Zheng, Charles; Honavar, Vasant; Dobbs, Drena (2016-11-07).
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Ng, Andy Ka-Leung; Wang, Jia-Huai; Shaw, Pang-Chui (2009-05-27). "Structure and sequence analysis of influenza A virus nucleoprotein".
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In eukaryotic cells, DNA is associated with about an equal mass of histone proteins in a highly condensed nucleoprotein complex called
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Momose, Fumitaka; Sekimoto, Tetsuya; Ohkura, Takashi; Jo, Shuichi; Kawaguchi, Atsushi; Nagata, Kyosuke; Morikawa, Yuko (2011-06-22).
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Cox MM, Goodman MF, Kreuzer KN, Sherratt DJ, Sandler SJ, Marians KJ (2000). "The importance of repairing stalled replication forks".
448: 283: 898:"Nucleocapsid protein structures from orthobunyaviruses reveal insight into ribonucleoprotein architecture and RNA polymerization" 406:
portion of RNA-binding proteins help to stabilize interactions with nucleic acids. This nucleic acid binding is strengthened by
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Ruigrok, Rob WH; Crépin, Thibaut; Kolakofsky, Dan (2011). "Nucleoproteins and nucleocapsids of negative-strand RNA viruses".
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that appears to be nearly universal. A central intermediate step in this process is the interaction of multiple copies of a
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Nucleoproteins tend to be positively charged, facilitating interaction with the negatively charged nucleic acid chains. The
2028: 1430:"Diverse RNA-Binding Proteins Interact with Functionally Related Sets of RNAs, Suggesting an Extensive Regulatory System" 165: 618:
Graeme K. Hunter G. K. (2000): Vital Forces. The discovery of the molecular basis of life. Academic Press, London 2000,
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Muller, Mandy; Hutin, Stephanie; Marigold, Oliver; Li, Kathy H.; Burlingame, Al; Glaunsinger, Britt A. (2015-05-12).
623: 1371:"A Ribonucleoprotein Complex Protects the Interleukin-6 mRNA from Degradation by Distinct Herpesviral Endonucleases" 1555: 710:
Purohit, Prashant K.; Inamdar, Mandar M.; Grayson, Paul D.; Squires, Todd M.; Kondev, Jané; Phillips, Rob (2005).
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RNA. At this point, once the virus enters a host cell it will be prepared to begin the process of replication.
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protein with single-stranded DNA to form a DNP filament. Recombinases employed in this process are produced by
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Hogan, Daniel J; Riordan, Daniel P; Gerber, André P; Herschlag, Daniel; Brown, Patrick O (2016-11-07).
460: 440: 106: 98: 1014:"Structure, Function, and Evolution of the Crimean-Congo Hemorrhagic Fever Virus Nucleocapsid Protein" 1179:"Nucleoprotein structures initiating DNA replication, transcription, and site-specific recombination" 474:. The influenza viral genome is composed of eight ribonucleoprotein particles formed by a complex of 1712:"Apical Transport of Influenza A Virus Ribonucleoprotein Requires Rab11-positive Recycling Endosome" 1587: 1320:"Spontaneous self-segregation of Rad51 and Dmc1 DNA recombinases within mixed recombinase filaments" 1129: 1125: 603: 490: 251: 110: 516: 2008: 1141:
Nelson D. L., Michael M. Cox M. M. (2013): Lehninger Principles of Biochemistry. W. H. Freeman,
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A deoxyribonucleoprotein (DNP) is a complex of DNA and protein. The prototypical examples are
1574: 563: 1723: 1276: 1082: 841: 733: 666: 325: 266:(RadA recombinase), by bacteria (RecA recombinase) and by eukaryotes from yeast to humans ( 599: 8: 2042: 1932: 580: 575: 536: 512: 341: 157: 1727: 1280: 1086: 845: 737: 670: 1794: 1754: 1711: 1692: 1635: 1602: 1464: 1429: 1405: 1370: 1346: 1319: 1300: 1103: 1070: 1046: 1013: 989: 954: 930: 897: 875: 810: 754: 723: 711: 687: 654: 475: 85: 1811: 1778: 1244: 1219: 1195: 1178: 678: 653:
Tzlil, Shelly; Kindt, James T.; Gelbart, William M.; Ben-Shaul, Avinoam (March 2003).
