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S100A1
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<h2 id="structure">Structure</h2> <p>S100A1 is a member of the <a href="/facts/S-100_protein/NEVdr8Ue">S100 family</a> of proteins expressed in <a href="/facts/Cardiac_muscle/oMqU4Sdu">cardiac muscle</a>, <a href="/facts/Skeletal_muscle/en1tVYFN">skeletal muscle</a> and brain,<a class="footnote-ref" id="fnref:3" href="#fn:3"><sup>3</sup></a> with highest density at <a href="/facts/Sarcomere/9jQ5DaTz">Z-lines</a> and <a href="/facts/Sarcoplasmic_reticulum/5tSqPRlk">sarcoplasmic reticulum</a>.<a class="footnote-ref" id="fnref:4" href="#fn:4"><sup>4</sup></a> S100A1 contains 4 <a href="/facts/EF-hand/UVAqabCP">EF-hand</a> <a href="/facts/Calcium/hf252CC0">calcium</a>-binding <a href="/facts/Structural_motif/g8EBDBGW">motifs</a> in its dimerized form,<a class="footnote-ref" id="fnref:5" href="#fn:5"><sup>5</sup></a> and can exist as either a hetero or homo<a href="/facts/Protein_dimer/c8LwFJPG">dimer</a>. The S100A1 homodimer is high affinity (nanomolar range or tighter), and is formed through <a href="/facts/Hydrophobic/Ifya0CXQ">hydrophobic</a> packing of an X-type 4-helix bundle created between helices 1, 1', 4, and 4'. <a href="/facts/Protein_nuclear_magnetic_resonance_spectroscopy/lCIXAFzQ">Protein nuclear magnetic resonance spectroscopy</a> structural information on the homodimeric form of this protein shows that each monomer is helical and contains two <a href="/facts/EF_hand/UVAqabCP">EF-hand calcium-binding loops</a>; one in the <a href="/facts/N-terminus/yKYpuaBJ">N-terminus</a> and a canonical <a href="/facts/EF_hand/UVAqabCP">EF hand</a> in the <a href="/facts/C-terminus/ws4scHgT">C-terminus</a> having higher <a href="/facts/Calcium/hf252CC0">calcium</a> affinity (<a href="/facts/Dissociation_constant/uvaKXf26">dissociation constant</a> of roughly 20 micromolar). The two <a href="/facts/EF_hand/UVAqabCP">EF hand</a> domains neighbor each other in three dimensional space, and are connected to each other through a short <a href="/facts/Beta_sheet/B6mwwR6H">beta sheet</a> region (residues 27–29 and 68–70). </p><p>Upon binding calcium, helix 3 of S100A1 re-orients from being relatively antiparallel to <a href="/facts/Alpha_helix/7CESPIYJ">helix</a> 4 to being roughly perpendicular. This conformational change is different from most <a href="/facts/EF_hand/UVAqabCP">EF hands</a>, in that the entering helix, and not the exiting helix, moves. This conformational change exposes a large hydrophobic pocket between helix 3, 4, and the hinge region of S100A1 that is involved in virtually all <a href="/facts/Calcium/hf252CC0">calcium</a>-dependent target protein interactions. These biophysical properties seem to be well conserved across the S100 family of proteins. Helix 3, 4, and the hinge region are the most divergent areas between individual S100 proteins, and so it is likely that the sequence of these regions is pivotal in fine-tuning calcium-dependent target binding by S100 proteins.<a class="footnote-ref" id="fnref:6" href="#fn:6"><sup>6</sup></a> <a href="/facts/S-Nitrosylation/Lcxa7IIu">S-Nitrosylation</a> of S100A1 at <a href="/facts/Cysteine/kbqvUm6d">Cys</a>85 reorganizes the conformation of S100A1 at the <a href="/facts/C-terminus/ws4scHgT">C-terminal</a> helix and the linker connecting the two <a href="/facts/EF_hand/UVAqabCP">EF hand</a> domains.