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SNAP25
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<h2 id="structure-and-function">Structure and function</h2> <p>SNAP-25, a <a href="/facts/Q-SNARE/DaJQkGYp">Q-SNARE</a> protein, is anchored to the <a href="/facts/Cytosol/VyXgygWm">cytosolic</a> face of <a href="/facts/Cell_membrane/vAXSD0DT">membranes</a> via <a href="/facts/Palmitoyl_chain/soDel1Xt">palmitoyl side chains</a> covalently bound to <a href="/facts/Cysteine/kbqvUm6d">cysteine</a> amino acid residues in the central linker domain of the <a href="/facts/Molecule/N9ljSfFq">molecule</a>. This means that SNAP-25 does not contain a <a href="/facts/Transmembrane_domain/D1j0PwSR">trans-membrane domain</a>.<a class="footnote-ref" id="fnref:4" href="#fn:4"><sup>4</sup></a> </p><p>SNAP-25 has been identified to contribute two<a class="footnote-ref" id="fnref:5" href="#fn:5"><sup>5</sup></a> <a href="/facts/%25CE%2591-helices/7CESPIYJ">α-helices</a> to the <a href="/facts/SNARE_(protein)/DaJQkGYp">SNARE complex</a>, a four-α-helix domain complex.<a class="footnote-ref" id="fnref:6" href="#fn:6"><sup>6</sup></a> The SNARE complex participates in <a href="/facts/Vesicle_fusion/aksya4JS">vesicle fusion</a>, which involves the docking, priming and merging of a <a href="/facts/Vesicle_(biology_and_chemistry)/1KjHpjMM">vesicle</a> with the <a href="/facts/Cell_membrane/vAXSD0DT">cell membrane</a> to initiate an <a href="/facts/Exocytosis/4P4oQdtA">exocytotic</a> event. <a href="/facts/Synaptobrevin/qu2VzN6H">Synaptobrevin</a>, a protein that is a part of the <a href="/facts/Vesicle-associated_membrane_protein/jnv51xBn">vesicle-associated membrane protein</a> (VAMP) family, and <a href="/facts/Syntaxin/35y4hWCo">syntaxin-1</a> also help form the SNARE complex by each contributing a single α-helix. SNAP-25 assembles with synaptobrevin and syntaxin-1, and the selective binding of these proteins enables vesicle docking and fusion to occur at active zones on the plasma membrane.<a class="footnote-ref" id="fnref:7" href="#fn:7"><sup>7</sup></a> The energy needed for fusion to occur, results from the assembly of the SNARE proteins along with additional Sec1/Munc18-like (SM) proteins.<a class="footnote-ref" id="fnref:8" href="#fn:8"><sup>8</sup></a> </p><p>To form the SNARE complex, synaptobrevin, syntaxin-1, and SNAP-25 associate and begin to wrap around each other to form a <a href="/facts/Coiled_coil/U0YEzcB4">coiled coil</a> <a href="/facts/Protein_quaternary_structure/ukuyKJfj">quaternary structure</a>. The α-helices of both synaptobrevin and syntaxin-1 bind to those of SNAP-25. Synaptobrevin binds the α-helix near the <a href="/facts/C-terminus/ws4scHgT">C-terminus</a> of SNAP-25, while syntaxin-1 binds the α-helix near the <a href="/facts/N-terminus/yKYpuaBJ">N-terminus</a>.<a class="footnote-ref" id="fnref:9" href="#fn:9"><sup>9</sup></a> Dissociation of the SNARE complex is driven by ATPase <i>N</i>-ethylmaleimide-sensitive fusion (NSF) protein.<a class="footnote-ref" id="fnref:10" href="#fn:10"><sup>10</sup></a> </p><p>SNAP-25 inhibits <a href="/facts/Chemical_synapse/M1x5rhz7">presynaptic</a> <a href="/facts/P-type_calcium_channel/YNyJ4B8D">P-</a>, <a href="/facts/Q-type_calcium_channel/zbbrAFhL">Q-</a>, and <a href="/facts/L-type_calcium_channel/4vbqP8B7">L-type</a> <a href="/facts/Voltage-gated_calcium_channel/H9nAybJJ">voltage-gated calcium channels</a><a class="footnote-ref" id="fnref:11" href="#fn:11"><sup>11</sup></a> and interacts with the <a href="/facts/Synaptotagmin/W95BhCN5">synaptotagmin</a> C2B domain in a <a href="/facts/Calcium/hf252CC0">Ca2+</a>-independent fashion.