2094: 2033: 1875: 1816: 1798: 1759: 1741: 1684: 1676: 1640: 1622: 1512: 1504: 1469: 1451: 1410: 1392: 1351: 1292: 1249: 1220:"RadA protein is an archaeal RecA protein homolog that catalyzes DNA strand exchange" 1200: 1142: 1108: 1051: 1033: 994: 976: 935: 917: 867: 859: 802: 794: 759: 692: 636: 619: 471: 468: 422: 353: 141: 102: 1696: 879: 1867: 1806: 1790: 1749: 1731: 1668: 1630: 1614: 1496: 1459: 1441: 1400: 1382: 1341: 1331: 1304: 1284: 1239: 1231: 1190: 1098: 1090: 1041: 1025: 984: 966: 925: 909: 849: 786: 749: 741: 682: 674: 444: 388: 337: 153: 814: 1736: 1446: 1387: 20: 1672: 745: 489:, it is able to expose the nucleotide bases which allow the viral polymerase to 528: 502: 479: 407: 93:
particle, with structures of the major proteins shown and labelled on the right
1871: 1500: 971: 790: 2088: 1958: 1802: 1745: 1680: 1626: 1508: 1455: 1396: 1336: 1037: 980: 921: 863: 798: 317: 854: 829: 1879: 1763: 1688: 1644: 1530: 1516: 1473: 1414: 1355: 1296: 1112: 1055: 998: 939: 871: 806: 763: 696: 415: 372: 305: 161: 145: 74: 54: 1820: 1618: 1253: 1235: 1204: 1071:"Cap binding and immune evasion revealed by Lassa nucleoprotein structure" 1978: 1029: 913: 392: 376: 271: 259: 213: 169: 149: 90: 1094: 1901: 1559: 1218:
Seitz EM, Brockman JP, Sandler SJ, Clark AJ, Kowalczykowski SC (1998).
411: 395: 349: 255: 237: 229: 225: 209: 181: 70: 31: 26: 728: 655:"Forces and Pressures in DNA Packaging and Release from Viral Capsids" 1983: 1953: 1288: 452: 418: 380: 309: 289: 244: 233: 221: 197: 193: 189: 184:, complexes in which genomic DNA is wrapped around clusters of eight 129: 125: 369: 345: 66: 515:
patients. Two types of anti-RNP antibodies are closely related to
463:. Ribonucleoprotein particles are distinct intracellular foci for 1943: 1657: 830:"Crystal Structure of the Rabies Virus Nucleoprotein-RNA Complex" 562:
for viruses because they have strain-specific and group-specific
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residues in this motif result in stacking interactions with RNA.
357: 263: 217: 185: 50: 39: 955:"The crystal structure of the Hazara virus nucleocapsid protein" 635:
Nelson D. L., Cox M. M. (2013): Lehninger Biochemie. Springer,
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bound to a viral nucleoprotein. Each RNP carries with it an
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Crickard JB, Kaniecki K, Kwon Y, Sung P, Greene EC (2018).
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Baudin, F; Bach, C; Cusack, S; Ruigrok, R W (1994-07-01).