<a class="footnote-ref" id="fnref:7" href="#fn:7"><sup>7</sup></a> </p><p>The most accurate high-resolution solution structure of human apo-S100A1 protein (PDB accession code: 2L0P) has been determined by means of NMR spectroscopy in 2011.<a class="footnote-ref" id="fnref:8" href="#fn:8"><sup>8</sup></a> </p><p>S100 genes include at least 19 members which are located as a cluster on chromosome 1q21.<a class="footnote-ref" id="fnref:9" href="#fn:9"><sup>9</sup></a><a class="footnote-ref" id="fnref:10" href="#fn:10"><sup>10</sup></a> </p> <h2 id="function">Function</h2> <p>S100 proteins are localized in the <a href="/facts/Cytoplasm/Wa0sE6xf">cytoplasm</a> and/or <a href="/facts/Cell_nucleus/D7sFRa3c">nucleus</a> of a wide range of cells, and involved in the regulation of a number of cellular processes such as <a href="/facts/Cell_cycle/nLMT7K4r">cell cycle</a> progression and <a href="/facts/Cellular_differentiation/bCVqUG7w">differentiation</a>. This protein may function in stimulation of Ca2+-induced Ca2+ release, inhibition of <a href="/facts/Microtubule/ENL1TxSe">microtubule</a> assembly, and inhibition of <a href="/facts/Protein_kinase_C/6WSQgAWv">protein kinase C</a>-mediated <a href="/facts/Phosphorylation/LXUEEeIL">phosphorylation</a>. </p><p>S100A1 is expressed during development in the primitive heart at embryonic day 8 in levels that are similar between <a href="/facts/Atrium_(heart)/eYNg8Vw2">atria</a> and <a href="/facts/Ventricle_(heart)/FCzV1xm7">ventricles</a>. As development progresses up to embryonic day 17.5, S100A1 expression shifts to a lower levels in <a href="/facts/Atrium_(heart)/eYNg8Vw2">atria</a> and higher levels in <a href="/facts/Cardiac_ventricle/FCzV1xm7">ventricular</a> <a href="/facts/Myocardium/oMqU4Sdu">myocardium</a>.<a class="footnote-ref" id="fnref:11" href="#fn:11"><sup>11</sup></a> </p><p>S100A1 has shown to be a regulator of myocardial contractility. S100A1 overexpression via <a href="/facts/Adenovirus/JLX5IKHt">adenoviral</a> gene transfer in adult rabbit <a href="/facts/Cardiomyocyte/fE40oTQz">cardiomyocytes</a> or a cardiac-restricted S100A1 murine transgenic enhanced <a href="/facts/Contractility/e4A65oky">cardiac contractile performance</a> by increasing <a href="/facts/Sarcoplasmic_reticulum/5tSqPRlk">sarcoplasmic reticular</a> <a href="/facts/Calcium/hf252CC0">calcium</a> transients and uptake, altering the <a href="/facts/Calcium/hf252CC0">calcium</a> sensitivity and cooperativity of <a href="/facts/Myofibril/uGRRhxms">myofibrils</a>, enhancing <a href="/facts/ATP2A2/pqscn3GG">SERCA2A</a> activity and enhancing <a href="/facts/Calcium-induced_calcium_release/SjR36J5K">calcium-induced calcium release</a>.<a class="footnote-ref" id="fnref:12" href="#fn:12"><sup>12</sup></a><a class="footnote-ref" id="fnref:13" href="#fn:13"><sup>13</sup></a><a class="footnote-ref" id="fnref:14" href="#fn:14"><sup>14</sup></a> Specifically, S100A1 increases the gain of <a href="/facts/Excitation-contraction_coupling/EbloCYfV">excitation-contraction coupling</a><a class="footnote-ref" id="fnref:15" href="#fn:15"><sup>15</sup></a> and decreases calcium spark frequency<a class="footnote-ref" id="fnref:16" href="#fn:16"><sup>16</sup></a> in <a href="/facts/Cardiomyocytes/fE40oTQz">cardiomyocytes</a>. Enhancement of <a href="/facts/L-type_calcium_channel/4vbqP8B7">L-type calcium channel</a> trans<a href="/facts/Sarcolemma/s62stjxE">sarcolemmal</a> <a href="/facts/Calcium/hf252CC0">calcium</a> influx by S100A has been shown to be dependent on <a href="/facts/Protein_kinase_A/kaKoYfbp">protein kinase A</a>.