Menu
Home
People
Places
Arts
History
Plants & Animals
Science
Life & Culture
Technology
Reference.org
Nucleoprotein
open-in-new
<h2 id="structures">Structures</h2> <p>Nucleoproteins tend to be positively charged, facilitating interaction with the negatively charged nucleic acid chains. The <a href="/facts/Protein_tertiary_structure/1QJVj1V1">tertiary structures</a> and biological functions of many nucleoproteins are understood.<a class="footnote-ref" id="fnref:2" href="#fn:2"><sup>2</sup></a><a class="footnote-ref" id="fnref:3" href="#fn:3"><sup>3</sup></a> Important techniques for determining the structures of nucleoproteins include <a href="/facts/X-ray_diffraction/WtI0F5DN">X-ray diffraction</a>, <a href="/facts/Nuclear_magnetic_resonance/pGYAn9Bz">nuclear magnetic resonance</a> and <a href="/facts/Cryo-electron_microscopy/Hjbcf4Ec">cryo-electron microscopy</a>. </p> <h3>Viruses</h3> <p><a href="/facts/Virus/mf88Bcbl">Virus</a> genomes (either <a href="/facts/DNA_virus/sAHrgFsv">DNA</a> or <a href="/facts/RNA_virus/qwXPeATD">RNA</a>) are extremely tightly packed into the <a href="/facts/Capsid/hm7V6Ewm">viral capsid</a>.<a class="footnote-ref" id="fnref:4" href="#fn:4"><sup>4</sup></a><a class="footnote-ref" id="fnref:5" href="#fn:5"><sup>5</sup></a> Many <a href="/facts/Virus/mf88Bcbl">viruses</a> are therefore little more than an organised collection of nucleoproteins with their binding sites pointing inwards. Structurally characterised viral nucleoproteins include <a href="/facts/Influenza_A_virus/bKMeST8Q">influenza</a>,<a class="footnote-ref" id="fnref:6" href="#fn:6"><sup>6</sup></a> <a href="/facts/Rabies_virus/jRTQgIFB">rabies</a>,<a class="footnote-ref" id="fnref:7" href="#fn:7"><sup>7</sup></a> <a href="/facts/Ebola_virus/BneCtC2m">Ebola</a>, <a href="/facts/Bunyamwera_virus/5N4DnQ40">Bunyamwera</a>,<a class="footnote-ref" id="fnref:8" href="#fn:8"><sup>8</sup></a> <a href="/facts/Schmallenberg_virus/wCgJ9tpw">Schmallenberg</a>,<a class="footnote-ref" id="fnref:9" href="#fn:9"><sup>9</sup></a> <a href="/facts/Hazara_virus/XepMacFT">Hazara</a>,<a class="footnote-ref" id="fnref:10" href="#fn:10"><sup>10</sup></a> <a href="/facts/Crimean%25E2%2580%2593Congo_hemorrhagic_fever/gz52Bwrf">Crimean-Congo hemorrhagic fever</a>,<a class="footnote-ref" id="fnref:11" href="#fn:11"><sup>11</sup></a> and <a href="/facts/Lassa_virus/M7pl2Xgo">Lassa</a>.<a class="footnote-ref" id="fnref:12" href="#fn:12"><sup>12</sup></a> </p> <h2 id="deoxyribonucleoproteins">Deoxyribonucleoproteins</h2> <p>A deoxyribonucleoprotein (DNP) is a complex of DNA and protein.<a class="footnote-ref" id="fnref:13" href="#fn:13"><sup>13</sup></a> The prototypical examples are <a href="/facts/Nucleosome/HX5DR9bn">nucleosomes</a>, complexes in which genomic DNA is wrapped around clusters of eight <a href="/facts/Histone/krb5VJfp">histone</a> proteins in <a href="/facts/Eukaryote/SkwyPLMA">eukaryotic</a> cell nuclei to form <a href="/facts/Chromatin/ha0TJheJ">chromatin</a>. <a href="/facts/Protamine/ekhVN47R">Protamines</a> replace histones during spermatogenesis. </p> <h3>Functions</h3> <p>The most widespread deoxyribonucleoproteins are <a href="/facts/Nucleosome/HX5DR9bn">nucleosomes</a>, in which the component is <a href="/facts/Nuclear_DNA/5wzCJQlb">nuclear DNA</a>. The proteins combined with DNA are <a href="/facts/Histone/krb5VJfp">histones</a> and <a href="/facts/Protamine/ekhVN47R">protamines</a>; the resulting nucleoproteins are located in <a href="/facts/Chromosome/FRGf11FC">chromosomes</a>. Thus, the entire <a href="/facts/Chromosome/FRGf11FC">chromosome</a>, i.e. <a href="/facts/Chromatin/ha0TJheJ">chromatin</a> in <a href="/facts/Eukaryotes/SkwyPLMA">eukaryotes</a> consists of such nucleoproteins.