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to move more rapidly within the cell than by simple
547:The ribonucleoproteins play a role of protection. 320:). This protects those mRNAs from degradation by 2086: 1068: 208:The most widespread deoxyribonucleoproteins are 1968:Cleavage and polyadenylation specificity factor 224:; the resulting nucleoproteins are located in 1917: 482:complex. When the nucleoprotein binds to the 250:Deoxyribonucleoproteins are also involved in 1959:hu paraneoplastic encephalomyelitis antigens 1311: 1260: 467:. These particles play an important role in 439:Cell infected with influenza A virus. Viral 1211: 426:understanding the overall function the RNP. 421:backbones. Additionally, it is possible to 379:) and are among the main components of the 1924: 1910: 776: 175: 1964:mRNA cleavage and polyadenylation factors 1810: 1753: 1735: 1634: 1603:"PRIDB: a protein–RNA interface database" 1463: 1445: 1404: 1386: 1345: 1335: 1243: 1194: 1128:at the U.S. National Library of Medicine 1102: 1045: 988: 970: 929: 853: 753: 727: 686: 602:at the U.S. National Library of Medicine 312:in red. The nucleolin protein binds some 200:replace histones during spermatogenesis. 1931: 779:Science in China Series C: Life Sciences 428: 293: 284:Heterogeneous ribonucleoprotein particle 132:) are extremely tightly packed into the 84: 25: 511:and are also detected in nearly 40% of 410:attraction between the positive lysine 322:Kaposi's sarcoma-associated herpesvirus 2087: 1176: 496: 1905: 1157: 1155: 558:. Nucleoproteins are often the major 277: 216:. The proteins combined with DNA are 2029:polypyrimidine tract-binding protein 1949:Fragile X mental retardation protein 1897:PRIDB Protein-RNA Interface Database 891: 889: 1556:"RCSB Protein Data Bank - RCSB PDB" 1183:The Journal of Biological Chemistry 65:). Typical nucleoproteins include 13: 1795:10.1002/j.1460-2075.1994.tb06614.x 1161: 1152: 14: 2106: 1890: 886: 368:), which have been implicated in 240:consists of such nucleoproteins. 1553: 443:proteins, stained white, hijack 1860:Current Opinion in Microbiology 1851: 1827: 1770: 1703: 1651: 1594: 1547: 1523: 1480: 1421: 1362: 1170: 1135: 1119: 1062: 1005: 508:mixed connective tissue disease 465:post-transcriptional regulation 385:Protein-RNA Interface Data Base 166:Crimean-Congo hemorrhagic fever 89:Cross-sectional drawing of the 946: 821: 770: 703: 646: 629: 593: 542: 1: 1613:(Database issue): D277–D282. 1196:10.1016/S0021-9258(18)77163-9 679:10.1016/s0006-3495(03)74971-6 586: 80: 1737:10.1371/journal.pone.0021123 1447:10.1371/journal.pbio.0060255 1388:10.1371/journal.ppat.1004899 391:in its RNA-binding protein. 