<a class="footnote-ref" id="fnref:17" href="#fn:17"><sup>17</sup></a> Effects of S100A1 on myofilament proteins may be via <a href="/facts/Titin/w6yGjgcx">Titin</a>; S100A1 has been shown to interact with the <a href="/facts/PEVK_region/w6yGjgcx">PEVK region</a> of <a href="/facts/Titin/w6yGjgcx">Titin</a> in a <a href="/facts/Calcium/hf252CC0">calcium</a>-dependent manner, and its binding reduces the force in an in vitro motility assay, suggesting that S100A may modulate <a href="/facts/Titin/w6yGjgcx">Titin</a>-based passive tension prior to <a href="/facts/Systole/5KDbjw4B">systole</a>.<a class="footnote-ref" id="fnref:18" href="#fn:18"><sup>18</sup></a><a class="footnote-ref" id="fnref:19" href="#fn:19"><sup>19</sup></a> In mice with ablation of the S100A1 gene (S100A1-/-), cardiac reserve upon <a href="/facts/Adrenergic_receptor/uoAeJbcN">beta adrenergic stimulation</a> was impaired, showing reduced <a href="/facts/Cardiac_contractility/0BdQPIsv">contraction rate</a> and relaxation rate, as well as reduced <a href="/facts/Calcium/hf252CC0">calcium</a> sensitivity. However, S100A1-/- did not show the eventual <a href="/facts/Cardiac_hypertrophy/YNcQhDVE">cardiac hypertrophy</a> or chamber dilation in aged mice.<a class="footnote-ref" id="fnref:20" href="#fn:20"><sup>20</sup></a> </p><p>In animal models of disease, S100A1 <a href="/facts/Protein/Jxmagu3E">protein</a> levels has been shown to be altered in <a href="/facts/Right_ventricle/FCzV1xm7">right ventricular</a> <a href="/facts/Cardiac_hypertrophy/YNcQhDVE">hypertrophied</a> tissue in a model of <a href="/facts/Pulmonary_hypertension/4848aBJl">pulmonary hypertension</a>;<a class="footnote-ref" id="fnref:21" href="#fn:21"><sup>21</sup></a> several tissue types (<a href="/facts/Brain/EKla9NkJ">brain</a>, <a href="/facts/Skeletal_muscle/en1tVYFN">skeletal muscle</a> and <a href="/facts/Cardiac_muscle/oMqU4Sdu">cardiac muscle</a>) in a model of <a href="/facts/Type_I_diabetes_mellitus/IkuQadGx">type I diabetes mellitus</a>;<a class="footnote-ref" id="fnref:22" href="#fn:22"><sup>22</sup></a> S100A1 has been demonstrated as a regulator of the genetic program underlying <a href="/facts/Cardiac_hypertrophy/YNcQhDVE">cardiac hypertrophy</a>, in that S100A1 inhibits alpha1 <a href="/facts/Adrenergic_receptor/uoAeJbcN">adrenergic stimulation</a> of <a href="/facts/Cardiac_hypertrophy/YNcQhDVE">hypertrophic</a> genes, including <a href="/facts/MYH7/X7Rx98KX">MYH7</a>, <a href="/facts/ACTA1/s1bl1ta3">ACTA1</a> and <a href="/facts/S100B/dhSpGQRz">S100B</a>.<a class="footnote-ref" id="fnref:23" href="#fn:23"><sup>23</sup></a> In a rat model of <a href="/facts/Myocardial_infarction/xoGw0qcG">myocardial infarction</a>, intracoronary S100A1 <a href="/facts/Adenovirus/JLX5IKHt">adenoviral</a> gene transfer restored <a href="/facts/Sarcoplasmic_reticulum/5tSqPRlk">sarcoplasmic reticular</a> <a href="/facts/Calcium/hf252CC0">calcium</a> transients and load, normalized intracellular <a href="/facts/Sodium/eYuSPu2V">sodium</a> concentrations, reversed the pathologic expression of the fetal gene program, restored energy supply, normalized contractile function, preserved inotropic reserve, and reduced <a href="/facts/Cardiac_hypertrophy/YNcQhDVE">cardiac hypertrophy</a> 1 week post-<a href="/facts/Myocardial_infarction/xoGw0qcG">myocardial infarction</a>.