<a class="footnote-ref" id="fnref:12" href="#fn:12"><sup>12</sup></a> In <a href="/facts/Glutamate/7oXbNcvu">glutamatergic</a> <a href="/facts/Synapse/vdMRJCUn">synapses</a>, SNAP-25 decreases the Ca2+ responsiveness, while it is normally absent in <a href="/facts/GABA/vRTeQQUG">GABAergic</a> synapses.<a class="footnote-ref" id="fnref:13" href="#fn:13"><sup>13</sup></a> </p><p>Two <a href="/facts/Protein_isoform/oWmzfg4l">isoforms</a> (<a href="/facts/MRNA/oUL6qxQn">mRNA</a> <a href="/facts/Alternative_splicing/nNRwPVNK">splice variants</a>) of SNAP-25 exist, which are SNAP-25a and SNAP-25b. The two isoforms differ by nine <a href="/facts/Amino_acid/WDxYwBny">amino acid</a> residues, including a re-localization of one of the four palmitoylated cysteine residues involved in membrane attachment.<a class="footnote-ref" id="fnref:14" href="#fn:14"><sup>14</sup></a> The major characteristics of these two forms are outlined in the table below. </p> <table><tbody><tr><th></th><th>SNAP25a</th><th>SNAP25b</th></tr><tr><td>Structure</td><td>N-terminal α-helix<p>Random coil linker region with four cysteines clustered towards the center</p><p>C-terminal α-helix</p></td><td>N-terminal α-helix<p>Random coil linker region with four cysteines clustered towards the C-terminus</p><p>C-terminal α-helix</p></td></tr><tr><td>Expression</td><td>Major SNAP-25 isoform in embryos and developing neural tissue<p>Minimal expression in adult tissue except in pituitary and adrenal gland tissues</p></td><td>Minimal expression during development, major isoform in adult neural tissue<a class="footnote-ref" id="fnref:15" href="#fn:15"><sup>15</sup></a></td></tr><tr><td>Localization</td><td>Diffuse</td><td>Localized to terminals and varicosities<a class="footnote-ref" id="fnref:16" href="#fn:16"><sup>16</sup></a></td></tr></tbody></table> <p>SNAP-25 not only plays a role in <a href="/facts/Synaptogenesis/1fVRWK6e">synaptogenesis</a> and the exocytotic release of neurotransmitters, but it also affects spine morphogenesis and density, post synaptic receptor trafficking and neuronal plasticity. Other non-neuronal processes such as metabolism can also be affected by SNAP-25 protein expression.<a class="footnote-ref" id="fnref:17" href="#fn:17"><sup>17</sup></a><a class="footnote-ref" id="fnref:18" href="#fn:18"><sup>18</sup></a> </p> <h2 id="clinical-significance">Clinical significance</h2> <h3>Developmental and epileptic encephalopathies (DEEs)</h3> <p>Individuals harboring pathogenic heterozygous <i>de novo</i> missense or loss-of-function variants in SNAP-25 often present with an early-onset developmental and epileptic encephalopathy. The core symptoms comprise intellectual disability ranging between mild to profound and early-onset seizures mostly occurring before the age of two years. Further recurrent symptoms include movement disorders, cerebral visual impairment, and brain atrophy.<a class="footnote-ref" id="fnref:19" href="#fn:19"><sup>19</sup></a> Electrophysiological studies identified aberrant spontaneous neurotransmission as causative and suggest that structurally clustered pathogenic variants lead to similar synaptic phenotypes.