<a class="footnote-ref" id="fnref:14" href="#fn:14"><sup>14</sup></a><a class="footnote-ref" id="fnref:15" href="#fn:15"><sup>15</sup></a> </p><p>In eukaryotic cells, DNA is associated with about an equal mass of histone proteins in a highly condensed nucleoprotein complex called <a href="/facts/Chromatin/ha0TJheJ">chromatin</a>.<a class="footnote-ref" id="fnref:16" href="#fn:16"><sup>16</sup></a> 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.<a class="footnote-ref" id="fnref:17" href="#fn:17"><sup>17</sup></a> </p><p>Deoxyribonucleoproteins are also involved in <a href="/facts/Homologous_recombination/WU0IIVVv">homologous recombination</a>, a process for <a href="/facts/DNA_repair/hsURuYYq">repairing DNA</a> that appears to be nearly universal. A central intermediate step in this process is the interaction of multiple copies of a <a href="/facts/Recombinase/X96ECeBj">recombinase</a> protein with single-stranded DNA to form a DNP filament. Recombinases employed in this process are produced by <a href="/facts/Archaea/Adxh0aHw">archaea</a> (RadA recombinase),<a class="footnote-ref" id="fnref:18" href="#fn:18"><sup>18</sup></a> by bacteria (RecA recombinase)<a class="footnote-ref" id="fnref:19" href="#fn:19"><sup>19</sup></a> and by eukaryotes from yeast to humans (<a href="/facts/Rad51/ml7klNxX">Rad51</a> and <a href="/facts/DMC1_(gene)/dTuoqH22">Dmc1</a> recombinases).<a class="footnote-ref" id="fnref:20" href="#fn:20"><sup>20</sup></a> </p> <h2 id="ribonucleoproteins">Ribonucleoproteins</h2> <p class="note">Main article: <a href="/facts/Heterogeneous_ribonucleoprotein_particle/YrbVK8r9">Heterogeneous ribonucleoprotein particle</a></p> <p class="note">See also: <a href="/facts/RNP_world/PDNIe8ph">RNP world</a></p> <p>A ribonucleoprotein (RNP) is a complex of <a href="/facts/Ribonucleic_acid/HxPeNfNj">ribonucleic acid</a> and <a href="/facts/RNA-binding_protein/qTPTczLC">RNA-binding protein</a>. These complexes play an integral part in a number of important biological functions that include transcription, translation and regulating gene expression<a class="footnote-ref" id="fnref:21" href="#fn:21"><sup>21</sup></a> and regulating the metabolism of RNA.<a class="footnote-ref" id="fnref:22" href="#fn:22"><sup>22</sup></a> A few examples of RNPs include the <a href="/facts/Ribosome/CF2u2gtg">ribosome</a>, the enzyme <a href="/facts/Telomerase/tUtWedEg">telomerase</a>, <a href="/facts/Vault_(organelle)/Flftc0sf">vault ribonucleoproteins</a>, <a href="/facts/RNase_P/KVn6jLV9">RNase P</a>, <a href="/facts/HnRNP/YrbVK8r9">hnRNP</a> and small nuclear RNPs (<a href="/facts/SnRNP/oj1C18HB">snRNPs</a>), which have been implicated in <a href="/facts/Pre-mRNA/4UXtKPHw">pre-mRNA</a> <a href="/facts/RNA_splicing/a2QEvCRI">splicing</a> (<a href="/facts/Spliceosome/H3nnb6rd">spliceosome</a>) and are among the main components of the <a href="/facts/Nucleolus/X7B5HKM4">nucleolus</a>.<a class="footnote-ref" id="fnref:23" href="#fn:23"><sup>23</sup></a> 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).