<a class="footnote-ref" id="fnref:24" href="#fn:24"><sup>24</sup></a><a class="footnote-ref" id="fnref:25" href="#fn:25"><sup>25</sup></a> In support of the <a href="/facts/Adenovirus/JLX5IKHt">adenoviral</a> experiments, S100A1 transgenic overexpressing mice subjected to <a href="/facts/Myocardial_infarction/xoGw0qcG">myocardial infarction</a> showed preserved contractile function, abrogated <a href="/facts/Apoptosis/8dVzSm4y">apoptosis</a>, preserved <a href="/facts/Sarcoplasmic_reticulum/5tSqPRlk">sarcoplasmic reticulum</a> <a href="/facts/Calcium/hf252CC0">calcium</a> cycling and <a href="/facts/Adrenergic_receptor/uoAeJbcN">beta adrenergic signaling</a>, prevention from <a href="/facts/Cardiac_hypertrophy/YNcQhDVE">cardiac hypertrophy</a> and <a href="/facts/Heart_failure/7fckX3Jm">heart failure</a>, as well as prolonged survival relative to non-transgenic controls.<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> </p><p>S100A1 has also been identified as a novel regulator of <a href="/facts/Endothelial_cell/L4ENFVnw">endothelial cell</a> post-ischemic <a href="/facts/Angiogenesis/h0HF9IUd">angiogenesis</a>, as patients with limb ischemia exhibited downregulation of S100A1 expression in hypoxic tissue.<a class="footnote-ref" id="fnref:28" href="#fn:28"><sup>28</sup></a><a class="footnote-ref" id="fnref:29" href="#fn:29"><sup>29</sup></a> </p><p>In <a href="/facts/Melanocytic_nevus/wmXWTklP">melanocytic</a> cells, S100A1 gene expression may be regulated by <a href="/facts/Microphthalmia-associated_transcription_factor/loE6X4HQ">MITF</a>.<a class="footnote-ref" id="fnref:30" href="#fn:30"><sup>30</sup></a> </p> <h2 id="clinical-significance">Clinical Significance</h2> <p>S100A1 has shown efficacy in feasibility in treating <a href="/facts/Heart_failure/7fckX3Jm">heart failure</a> symptoms in large, preclinical models and human cardiomyocytes,<a class="footnote-ref" id="fnref:31" href="#fn:31"><sup>31</sup></a><a class="footnote-ref" id="fnref:32" href="#fn:32"><sup>32</sup></a> and thus shows great promise for clinical trials.<a class="footnote-ref" id="fnref:33" href="#fn:33"><sup>33</sup></a><a class="footnote-ref" id="fnref:34" href="#fn:34"><sup>34</sup></a><a class="footnote-ref" id="fnref:35" href="#fn:35"><sup>35</sup></a><a class="footnote-ref" id="fnref:36" href="#fn:36"><sup>36</sup></a><a class="footnote-ref" id="fnref:37" href="#fn:37"><sup>37</sup></a><a class="footnote-ref" id="fnref:38" href="#fn:38"><sup>38</sup></a><a class="footnote-ref" id="fnref:39" href="#fn:39"><sup>39</sup></a> </p><p>Reduced expression of this protein has been implicated in <a href="/facts/Cardiomyopathy/rhXF3Vcj">cardiomyopathies</a>,<a class="footnote-ref" id="fnref:40" href="#fn:40"><sup>40</sup></a> and <a href="/facts/Left_ventricular_assist_device/kzwCcA9r">left ventricular assist device</a>-based therapy does not restore S100A1 levels in patients.<a class="footnote-ref" id="fnref:41" href="#fn:41"><sup>41</sup></a> S100A1 has shown promise as an early diagnostic biomarker for acute <a href="/facts/Myocardial_ischemia/szCt0nVx">myocardial ischemia</a>, presenting with a distinct timecourse in human plasma following an ischemic event relative to traditional markers <a href="/facts/Creatine_kinase/kYtNQKjy">creatine kinase</a>, <a href="/facts/CKMB/hozINoVl">CKMB</a> and <a href="/facts/TNNI3/jK1XqwHr">troponin I</a>.