212:, in which the component is 203: 7: 1973:Cleavage stimulation factor 1673:10.1016/j.ymeth.2013.09.014 746:10.1529/biophysj.104.047134 569: 461:ribonucleoprotein particles 308:with DNA stained blue, and 10: 2111: 1999:nuclear factor 90 proteins 1944:Butyrate response factor 1 441:ribonucleoprotein particle 287: 281: 116: 107:nuclear magnetic resonance 18: 1939: 1872:10.1016/j.mib.2011.07.011 1554:Bank, RCSB Protein Data. 1501:10.1016/j.tig.2008.05.004 1177:Echols, Harrison (1990). 972:10.1186/s12900-015-0051-3 791:10.1007/s11427-009-0064-x 326:antiviral immune response 1337:10.1074/jbc.RA117.001143 1130:Medical Subject Headings 604:Medical Subject Headings 501:Anti-RNP antibodies are 459:'RNP' can also refer to 364:and small nuclear RNPs ( 354:vault ribonucleoproteins 252:homologous recombination 111:cryo-electron microscopy 19:Not to be confused with 2039:RNA cap-binding protein 2009:Poly(A)-binding protein 1126:Deoxyribonucleoproteins 855:10.1126/science.1125280 176:Deoxyribonucleoproteins 1839:my.clevelandclinic.org 1607:Nucleic Acids Research 1582:Cite journal requires 1164:Molecular Cell Biology 959:BMC Structural Biology 902:Nucleic Acids Research 564:antigenic determinants 456: 336:(RNP) is a complex of 329: 94: 43: 1979:host factor 1 protein 1236:10.1101/gad.12.9.1248 537:Anti-Smith antibodies 438: 304: 88: 29: 2059:SMN complex proteins 1933:RNA-binding proteins 1030:10.1128/JVI.01555-12 192:cell nuclei to form 34:is a combination of 2043:Cap binding complex 1728:2011PLoSO...621123M 1619:10.1093/nar/gkq1108 1531:"Ribonucleoprotein" 1281:2000Natur.404...37C 1095:10.1038/nature09605 1087:2010Natur.468..779Q 1024:(20): 10914–10923. 1018:Journal of Virology 846:2006Sci...313..360A 738:2005BpJ....88..851P 716:Biophysical Journal 671:2003BpJ....84.1616T 659:Biophysical Journal 581:RNA-binding protein 576:DNA-binding protein 513:Lupus erythematosus 497:Anti-RNP antibodies 342:RNA-binding protein 228:. Thus, the entire 99:tertiary structures 1489:Trends in Genetics 914:10.1093/nar/gkt268 517:Sjögren's syndrome 476:negative-sense RNA 457: 330: 278:Ribonucleoproteins 95: 44: 2082: 2081: 2034:ribonucleoprotein 1789:(13): 3158–3165. 1330:(11): 4191–4200. 1189:(25): 14697–700. 1147:978-1-4641-0962-1 1081:(7325): 779–783. 908:(11): 5912–5926. 840:(5785): 360–363. 641:978-3-540-68637-8 469:influenza A virus 436: 414:and the negative 334:ribonucleoprotein 310:nucleolin protein 302: 103:X-ray diffraction 2102: 1926: 1919: 1912: 1903: 1902: 1884: 1883: 1855: 1849: 1848: 1846: 1845: 1831: 1825: 1824: 1814: 1783:The EMBO Journal 1774: 1768: 1767: 1757: 1739: 1707: 1701: 1700: 1655: 1649: 1648: 1638: 1598: 1592: 1591: 1585: 1580: 1578: 1570: 1568: 1567: 1558:. Archived from 1551: 1545: 1544: 1542: 1541: 1527: 1521: 1520: 1484: 1478: 1477: 1467: 1449: 1425: 1419: 1418: 1408: 1390: 1366: 1360: 1359: 1349: 1339: 1315: 1309: 1308: 1289:10.1038/35003501 1264: 1258: 1257: 1247: 1215: 1209: 1208: 1198: 1174: 1168: 1167: 1162:Lodish, Harvey. 