<a class="footnote-ref" id="fnref:24" href="#fn:24"><sup>24</sup></a> Furthermore, the <a href="/facts/Protein-RNA_interface_database/vzthNI93">Protein-RNA Interface Data Base</a> (PRIDB) possesses a collection of information on RNA-protein interfaces based on data drawn from the PDB.<a class="footnote-ref" id="fnref:25" href="#fn:25"><sup>25</sup></a> Some common features of protein-RNA interfaces were deduced based on known structures. For example, RNP in snRNPs have an RNA-binding <a href="/facts/Structural_motif/g8EBDBGW">motif</a> in its RNA-binding protein. <a href="/facts/Aromaticity/wK0DzRY6">Aromatic</a> <a href="/facts/Amino_acid/WDxYwBny">amino acid</a> residues in this motif result in stacking interactions with RNA. <a href="/facts/Lysine/CEetgA9L">Lysine</a> residues in the <a href="/facts/Helix/BqC4AKwL">helical</a> portion of RNA-binding proteins help to stabilize interactions with nucleic acids. This nucleic acid binding is strengthened by <a href="/facts/Electrostatics/bxkuW6s4">electrostatic</a> attraction between the positive lysine <a href="/facts/Side_chain/Lw8KPAXn">side chains</a> and the negative <a href="/facts/Nucleic_acid/2tTgcI0v">nucleic acid</a> <a href="/facts/Phosphate/FDGVCxUG">phosphate</a> backbones. Additionally, it is possible to <a href="/facts/Homology_modeling/rgaHkvJX">model</a> RNPs computationally.<a class="footnote-ref" id="fnref:26" href="#fn:26"><sup>26</sup></a> 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 understanding the overall function the RNP.</p><p>'RNP' can also refer to <a href="/facts/Ribonucleoprotein_Particle/lGDWyKMd">ribonucleoprotein particles</a>. Ribonucleoprotein particles are distinct intracellular foci for <a href="/facts/Post-transcriptional_regulation/7DVV3tDd">post-transcriptional regulation</a>. These particles play an important role in <a href="/facts/Influenza_A_virus/bKMeST8Q">influenza A virus</a> <a href="/facts/Viral_replication/btE3fu1w">replication</a>.<a class="footnote-ref" id="fnref:27" href="#fn:27"><sup>27</sup></a> The influenza viral genome is composed of eight ribonucleoprotein particles formed by a complex of <a href="/facts/Negative-sense_RNA/hcKgNvy6">negative-sense RNA</a> bound to a viral nucleoprotein. Each RNP carries with it an <a href="/facts/RNA_polymerase/gHd0ET9R">RNA polymerase</a> complex. When the nucleoprotein binds to the <a href="/facts/Virus/mf88Bcbl">viral</a> <a href="/facts/RNA/HxPeNfNj">RNA</a>, it is able to expose the nucleotide bases which allow the viral polymerase to <a href="/facts/Transcription_(genetics)/bDgp9HDN">transcribe</a> RNA. At this point, once the virus enters a host cell it will be prepared to begin the process of replication. </p><h3>Anti-RNP antibodies</h3> <p>Anti-RNP antibodies are <a href="/facts/Autoantibodies/gkMT0XyQ">autoantibodies</a> associated with <i><a href="/facts/Mixed_connective_tissue_disease/3NgWCz7h">mixed connective tissue disease</a></i> and are also detected in nearly 40% of <a href="/facts/Lupus_erythematosus/MrAollWP">Lupus erythematosus</a> patients. Two types of anti-RNP antibodies are closely related to <a href="/facts/Sj%25C3%25B6gren%2527s_syndrome/U1p9IbFU">Sjögren's syndrome</a>: <a href="/facts/SS-A/rv3Gs5Pd">SS-A</a> (Ro) and <a href="/facts/SS-B/rKxKt85z">SS-B</a> (La). <a href="/facts/Autoantibodies/gkMT0XyQ">Autoantibodies</a> against <a href="/facts/SnRNP/oj1C18HB">snRNP</a> are called <a href="/facts/Anti-smith_antibody/Uj4vBjHm">Anti-Smith antibodies</a> 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.