<a class="footnote-ref" id="fnref:42" href="#fn:42"><sup>42</sup></a><a class="footnote-ref" id="fnref:43" href="#fn:43"><sup>43</sup></a> This injury-released, extracellular pool of S100A1 was investigated in neonatal murine <a href="/facts/Cardiomyocyte/fE40oTQz">cardiomyocytes</a> and was shown to prevent apoptosis via an ERK1/2-dependent pathway, suggesting that the release of S100A1 from injured cells is an intrinsic survival mechanism for viable myocardium.<a class="footnote-ref" id="fnref:44" href="#fn:44"><sup>44</sup></a> S100 has also shown promise as a biomarker for uncontrolled hyperoxic reoxygenation during <a href="/facts/Cardiopulmonary_bypass/UQ8FxFa0">cardiopulmonary bypass</a> in infants with <a href="/facts/Cyanotic_heart_disease/bAan4jc8">cyanotic heart disease</a><a class="footnote-ref" id="fnref:45" href="#fn:45"><sup>45</sup></a> and in adults.<a class="footnote-ref" id="fnref:46" href="#fn:46"><sup>46</sup></a> S100A1 gene transfer to engineered heart tissue was shown to augment contractile performance of the tissue implants, suggesting that S100A1 may be effective in facilitating cardiac tissue replacement therapy in <a href="/facts/Heart_failure/7fckX3Jm">heart failure</a> patients.<a class="footnote-ref" id="fnref:47" href="#fn:47"><sup>47</sup></a> However, the clinical efficacy of this strategy remains to be determined. In addition, multiple drugs, including <a href="/facts/Pentamidine/xz00bxxS">Pentamidine</a>,<a class="footnote-ref" id="fnref:48" href="#fn:48"><sup>48</sup></a> <a href="/facts/Amlexanox/7d946dzv">Amlexanox</a>, <a href="/facts/Olopatadine/J4oxWdXt">Olopatadine</a>, <a href="/facts/Cromolyn/GHnWWVqK">Cromolyn</a>, and <a href="/facts/Propranolol/QvH2XYt1">Propranolol</a>,<a class="footnote-ref" id="fnref:49" href="#fn:49"><sup>49</sup></a> are known to bind to S100A1, although their affinities are often in the mid-micromolar range. </p> <h2 id="interactions">Interactions</h2> <p>S100 <a href="/facts/Protein-protein_interaction/etvm9Wmg">interacts</a> with </p> <ul><li><a href="/facts/PGM1/67sYnwVC">PGM1</a><a class="footnote-ref" id="fnref:50" href="#fn:50"><sup>50</sup></a></li> <li><a href="/facts/S100B/dhSpGQRz">S100B</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><a class="footnote-ref" id="fnref:53" href="#fn:53"><sup>53</sup></a></li> <li><a href="/facts/S100A4/svvenkKb">S100A4</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></li> <li><a href="/facts/TRPM3/HBUjLayV">TRPM3</a><a class="footnote-ref" id="fnref:56" href="#fn:56"><sup>56</sup></a></li> <li><a href="/facts/Titin/w6yGjgcx">Titin</a><a class="footnote-ref" id="fnref:57" href="#fn:57"><sup>57</sup></a></li> <li><a href="/facts/RYR2/mLrPQamI">RYR2</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></li> <li><a href="/facts/ATP2A2/pqscn3GG">SERCA2A</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></li> <li><a href="/facts/PLB/gTgCx1yt">PLB</a><a class="footnote-ref" id="fnref:63" href="#fn:63"><sup>63</sup></a></li> <li><a href="/facts/RYR1/ITPtPc2r">RYR1</a><a class="footnote-ref" id="fnref:64" href="#fn:64"><sup>64</sup></a></li></ul> <h2 id="further-reading">Further reading</h2> <ul><li>Zimmer DB, Cornwall EH, Landar A, Song W (1995). "The S100 protein family: history, function, and expression". <i>Brain Research Bulletin</i>. 