<a class="footnote-ref" id="fnref:20" href="#fn:20"><sup>20</sup></a> </p> <h3>Attention Deficit Hyperactivity Disorder (ADHD)</h3> <p>Consistent with the regulation of synaptic Ca2+ responsiveness, heterozygous deletion of the SNAP-25 gene in mice results in a hyperactive phenotype similar to <a href="/facts/Attention-deficit_hyperactivity_disorder/uSqjIyhd">attention deficit hyperactivity disorder (ADHD)</a>. In heterozygous mice, a decrease in hyperactivity is observed with <a href="/facts/Dextroamphetamine/SoVP3mKN">dextroamphetamine</a> (or Dexedrine), an active ingredient in the ADHD drug <a href="/facts/Adderall/87QufGGT">Adderall</a>. Homozygous deletions of the SNAP-25 gene are lethal. An additional study indicated that incorporation of a SNAP-25 <a href="/facts/Transgene/8DvIYSGt">transgene</a> back into the heterozygous SNAP-25 mutant mouse can rescue normal activity levels similar to wildtype mice. This suggests that low protein levels of SNAP-25 can be a cause of hyper-kinetic behavior.<a class="footnote-ref" id="fnref:21" href="#fn:21"><sup>21</sup></a> Subsequent studies have suggested that at least some of the SNAP-25 gene mutations in humans might predispose to ADHD.<a class="footnote-ref" id="fnref:22" href="#fn:22"><sup>22</sup></a><a class="footnote-ref" id="fnref:23" href="#fn:23"><sup>23</sup></a> Identification of polymorphisms in the 3’ untranslated region of the SNAP-25 gene was established in linkage studies with families that had been pre-diagnosed ADHD.<a class="footnote-ref" id="fnref:24" href="#fn:24"><sup>24</sup></a> </p> <h3>Schizophrenia</h3> <p>Studies in the post mortem brains of patients with Schizophrenia have shown that altered protein levels of SNAP-25 are specific to regions of the brain. Reduced SNAP-25 protein expression has been observed in the hippocampus as well as an area of the frontal lobe known as Broadman's area 10 whereas SNAP-25 expression has increased in both the cingulate cortex and prefrontal lobe of Broadman's area 9. The varying levels of SNAP-25 protein found in different areas of the brain have been thought to contribute to the conflicting psychological behaviors (depressive vs. hyperactive) expressed in some Schizophrenic patients.<a class="footnote-ref" id="fnref:25" href="#fn:25"><sup>25</sup></a><a class="footnote-ref" id="fnref:26" href="#fn:26"><sup>26</sup></a><a class="footnote-ref" id="fnref:27" href="#fn:27"><sup>27</sup></a><a class="footnote-ref" id="fnref:28" href="#fn:28"><sup>28</sup></a> </p><p>The blind-drunk (Bdr) mouse model which has a point mutations in the SNAP-25b protein has provided a complex phenotype involving behaviors such as an abnormal circadian rhythm,<a class="footnote-ref" id="fnref:29" href="#fn:29"><sup>29</sup></a> uncoordinated gait, and disinterest in new objects/toys.<a class="footnote-ref" id="fnref:30" href="#fn:30"><sup>30</sup></a> Another mouse model generated from <a href="/facts/Cre-Lox_recombination/Ha9d2CKT">Cre-LoxP recombination</a>, showed that conditional knockout (cKO) of the SNAP-25 gene in the forebrain, showed inactive SNAP-25 gene expression in glutamatergic neurons. However, significant glutamate levels were found in the cortex of these cKO mice.<a class="footnote-ref" id="fnref:31" href="#fn:31"><sup>31</sup></a> These mice also exhibited deficient social skills, impaired learning and memory, enhanced kinesthetic activity, a reduced startle response, impaired self-care, nursing ability and nest-building skills. Antipsychotic drugs such as Clozapine and Riluzole have been shown to significantly reduce the schizophrenic phenotype expressed in SNAP-25 cKO mice.<a class="footnote-ref" id="fnref:32" href="#fn:32"><sup>32</sup></a> </p> <h3>Alzheimer's disease</h3> <p>Individuals with Alzhiemer's disease have been shown to have decreased presynaptic protein levels and impaired synaptic function in neurons. SNAP-25 can be used as a biomarker in the cerebral spinal fluid (CSF) of patients exhibiting different variations of Alzheimer's disease (prodromal Alzheimer's and overt Alzheimer's). Increased levels of SNAP-25 protein were observed in patients with Alzheimer's compared to control individuals. Additionally, the presence of truncated SNAP-25 protein can be seen in the CSF of some patients with this disease. <a class="footnote-ref" id="fnref:33" href="#fn:33"><sup>33</sup></a> In five distinct regions of the brain, low levels of SNAP-25 can be seen in patients with Alzheimer's.