<a class="footnote-ref" id="fnref:28" href="#fn:28"><sup>28</sup></a> </p> <h3>Functions</h3> <p>The ribonucleoproteins play a role of protection. <a href="/facts/MRNA/oUL6qxQn">mRNAs</a> never occur as free RNA molecules in the cell. They always associate with ribonucleoproteins and function as ribonucleoprotein complexes.<a class="footnote-ref" id="fnref:29" href="#fn:29"><sup>29</sup></a> </p><p>In the same way, the genomes of negative-strand RNA viruses never exist as free RNA molecule. The ribonucleoproteins protect their genomes from <a href="/facts/RNase/Fod4qUu5">RNase</a>.<a class="footnote-ref" id="fnref:30" href="#fn:30"><sup>30</sup></a> Nucleoproteins are often the major <a href="/facts/Antigen/9JlAernG">antigens</a> for viruses because they have strain-specific and group-specific <a href="/facts/Antigenic_determinant/PL0oBuGh">antigenic determinants</a>. </p> <h2 id="see-also">See also</h2> <ul><li><a href="/facts/DNA-binding_protein/HEMm9eDX">DNA-binding protein</a></li> <li><a href="/facts/RNA-binding_protein/qTPTczLC">RNA-binding protein</a></li></ul> <h2 id="external-links">External links</h2> <ul><li><a href="https://web.archive.org/web/20160304234021/http://pridb.gdcb.iastate.edu/">PRIDB Protein-RNA Interface Database</a></li></ul> <h2 id="references">References</h2> <ol> <li id="fn:1"><p>Nucleoproteins at the U.S. National Library of Medicine Medical Subject Headings (MeSH) <a href="https://meshb.nlm.nih.gov/record/ui?name=Nucleoproteins" target="_blank">https://meshb.nlm.nih.gov/record/ui?name=Nucleoproteins</a> <a href="#fnref:1" class="footnote-back-ref">↩</a></p></li> <li id="fn:2"><p>Graeme K. Hunter G. K. (2000): Vital Forces. The discovery of the molecular basis of life. Academic Press, London 2000, ISBN 0-12-361811-8. <a href="/wiki/ISBN_(identifier)" target="_blank">/wiki/ISBN_(identifier)</a> <a href="#fnref:2" class="footnote-back-ref">↩</a></p></li> <li id="fn:3"><p>Nelson D. L., Cox M. M. (2013): Lehninger Biochemie. Springer, ISBN 978-3-540-68637-8. <a href="/wiki/ISBN_(identifier)" target="_blank">/wiki/ISBN_(identifier)</a> <a href="#fnref:3" class="footnote-back-ref">↩</a></p></li> <li id="fn:4"><p>Tzlil, Shelly; Kindt, James T.; Gelbart, William M.; Ben-Shaul, Avinoam (March 2003). "Forces and Pressures in DNA Packaging and Release from Viral Capsids". Biophysical Journal. 84 (3): 1616–1627. Bibcode:2003BpJ....84.1616T. doi:10.1016/s0006-3495(03)74971-6. PMC 1302732. PMID 12609865. <a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1302732" target="_blank">https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1302732</a> <a href="#fnref:4" class="footnote-back-ref">↩</a></p></li> <li id="fn:5"><p>Purohit, Prashant K.; Inamdar, Mandar M.; Grayson, Paul D.; Squires, Todd M.; Kondev, Jané; Phillips, Rob (2005). "Forces during Bacteriophage DNA Packaging and Ejection". Biophysical Journal. 88 (2): 851–866. arXiv:q-bio/0406022. Bibcode:2005BpJ....88..851P. doi:10.1529/biophysj.104.047134. PMC 1305160. PMID 15556983. <a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1305160" target="_blank">https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1305160</a> <a href="#fnref:5" class="footnote-back-ref">↩</a></p></li> <li id="fn:6"><p>Ng, Andy Ka-Leung; Wang, Jia-Huai; Shaw, Pang-Chui (2009-05-27). "Structure and sequence analysis of influenza A virus nucleoprotein". Science in China Series C: Life Sciences. 