1159: 1150: 1139: 1133: 1123: 1117: 1116: 1106: 1066: 1060: 1059: 1049: 1009: 1003: 1002: 992: 974: 950: 944: 943: 933: 893: 884: 883: 857: 825: 819: 818: 774: 768: 767: 757: 731: 707: 701: 700: 690: 665:(3): 1616–1627. 650: 644: 633: 627: 616: 607: 597: 505:associated with 445:active transport 437: 402:residues in the 338:ribonucleic acid 303: 254:, a process for 124:genomes (either 53:conjugated with 40:histone proteins 2110: 2109: 2105: 2104: 2103: 2101: 2100: 2099: 2085: 2084: 2083: 2078: 1935: 1930: 1893: 1888: 1887: 1856: 1852: 1843: 1841: 1833: 1832: 1828: 1775: 1771: 1708: 1704: 1656: 1652: 1599: 1595: 1583: 1581: 1572: 1571: 1565: 1563: 1552: 1548: 1539: 1537: 1535:www.uniprot.org 1529: 1528: 1524: 1485: 1481: 1426: 1422: 1381:(5): e1004899. 1367: 1363: 1316: 1312: 1275:(6773): 37–41. 1265: 1261: 1216: 1212: 1175: 1171: 1160: 1153: 1140: 1136: 1124: 1120: 1067: 1063: 1010: 1006: 951: 947: 894: 887: 826: 822: 775: 771: 708: 704: 651: 647: 634: 630: 617: 610: 598: 594: 589: 572: 545: 499: 429: 316:(e.g. mRNA for 294: 292: 286: 280: 274:recombinases). 206: 178: 119: 83: 24: 21:Nuclear protein 17: 16:Type of protein 12: 11: 5: 2108: 2098: 2097: 2080: 2079: 2077: 2076: 2070: 2065: 2056: 2050: 2045: 2036: 2031: 2026: 2020: 2015: 2006: 1996: 1990: 1981: 1976: 1970: 1961: 1956: 1951: 1946: 1940: 1937: 1936: 1929: 1928: 1921: 1914: 1906: 1900: 1899: 1892: 1891:External links 1889: 1886: 1885: 1866:(4): 504–510. 1850: 1826: 1769: 1702: 1667:(3): 310–319. 1650: 1593: 1584:|journal= 1546: 1522: 1495:(8): 416–425. 1479: 1420: 1375:PLOS Pathogens 1361: 1310: 1259: 1230:(9): 1248–53. 1210: 1169: 1151: 1134: 1118: 1061: 1004: 945: 885: 820: 785:(5): 439–449. 769: 722:(2): 851–866. 702: 645: 628: 608: 600:Nucleoproteins 591: 590: 588: 585: 584: 583: 578: 571: 568: 544: 541: 529:Autoantibodies 503:autoantibodies 498: 495: 480:RNA polymerase 282:Main article: 279: 276: 205: 202: 177: 174: 118: 115: 82: 79: 47:Nucleoproteins 15: 9: 6: 4: 3: 2: 2107: 2096: 2093: 2092: 2090: 2074: 2071: 2069: 2066: 2064: 2060: 2057: 2054: 2051: 2049: 2046: 2044: 2040: 2037: 2035: 2032: 2030: 2027: 2024: 2021: 2019: 2016: 2014: 2010: 2007: 2004: 2000: 1997: 1994: 1991: 1989: 1985: 1982: 1980: 1977: 1974: 1971: 1969: 1965: 1962: 1960: 1957: 1955: 1952: 1950: 1947: 1945: 1942: 1941: 1938: 1934: 1927: 1922: 1920: 1915: 1913: 1908: 1907: 1904: 1898: 1895: 1894: 1881: 1877: 1873: 1869: 1865: 1861: 1854: 1840: 1836: 1830: 1822: 1818: 1813: 1808: 1804: 1800: 1796: 1792: 1788: 1784: 1780: 1773: 1765: 1761: 1756: 1751: 1747: 1743: 1738: 1733: 1729: 1725: 1722:(6): e21123. 