<a class="footnote-ref" id="fnref:34" href="#fn:34"><sup>34</sup></a> </p> <h3>Bipolar disorder</h3> <p>A <a href="/facts/Single-nucleotide_polymorphism/Qy5Y2wom">single nucleotide polymorphism</a> in the SNAP-25 gene <a href="/facts/Promoter_(genetics)/YDYBzLfg">promoter</a> has been shown to influence the expression levels of the SNAP-25b isoform in the prefrontal cortex. Increased levels of SNAP-25b have been shown to impair synaptic transmission and maturation which could lead to early-onset bipolar disorder (EOBD).The most abundant isoform of SNAP-25 is SNAP-25a during the early weeks of development in mice however in adulthood there is a change and the SNAP-25b isoform increases in the brain. This is shown to correlate with adolescent humans being increasingly diagnosed with EOBD during puberty.<a class="footnote-ref" id="fnref:35" href="#fn:35"><sup>35</sup></a> It has been suggested that early-onset bipolar disorder is more closely linked to Schizophrenia than to Bipolar Disorder itself. The single nucleotide polymorphism of SNAP-25 (rs6039769) associated with EOBD has been shown to increase the risk of patients developing Schizophrenia.<a class="footnote-ref" id="fnref:36" href="#fn:36"><sup>36</sup></a> </p> <h3>Botulism</h3> <p>A genome wide association study pointed to the rs362584 polymorphism in the gene as possibly associated with the personality trait <a href="/facts/Neuroticism/tmhrDpUS">neuroticism</a>.<a class="footnote-ref" id="fnref:37" href="#fn:37"><sup>37</sup></a> <a href="/facts/Botulin_toxin/F2LTx09G">Botulinum toxins A, C and E</a> cleave SNAP-25,<a class="footnote-ref" id="fnref:38" href="#fn:38"><sup>38</sup></a> leading to <a href="/facts/Paralysis/Sh1Rqr8R">paralysis</a> in clinically developed <a href="/facts/Botulism/7Jpsrcqv">botulism</a>. </p> <h3>Epilepsy</h3> <p>Deletion of the SNAP-25b isoform has been shown to cause developmental abnormalities and seizures in mice. High levels of SNAP-25a and the protein syntaxin appear to be linked to seizures found in infantile-epilepsy. SNAP-25 <a href="/facts/Knock-in/khSPPo1d">knock-in</a> mice have distinct phenotypic behavior similar to the fits and seizures of epileptic patients, as well as anxiety.<a class="footnote-ref" id="fnref:39" href="#fn:39"><sup>39</sup></a> </p> <h3>Learning disabilities</h3> <p>In the coloboma hyperactive mutant mouse model where SNAP-25 protein levels are reduced to 50% of the normal level, depolarized neurotransmitter release of dopamine and serotonin were reduced as well as glutamate release. The reduction in glutamate levels can lead to deficient memory and increased learning disabilities.<a class="footnote-ref" id="fnref:40" href="#fn:40"><sup>40</sup></a> Certain polymorphisms of SNAP-25 (rs363043, rs353016, rs363039, rs363050) have been shown to affect the cognitive behavior, specifically the Intelligence Quotient (IQ)), of patients without pre-existing neurological diseases.<a class="footnote-ref" id="fnref:41" href="#fn:41"><sup>41</sup></a> </p> <h3>Neonatal development</h3> <p>SNAP-25 protein expression can be altered by sex hormone levels in neonatal rats. Male rats that received an antiestrogen drug showed a 30% decrease in SNAP-25 levels and females treated with estrogen or testosterone showed a 30% increase in SNAP-25 levels.