52 (5): 439–449. doi:10.1007/s11427-009-0064-x. ISSN 1006-9305. PMID 19471866. S2CID 610062. <a href="/wiki/Doi_(identifier)" target="_blank">/wiki/Doi_(identifier)</a> <a href="#fnref:6" class="footnote-back-ref">↩</a></p></li> <li id="fn:7"><p>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). "Crystal Structure of the Rabies Virus Nucleoprotein-RNA Complex". Science. 313 (5785): 360–363. Bibcode:2006Sci...313..360A. doi:10.1126/science.1125280. ISSN 0036-8075. PMID 16778023. S2CID 29937744. <a href="https://doi.org/10.1126%2Fscience.1125280" target="_blank">https://doi.org/10.1126%2Fscience.1125280</a> <a href="#fnref:7" class="footnote-back-ref">↩</a></p></li> <li id="fn:8"><p>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). "Nucleocapsid protein structures from orthobunyaviruses reveal insight into ribonucleoprotein architecture and RNA polymerization". Nucleic Acids Research. 41 (11): 5912–5926. doi:10.1093/nar/gkt268. ISSN 0305-1048. PMC 3675483. PMID 23595147. <a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3675483" target="_blank">https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3675483</a> <a href="#fnref:8" class="footnote-back-ref">↩</a></p></li> <li id="fn:9"><p>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). "Nucleocapsid protein structures from orthobunyaviruses reveal insight into ribonucleoprotein architecture and RNA polymerization". Nucleic Acids Research. 41 (11): 5912–5926. doi:10.1093/nar/gkt268. ISSN 0305-1048. PMC 3675483. PMID 23595147. <a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3675483" target="_blank">https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3675483</a> <a href="#fnref:9" class="footnote-back-ref">↩</a></p></li> <li id="fn:10"><p>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). "The crystal structure of the Hazara virus nucleocapsid protein". BMC Structural Biology. 15: 24. doi:10.1186/s12900-015-0051-3. ISSN 1472-6807. PMC 4696240. PMID 26715309. <a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4696240" target="_blank">https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4696240</a> <a href="#fnref:10" class="footnote-back-ref">↩</a></p></li> <li id="fn:11"><p>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). "Structure, Function, and Evolution of the Crimean-Congo Hemorrhagic Fever Virus Nucleocapsid Protein". Journal of Virology. 86 (20): 10914–10923. doi:10.1128/JVI.01555-12. ISSN 0022-538X. PMC 3457148. PMID 22875964. <a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3457148" target="_blank">https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3457148</a> <a href="#fnref:11" class="footnote-back-ref">↩</a></p></li> <li id="fn:12"><p>Qi, Xiaoxuan; Lan, Shuiyun; Wang, Wenjian; Schelde, Lisa McLay; Dong, Haohao; Wallat, Gregor D.; Ly, Hinh; Liang, Yuying; Dong, Changjiang (2010). "Cap binding and immune evasion revealed by Lassa nucleoprotein structure". Nature. 