1721: 1717: 1713: 1706: 1698: 1694: 1690: 1686: 1682: 1678: 1674: 1670: 1666: 1662: 1654: 1646: 1642: 1637: 1632: 1628: 1624: 1620: 1616: 1612: 1608: 1604: 1597: 1589: 1576: 1562:on 2015-04-18 1561: 1557: 1550: 1536: 1532: 1526: 1518: 1514: 1510: 1506: 1502: 1498: 1494: 1490: 1483: 1475: 1471: 1466: 1461: 1457: 1453: 1448: 1443: 1439: 1435: 1431: 1424: 1416: 1412: 1407: 1402: 1398: 1394: 1389: 1384: 1380: 1376: 1372: 1365: 1357: 1353: 1348: 1343: 1338: 1333: 1329: 1325: 1324:J. Biol. Chem 1321: 1314: 1306: 1302: 1298: 1294: 1290: 1286: 1282: 1278: 1274: 1270: 1263: 1255: 1251: 1246: 1241: 1237: 1233: 1229: 1225: 1221: 1214: 1206: 1202: 1197: 1192: 1188: 1184: 1180: 1173: 1165: 1158: 1156: 1148: 1144: 1138: 1131: 1127: 1122: 1114: 1110: 1105: 1100: 1096: 1092: 1088: 1084: 1080: 1076: 1072: 1065: 1057: 1053: 1048: 1043: 1039: 1035: 1031: 1027: 1023: 1019: 1015: 1008: 1000: 996: 991: 986: 982: 978: 973: 968: 964: 960: 956: 949: 941: 937: 932: 927: 923: 919: 915: 911: 907: 903: 899: 892: 890: 881: 877: 873: 869: 865: 861: 856: 851: 847: 843: 839: 835: 831: 824: 816: 812: 808: 804: 800: 796: 792: 788: 784: 780: 773: 765: 761: 756: 751: 747: 743: 739: 735: 730: 729:q-bio/0406022 725: 721: 717: 713: 706: 698: 694: 689: 684: 680: 676: 672: 668: 664: 660: 656: 649: 642: 638: 632: 625: 624:0-12-361811-8 621: 615: 613: 605: 601: 596: 592: 582: 579: 577: 574: 573: 567: 565: 561: 557: 552: 550: 540: 538: 534: 530: 526: 522: 518: 514: 510: 509: 504: 494: 492: 488: 485: 481: 477: 473: 470: 466: 462: 454: 450: 446: 442: 427: 424: 420: 417: 413: 409: 408:electrostatic 405: 401: 397: 394: 390: 386: 382: 378: 374: 371: 367: 363: 359: 355: 351: 348:, the enzyme 347: 343: 339: 335: 327: 323: 319: 318:Interleukin-6 315: 311: 307: 291: 285: 275: 273: 269: 265: 261: 257: 256:repairing DNA 253: 248: 246: 241: 239: 235: 231: 227: 223: 219: 215: 211: 201: 199: 195: 191: 187: 183: 173: 171: 167: 163: 159: 158:Schmallenberg 155: 151: 147: 143: 139: 135: 131: 127: 123: 114: 112: 108: 104: 100: 92: 87: 78: 76: 72: 68: 64: 60: 56: 55:nucleic acids 52: 48: 41: 37: 33: 28: 22: 1863: 1859: 1853: 1842:. Retrieved 1838: 1829: 1786: 1782: 1772: 1719: 1715: 1705: 1664: 1660: 1653: 1610: 1606: 1596: 1575:cite journal 1564:. Retrieved 1560:the original 1549: 1538:. 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Many 117:Viruses 2053:EIF4G1 2023:PABPC4 2018:PABPC3 2013:PABPC1 1878:  1819:  1812:395207 1809:  1801:  1762:  1752:  1744:  1695:  1687:  1679:  1643:  1633:  1625:  1515:  1507:  1472:  1462:  1454:  1413:  1403:  1395:  1354:  1344:  1303:  1295:  1269:Nature 1252:  1245:316774 1242:  1203:  1145:  1132:(MeSH) 1111:  1101:  1075:Nature 1054:  1044:  1036:  997:  987:  979:  965:: 24. 938:  928:  920:  878:  870:  862:  815:610062 813:  805:  797:  762:  752:  695:  685:  639:  622:  606:(MeSH) 527:(La). 