<a class="footnote-ref" id="fnref:42" href="#fn:42"><sup>42</sup></a> This suggests that synaptosomal proteins, such as SNAP-25, may have a dependence on neonatal hormone levels during brain development in rats. An additional study, showed that SNAP-25 levels in the hippocampus of the brain in neonatal mice were altered if the mother had been exposed to human influenza virus during pregnancy.<a class="footnote-ref" id="fnref:43" href="#fn:43"><sup>43</sup></a> </p> <h2 id="impact-in-other-non-humans">Impact in other non-humans</h2> <p>Loss is lethal to <i><a href="/facts/Drosophila/P4K7RkJl">Drosophila</a></i>, but can be fully substituted by overexpression of the related SNAP-24.<a class="footnote-ref" id="fnref:44" href="#fn:44"><sup>44</sup></a> </p> <h2 id="interactive-pathway-map">Interactive pathway map</h2> <p><i>Click on genes, proteins and metabolites below to link to respective articles.</i><a class="footnote-ref" id="fnref:45" href="#fn:45"><sup>45</sup></a> </p> <h2 id="interactions">Interactions</h2> <p>SNAP-25 has been shown to <a href="/facts/Protein-protein_interaction/etvm9Wmg">interact</a> with: </p> <ul><li><a href="/facts/CPLX1/mKffejVN">CPLX1</a>,<a class="footnote-ref" id="fnref:46" href="#fn:46"><sup>46</sup></a><a class="footnote-ref" id="fnref:47" href="#fn:47"><sup>47</sup></a></li> <li><a href="/facts/ITSN1/gkCGRBPg">ITSN1</a>,<a class="footnote-ref" id="fnref:48" href="#fn:48"><sup>48</sup></a></li> <li><a href="/facts/KIF5B/YLXXnATx">KIF5B</a>,<a class="footnote-ref" id="fnref:49" href="#fn:49"><sup>49</sup></a></li> <li><a href="/facts/SNAPAP/IpnlwRfW">SNAPAP</a><a class="footnote-ref" id="fnref:50" href="#fn:50"><sup>50</sup></a> and</li> <li><a href="/facts/STX11/zSy1ex1S">STX11</a>,<a class="footnote-ref" id="fnref:51" href="#fn:51"><sup>51</sup></a><a class="footnote-ref" id="fnref:52" href="#fn:52"><sup>52</sup></a></li> <li><a href="/facts/STX1A/dpd1ts4e">STX1A</a>,<a class="footnote-ref" id="fnref:53" href="#fn:53"><sup>53</sup></a><a class="footnote-ref" id="fnref:54" href="#fn:54"><sup>54</sup></a><a class="footnote-ref" id="fnref:55" href="#fn:55"><sup>55</sup></a><a class="footnote-ref" id="fnref:56" href="#fn:56"><sup>56</sup></a><a class="footnote-ref" id="fnref:57" href="#fn:57"><sup>57</sup></a><a class="footnote-ref" id="fnref:58" href="#fn:58"><sup>58</sup></a><a class="footnote-ref" id="fnref:59" href="#fn:59"><sup>59</sup></a><a class="footnote-ref" id="fnref:60" href="#fn:60"><sup>60</sup></a><a class="footnote-ref" id="fnref:61" href="#fn:61"><sup>61</sup></a><a class="footnote-ref" id="fnref:62" href="#fn:62"><sup>62</sup></a><a class="footnote-ref" id="fnref:63" href="#fn:63"><sup>63</sup></a></li> <li><a href="/facts/STX2/TSUNyons">STX2</a>,<a class="footnote-ref" id="fnref:64" href="#fn:64"><sup>64</sup></a><a class="footnote-ref" id="fnref:65" href="#fn:65"><sup>65</sup></a></li> <li><a href="/facts/STX4/VGQSYHH0">STX4</a>,<a class="footnote-ref" id="fnref:66" href="#fn:66"><sup>66</sup></a><a class="footnote-ref" id="fnref:67" href="#fn:67"><sup>67</sup></a><a class="footnote-ref" id="fnref:68" href="#fn:68"><sup>68</sup></a><a class="footnote-ref" id="fnref:69" href="#fn:69"><sup>69</sup></a></li> <li><a href="/facts/SYT1/amq8lfyc">SYT1</a>,<a class="footnote-ref" id="fnref:70" href="#fn:70"><sup>70</sup></a><a class="footnote-ref" id="fnref:71" href="#fn:71"><sup>71</sup></a></li> <li><a href="/facts/Syntaxin_3/UguKoKBm">Syntaxin 3</a>,<a class="footnote-ref" id="fnref:72" href="#fn:72"><sup>72</sup></a><a class="footnote-ref" id="fnref:73" href="#fn:73"><sup>73</sup></a><a class="footnote-ref" id="fnref:74" href="#fn:74"><sup>74</sup></a></li> <li><a href="/facts/TRIM9/orIVF8XD">TRIM9</a>,<a class="footnote-ref" id="fnref:75" href="#fn:75"><sup>75</sup></a> and</li> <li><a href="/facts/VAMP2/oY6rIr9x">VAMP2</a>.