468 (7325): 779–783. Bibcode:2010Natur.468..779Q. doi:10.1038/nature09605. PMC 3057469. PMID 21085117. <a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3057469" target="_blank">https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3057469</a> <a href="#fnref:12" class="footnote-back-ref">↩</a></p></li> <li id="fn:13"><p>Deoxyribonucleoproteins at the U.S. National Library of Medicine Medical Subject Headings (MeSH) <a href="https://meshb.nlm.nih.gov/record/ui?name=Deoxyribonucleoproteins" target="_blank">https://meshb.nlm.nih.gov/record/ui?name=Deoxyribonucleoproteins</a> <a href="#fnref:13" class="footnote-back-ref">↩</a></p></li> <li id="fn:14"><p>Graeme K. Hunter G. K. (2000): Vital Forces. The discovery of the molecular basis of life. Academic Press, London 2000, ISBN 0-12-361811-8. <a href="/wiki/ISBN_(identifier)" target="_blank">/wiki/ISBN_(identifier)</a> <a href="#fnref:14" class="footnote-back-ref">↩</a></p></li> <li id="fn:15"><p>Nelson D. L., Michael M. Cox M. M. (2013): Lehninger Principles of Biochemistry. W. H. Freeman, ISBN 978-1-4641-0962-1. <a href="/wiki/ISBN_(identifier)" target="_blank">/wiki/ISBN_(identifier)</a> <a href="#fnref:15" class="footnote-back-ref">↩</a></p></li> <li id="fn:16"><p>Lodish, Harvey. Molecular Cell Biology. <a href="#fnref:16" class="footnote-back-ref">↩</a></p></li> <li id="fn:17"><p>Echols, Harrison (1990). "Nucleoprotein structures initiating DNA replication, transcription, and site-specific recombination". The Journal of Biological Chemistry. 265 (25): 14697–700. doi:10.1016/S0021-9258(18)77163-9. PMID 2203758. <a href="https://doi.org/10.1016%2FS0021-9258%2818%2977163-9" target="_blank">https://doi.org/10.1016%2FS0021-9258%2818%2977163-9</a> <a href="#fnref:17" class="footnote-back-ref">↩</a></p></li> <li id="fn:18"><p>Seitz EM, Brockman JP, Sandler SJ, Clark AJ, Kowalczykowski SC (1998). "RadA protein is an archaeal RecA protein homolog that catalyzes DNA strand exchange". Genes Dev. 12 (9): 1248–53. doi:10.1101/gad.12.9.1248. PMC 316774. PMID 9573041. <a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC316774" target="_blank">https://www.ncbi.nlm.nih.gov/pmc/articles/PMC316774</a> <a href="#fnref:18" class="footnote-back-ref">↩</a></p></li> <li id="fn:19"><p>Cox MM, Goodman MF, Kreuzer KN, Sherratt DJ, Sandler SJ, Marians KJ (2000). "The importance of repairing stalled replication forks". Nature. 404 (6773): 37–41. Bibcode:2000Natur.404...37C. doi:10.1038/35003501. PMID 10716434. S2CID 4427794. <a href="/wiki/Bibcode_(identifier)" target="_blank">/wiki/Bibcode_(identifier)</a> <a href="#fnref:19" class="footnote-back-ref">↩</a></p></li> <li id="fn:20"><p>Crickard JB, Kaniecki K, Kwon Y, Sung P, Greene EC (2018). "Spontaneous self-segregation of Rad51 and Dmc1 DNA recombinases within mixed recombinase filaments". J. Biol. Chem. 293 (11): 4191–4200. doi:10.1074/jbc.RA117.001143. PMC 5858004. PMID 29382724. <a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5858004" target="_blank">https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5858004</a> <a href="#fnref:20" class="footnote-back-ref">↩</a></p></li> <li id="fn:21"><p>Hogan, Daniel J; Riordan, Daniel P; Gerber, André P; Herschlag, Daniel; Brown, Patrick O (2016-11-07). "Diverse RNA-Binding Proteins Interact with Functionally Related Sets of RNAs, Suggesting an Extensive Regulatory System". PLOS Biology. 6 (10): e255. doi:10.1371/journal.pbio.0060255. ISSN 1544-9173. PMC 2573929. PMID 18959479. <a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2573929" target="_blank">https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2573929</a> <a href="#fnref:21" class="footnote-back-ref">↩</a></p></li> <li id="fn:22"><p>Lukong, Kiven E.; Chang, Kai-wei; Khandjian, Edouard W.; Richard, Stéphane (2008-08-01). "RNA-binding proteins in human genetic disease". Trends in Genetics. 