400:Lysine 366:snRNPs 168:, and 162:Hazara 146:rabies 2073:DDX20 2048:EIF4E 1693:S2CID 1301:S2CID 876:S2CID 811:S2CID 724:arXiv 556:RNase 549:mRNAs 533:snRNP 484:viral 423:model 389:motif 362:hnRNP 314:mRNAs 268:Rad51 170:Lassa 150:Ebola 122:Virus 2068:SMN2 2063:SMN1 2003:ILF2 1993:ACO2 1988:ACO1 1876:PMID 1817:PMID 1799:ISSN 1760:PMID 1742:ISSN 1685:PMID 1677:ISSN 1641:PMID 1623:ISSN 1588:help 1513:PMID 1505:ISSN 1470:PMID 1452:ISSN 1411:PMID 1393:ISSN 1352:PMID 1293:PMID 1250:PMID 1201:PMID 1143:ISBN 1109:PMID 1052:PMID 1034:ISSN 995:PMID 977:ISSN 936:PMID 918:ISSN 868:PMID 860:ISSN 803:PMID 795:ISSN 760:PMID 693:PMID 637:ISBN 620:ISBN 525:SS-B 521:SS-A 340:and 272:Dmc1 270:and 220:and 109:and 49:are 1954:Rev 1868:doi 1807:PMC 1791:doi 1750:PMC 1732:doi 1669:doi 1631:PMC 1615:doi 1497:doi 1460:PMC 1442:doi 1401:PMC 1383:doi 1342:PMC 1332:doi 1328:293 1285:doi 1273:404 1240:PMC 1232:doi 1191:doi 1187:265 1099:PMC 1091:doi 1079:468 1042:PMC 1026:doi 985:PMC 967:doi 926:PMC 910:doi 850:doi 838:313 787:doi 750:PMC 742:doi 683:PMC 675:doi 487:RNA 236:in 130:RNA 128:or 126:DNA 63:RNA 61:or 59:DNA 36:DNA 2091:: 1874:. 1864:14 1862:. 1837:. 1815:. 1805:. 1797:. 1787:13 1785:. 1781:. 1758:. 1748:. 1740:. 1730:. 1718:. 1714:. 1691:. 1683:. 1675:. 1665:65 1663:. 1639:. 1629:. 1621:. 1611:39 1609:. 1605:. 1579:: 1577:}} 1573:{{ 1533:. 1511:. 1503:. 1493:24 1491:. 1468:. 1458:. 1450:. 1436:. 1432:. 1409:. 1399:. 1391:. 1379:11 1377:. 1373:. 1350:. 1340:. 1326:. 1322:. 1299:. 1291:. 1283:. 1271:. 1248:. 1238:. 1228:12 1226:. 1222:. 1199:. 1185:. 1181:. 1154:^ 1107:. 1097:. 1089:. 1077:. 1073:. 1050:. 1040:. 1032:. 1022:86 1020:. 1016:. 993:. 983:. 975:. 963:15 961:. 957:. 934:. 924:. 916:. 906:41 904:. 900:. 888:^ 874:. 866:. 858:. 848:. 836:. 832:. 809:. 801:. 793:. 783:52 781:. 758:. 748:. 740:. 732:. 720:88 718:. 714:. 691:. 681:. 673:. 663:84 661:. 657:. 611:^ 566:. 519:: 360:, 356:, 352:, 332:A 196:. 172:. 164:, 160:, 156:, 152:, 148:, 144:, 113:. 105:, 69:, 38:+ 30:A 2075:) 2061:( 2055:) 2041:( 2025:) 2011:( 2005:) 2001:( 1995:) 1986:( 1975:) 1966:( 1925:e 1918:t 1911:v 1882:. 1870:: 1847:. 1823:. 1793:: 1766:. 1734:: 1726:: 1720:6 1699:. 1671:: 1647:. 1617:: 1590:) 1586:( 1569:. 1543:. 1519:. 1499:: 1476:. 1444:: 1438:6 1417:. 1385:: 1358:. 1334:: 1307:. 1287:: 1279:: 1256:. 1234:: 1207:. 1193:: 1166:. 1149:. 1115:. 1093:: 1085:: 1058:. 1028:: 1001:. 969:: 942:. 912:: 882:. 852:: 844:: 817:. 789:: 766:. 744:: 736:: 726:: 699:. 677:: 669:: 643:. 626:. 455:. 375:( 328:. 42:. 23:.

Index

Nuclear protein

nucleosome
DNA
histone proteins
proteins
nucleic acids
DNA
RNA
ribosomes
nucleosomes
nucleocapsid

Ebola virus
tertiary structures
X-ray diffraction
nuclear magnetic resonance
cryo-electron microscopy
Virus
DNA
RNA
viral capsid
viruses
influenza
rabies
Ebola
Bunyamwera
Schmallenberg
Hazara
Crimean-Congo hemorrhagic fever

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