37 (4): 417–29. <a href="/facts/Doi_(identifier)/muM9Etpq">doi</a>:<a href="https://doi.org/10.1016%2F0361-9230%2895%2900040-2">10.1016/0361-9230(95)00040-2</a>. <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/7620916">7620916</a>. <a href="/facts/S2CID_(identifier)/ldJsHa2Y">S2CID</a> <a href="https://api.semanticscholar.org/CorpusID:34720854">34720854</a>.</li> <li>Schäfer BW, Heizmann CW (April 1996). "The S100 family of EF-hand calcium-binding proteins: functions and pathology". <i>Trends in Biochemical Sciences</i>. 21 (4): 134–40. <a href="/facts/Doi_(identifier)/muM9Etpq">doi</a>:<a href="https://doi.org/10.1016%2FS0968-0004%2896%2980167-8">10.1016/S0968-0004(96)80167-8</a>. <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/8701470">8701470</a>.</li> <li>Garbuglia M, Verzini M, Sorci G, Bianchi R, Giambanco I, Agneletti AL, Donato R (October 1999). <a href="https://doi.org/10.1590%2Fs0100-879x1999001000001">"The calcium-modulated proteins, S100A1 and S100B, as potential regulators of the dynamics of type III intermediate filaments"</a>. <i>Brazilian Journal of Medical and Biological Research</i>. 32 (10): 1177–85. <a href="/facts/Doi_(identifier)/muM9Etpq">doi</a>:<a href="https://doi.org/10.1590%2Fs0100-879x1999001000001">10.1590/s0100-879x1999001000001</a>. <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/10510252">10510252</a>.</li> <li>Engelkamp D, Schäfer BW, Erne P, Heizmann CW (October 1992). "S100 alpha, CAPL, and CACY: molecular cloning and expression analysis of three calcium-binding proteins from human heart". <i>Biochemistry</i>. 31 (42): 10258–64. <a href="/facts/Doi_(identifier)/muM9Etpq">doi</a>:<a href="https://doi.org/10.1021%2Fbi00157a012">10.1021/bi00157a012</a>. <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/1384693">1384693</a>.</li> <li>Morii K, Tanaka R, Takahashi Y, Minoshima S, Fukuyama R, Shimizu N, Kuwano R (February 1991). "Structure and chromosome assignment of human S100 alpha and beta subunit genes". <i>Biochemical and Biophysical Research Communications</i>. 175 (1): 185–91. <a href="/facts/Doi_(identifier)/muM9Etpq">doi</a>:<a href="https://doi.org/10.1016%2FS0006-291X%2805%2981218-5">10.1016/S0006-291X(05)81218-5</a>. <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/1998503">1998503</a>.</li> <li>Baudier J, Glasser N, Gerard D (June 1986). <a href="https://doi.org/10.1016%2FS0021-9258%2819%2983895-4">"Ions binding to S100 proteins. I. Calcium- and zinc-binding properties of bovine brain S100 alpha alpha, S100a (alpha beta), and S100b (beta beta) protein: Zn2+ regulates Ca2+ binding on S100b protein"</a>. <i>The Journal of Biological Chemistry</i>. 261 (18): 8192–203. <a href="/facts/Doi_(identifier)/muM9Etpq">doi</a>:<a href="https://doi.org/10.1016%2FS0021-9258%2819%2983895-4">10.1016/S0021-9258(19)83895-4</a>. <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/3722149">3722149</a>.</li> <li>Kato K, Kimura S (October 1985). "S100ao (alpha alpha) protein is mainly located in the heart and striated muscles". <i>Biochimica et Biophysica Acta (BBA) - General Subjects</i>. 842 (2–3): 146–50. <a href="/facts/Doi_(identifier)/muM9Etpq">doi</a>:<a href="https://doi.org/10.1016%2F0304-4165%2885%2990196-5">10.1016/0304-4165(85)90196-5</a>. <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/4052452">4052452</a>.</li> <li>Schäfer BW, Wicki R, Engelkamp D, Mattei MG, Heizmann CW (February 1995). 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