24 (8): 416–425. doi:10.1016/j.tig.2008.05.004. ISSN 0168-9525. PMID 18597886. <a href="/wiki/Doi_(identifier)" target="_blank">/wiki/Doi_(identifier)</a> <a href="#fnref:22" class="footnote-back-ref">↩</a></p></li> <li id="fn:23"><p>"Ribonucleoprotein". www.uniprot.org. Retrieved 2016-11-07. <a href="https://www.uniprot.org/keywords/KW-0687" target="_blank">https://www.uniprot.org/keywords/KW-0687</a> <a href="#fnref:23" class="footnote-back-ref">↩</a></p></li> <li id="fn:24"><p>Bank, RCSB Protein Data. "RCSB Protein Data Bank - RCSB PDB". Archived from the original on 2015-04-18. Retrieved 2018-04-14. {{cite journal}}: Cite journal requires |journal= (help) <a href="https://web.archive.org/web/20150418160606/http://www.rcsb.org/pdb/home/home.do" target="_blank">https://web.archive.org/web/20150418160606/http://www.rcsb.org/pdb/home/home.do</a> <a href="#fnref:24" class="footnote-back-ref">↩</a></p></li> <li id="fn:25"><p>Lewis, Benjamin A.; Walia, Rasna R.; Terribilini, Michael; Ferguson, Jeff; Zheng, Charles; Honavar, Vasant; Dobbs, Drena (2016-11-07). "PRIDB: a protein–RNA interface database". Nucleic Acids Research. 39 (Database issue): D277 – D282. doi:10.1093/nar/gkq1108. ISSN 0305-1048. PMC 3013700. PMID 21071426. <a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3013700" target="_blank">https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3013700</a> <a href="#fnref:25" class="footnote-back-ref">↩</a></p></li> <li id="fn:26"><p>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". Methods. 65 (3): 310–319. doi:10.1016/j.ymeth.2013.09.014. ISSN 1095-9130. PMID 24083976. S2CID 37061678. <a href="/wiki/Doi_(identifier)" target="_blank">/wiki/Doi_(identifier)</a> <a href="#fnref:26" class="footnote-back-ref">↩</a></p></li> <li id="fn:27"><p>Baudin, F; Bach, C; Cusack, S; Ruigrok, R W (1994-07-01). "Structure of influenza virus RNP. I. Influenza virus nucleoprotein melts secondary structure in panhandle RNA and exposes the bases to the solvent". The EMBO Journal. 13 (13): 3158–3165. doi:10.1002/j.1460-2075.1994.tb06614.x. ISSN 0261-4189. PMC 395207. PMID 8039508. <a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC395207" target="_blank">https://www.ncbi.nlm.nih.gov/pmc/articles/PMC395207</a> <a href="#fnref:27" class="footnote-back-ref">↩</a></p></li> <li id="fn:28"><p>"Mixed Connective Tissue Disease (MCTD) | Cleveland Clinic". my.clevelandclinic.org. Retrieved 2016-11-07. <a href="http://my.clevelandclinic.org/health/diseases_conditions/hic_Mixed_Connective_Tissue_Disease" target="_blank">http://my.clevelandclinic.org/health/diseases_conditions/hic_Mixed_Connective_Tissue_Disease</a> <a href="#fnref:28" class="footnote-back-ref">↩</a></p></li> <li id="fn:29"><p>Lodish, Harvey. Molecular Cell Biology. <a href="#fnref:29" class="footnote-back-ref">↩</a></p></li> <li id="fn:30"><p>Ruigrok, Rob WH; Crépin, Thibaut; Kolakofsky, Dan (2011). "Nucleoproteins and nucleocapsids of negative-strand RNA viruses". Current Opinion in Microbiology. 14 (4): 504–510. doi:10.1016/j.mib.2011.07.011. PMID 21824806. <a href="/wiki/Doi_(identifier)" target="_blank">/wiki/Doi_(identifier)</a> <a href="#fnref:30" class="footnote-back-ref">↩</a></p></li> </ol>