<a class="footnote-ref" id="fnref:76" href="#fn:76"><sup>76</sup></a><a class="footnote-ref" id="fnref:77" href="#fn:77"><sup>77</sup></a><a class="footnote-ref" id="fnref:78" href="#fn:78"><sup>78</sup></a></li> <li><a href="/facts/Synaptotagmin/W95BhCN5">Synaptotagmin</a> binds SNAP-25 and syntaxins in the presence of <a href="/facts/Calcium/hf252CC0">Ca</a>2+ (and thus the entire SNARE complex)<a class="footnote-ref" id="fnref:79" href="#fn:79"><sup>79</sup></a></li></ul> <h2 id="further-reading">Further reading</h2> <ul><li>Hanson PI, Otto H, Barton N, Jahn R (July 1995). <a href="https://doi.org/10.1074%2Fjbc.270.28.16955">"The N-ethylmaleimide-sensitive fusion protein and alpha-SNAP induce a conformational change in syntaxin"</a>. <i>The Journal of Biological Chemistry</i>. 270 (28): 16955–61. <a href="/facts/Doi_(identifier)/muM9Etpq">doi</a>:<a href="https://doi.org/10.1074%2Fjbc.270.28.16955">10.1074/jbc.270.28.16955</a>. <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/7622514">7622514</a>.</li> <li>Hata Y, Südhof TC (June 1995). <a href="https://doi.org/10.1074%2Fjbc.270.22.13022">"A novel ubiquitous form of Munc-18 interacts with multiple syntaxins. Use of the yeast two-hybrid system to study interactions between proteins involved in membrane traffic"</a>. <i>The Journal of Biological Chemistry</i>. 270 (22): 13022–8. <a href="/facts/Doi_(identifier)/muM9Etpq">doi</a>:<a href="https://doi.org/10.1074%2Fjbc.270.22.13022">10.1074/jbc.270.22.13022</a>. <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/7768895">7768895</a>.</li> <li>Chapman ER, An S, Barton N, Jahn R (November 1994). <a href="https://doi.org/10.1016%2FS0021-9258%2818%2947003-2">"SNAP-25, a t-SNARE which binds to both syntaxin and synaptobrevin via domains that may form coiled coils"</a>. <i>The Journal of Biological Chemistry</i>. 269 (44): 27427–32. <a href="/facts/Doi_(identifier)/muM9Etpq">doi</a>:<a href="https://doi.org/10.1016%2FS0021-9258%2818%2947003-2">10.1016/S0021-9258(18)47003-2</a>. <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/7961655">7961655</a>.</li> <li>Zhao N, Hashida H, Takahashi N, Sakaki Y (August 1994). "Cloning and sequence analysis of the human SNAP25 cDNA". <i>Gene</i>. 145 (2): 313–4. <a href="/facts/Doi_(identifier)/muM9Etpq">doi</a>:<a href="https://doi.org/10.1016%2F0378-1119%2894%2990027-2">10.1016/0378-1119(94)90027-2</a>. <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/8056350">8056350</a>.</li> <li>Bark IC, Wilson MC (February 1994). "Human cDNA clones encoding two different isoforms of the nerve terminal protein SNAP-25". <i>Gene</i>. 139 (2): 291–2. <a href="/facts/Doi_(identifier)/muM9Etpq">doi</a>:<a href="https://doi.org/10.1016%2F0378-1119%2894%2990773-0">10.1016/0378-1119(94)90773-0</a>. <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/8112622">8112622</a>.</li> <li>Maruyama K, Sugano S (January 1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides". <i>Gene</i>. 138 (1–2): 171–4. <a href="/facts/Doi_(identifier)/muM9Etpq">doi</a>:<a href="https://doi.org/10.1016%2F0378-1119%2894%2990802-8">10.1016/0378-1119(94)90802-8</a>. <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/8125298">8125298</a>.</li> <li>Maglott DR, Feldblyum TV, Durkin AS, Nierman WC (May 1996). 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