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Commit d8a86220 authored by cylon-x's avatar cylon-x 🤖
Browse files

Update models

parent a255a567
Pipeline #37177 passed with stage
in 4 minutes and 10 seconds
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......@@ -997,7 +997,7 @@
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......@@ -1304,7 +1304,7 @@
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......@@ -1465,7 +1465,7 @@
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......@@ -1498,7 +1498,7 @@
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......@@ -1517,7 +1517,7 @@
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......@@ -1795,7 +1795,7 @@
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......@@ -2124,7 +2124,7 @@
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......@@ -2152,7 +2152,7 @@
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......@@ -2484,11 +2484,11 @@ Complex formation between thrombin and thrombomodulin inhibits both thrombin-cat
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</p>
<p>Molar ratio estimates indicated that 1 mol of C5b,C9dimer,C6,C7,an dC8 and 3-4mol of C9 monomer were present per M C5b-9 complex. PMID: 6796960
</rdf:RDF></annotation></qual:transition><qual:transition qual:id="tr_csa32"><qual:listOfInputs><qual:input qual:qualitativeSpecies="sa207" qual:transitionEffect="none" qual:sign="positive" qual:id="tr_csa32_in_0" /><qual:input qual:qualitativeSpecies="sa314" qual:transitionEffect="none" qual:sign="positive" qual:id="tr_csa32_in_1" /><qual:input qual:qualitativeSpecies="csa35" qual:transitionEffect="none" qual:sign="positive" qual:id="tr_csa32_in_2" /><qual:input qual:qualitativeSpecies="csa27" qual:transitionEffect="none" qual:sign="positive" qual:id="tr_csa32_in_3" /></qual:listOfInputs><qual:listOfOutputs><qual:output qual:qualitativeSpecies="csa32" qual:transitionEffect="assignmentLevel" qual:id="tr_csa32_out" /></qual:listOfOutputs><qual:listOfFunctionTerms><qual:defaultTerm qual:resultLevel="0" /><qual:functionTerm qual:resultLevel="1"><math xmlns="http://www.w3.org/1998/Math/MathML"><apply><or /><apply><eq /><ci>sa207</ci><cn type="integer">1</cn></apply><apply><and /><apply><or /><apply><eq /><ci>csa35</ci><cn type="integer">1</cn></apply><apply><eq /><ci>csa27</ci><cn type="integer">1</cn></apply></apply><apply><eq /><ci>sa314</ci><cn type="integer">1</cn></apply></apply></apply></math></qual:functionTerm></qual:listOfFunctionTerms><notes><html xmlns="http://www.w3.org/1999/xhtml"><head><title /></head><body><p>Molar ratio estimates indicated that 1 mol of C5b,C9dimer,C6,C7,an dC8 and 3-4mol of C9 monomer were present per M C5b-9 complex. PMID: 6796960
The first step requires cleavage of C5 into the small anaphylatoxin C5a and the large fragment C5b by the C5 convertase. C6 binds the labile C5b intermediate, resulting in a stable C5b6 complex. C7 binds C5b6, anchoring the newly formed C5b7 complex to the membrane surface. C8, a heterotrimeric protein composed of C8α, C8β and C8γ, is incorporated into the assembly precursor forming C5b8 and marking the first membrane penetrating event. Finally, multiple copies of C9 join the assembly and span membrane, resulting in the final membrane attack complex (MAC). PMID: 28630159
</p>
<p>The elevated circulatory levels of C5b-9 were also reported in severe cases of COVID-19. PMCID:PMC7260598
</p>
<p>Stable complexes of phospholipid and protein were formed by C5b--7, C5b--8, C5b--9, and the MAC (C5b--9 dimer) and they exhibited densities of 1.2164, 1.184, 1.2055, and 1.2275 g/ml, respectively. PMID: 284414
The first step requires cleavage of C5 into the small anaphylatoxin C5a and the large fragment C5b by the C5 convertase. C6 binds the labile C5b intermediate, resulting in a stable C5b6 complex. C7 binds C5b6, anchoring the newly formed C5b7 complex to the membrane surface. C8, a heterotrimeric protein composed of C8α, C8β and C8γ, is incorporated into the assembly precursor forming C5b8 and marking the first membrane penetrating event. Finally, multiple copies of C9 join the assembly and span membrane, resulting in the final membrane attack complex (MAC). PMID: 28630159
</p>
......@@ -2503,10 +2503,10 @@ Kinetic parameters revealed that the soluble form of the enzyme (C4b,C2a) cleave
When the density of C3b molecules on the cell surface becomes sufficiently high, the existing C3 convertases (C4b2a and C3bBb) gain the ability to cleave C5, leading to formation of C5a and C5b. PMID: 30083158
The first step requires cleavage of C5 into the small anaphylatoxin C5a and the large fragment C5b by the C5 convertase. C6 binds the labile C5b intermediate, resulting in a stable C5b6 complex. C7 binds C5b6, anchoring the newly formed C5b7 complex to the membrane surface. C8, a heterotrimeric protein composed of C8α, C8β and C8γ, is incorporated into the assembly precursor forming C5b8 and marking the first membrane penetrating event. Finally, multiple copies of C9 join the assembly and span membrane, resulting in the final membrane attack complex (MAC). PMID: 28630159
</p>
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......@@ -2515,10 +2515,10 @@ The first step requires cleavage of C5 into the small anaphylatoxin C5a and the
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......@@ -2883,21 +2883,26 @@ PMID:15746105
</rdf:Bag>
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</rdf:Description>
</rdf:RDF></annotation></qual:transition><qual:transition qual:id="tr_sa194"><qual:listOfInputs><qual:input qual:qualitativeSpecies="sa207" qual:transitionEffect="none" qual:sign="positive" qual:id="tr_sa194_in_0" /><qual:input qual:qualitativeSpecies="sa195" qual:transitionEffect="none" qual:sign="positive" qual:id="tr_sa194_in_1" /><qual:input qual:qualitativeSpecies="sa198" qual:transitionEffect="none" qual:sign="positive" qual:id="tr_sa194_in_2" /></qual:listOfInputs><qual:listOfOutputs><qual:output qual:qualitativeSpecies="sa194" qual:transitionEffect="assignmentLevel" qual:id="tr_sa194_out" /></qual:listOfOutputs><qual:listOfFunctionTerms><qual:defaultTerm qual:resultLevel="0" /><qual:functionTerm qual:resultLevel="1"><math xmlns="http://www.w3.org/1998/Math/MathML"><apply><or /><apply><eq /><ci>sa207</ci><cn type="integer">1</cn></apply><apply><eq /><ci>sa195</ci><cn type="integer">1</cn></apply><apply><and /><apply><eq /><ci>sa195</ci><cn type="integer">1</cn></apply><apply><eq /><ci>sa198</ci><cn type="integer">1</cn></apply></apply></apply></math></qual:functionTerm></qual:listOfFunctionTerms><notes><html xmlns="http://www.w3.org/1999/xhtml"><head><title /></head><body><p>SARS-COV-2 infection icreases the level of Angiotesin II in blood plasma. PMID:32048163
</rdf:RDF></annotation></qual:transition><qual:transition qual:id="tr_sa194"><qual:listOfInputs><qual:input qual:qualitativeSpecies="sa195" qual:transitionEffect="none" qual:sign="positive" qual:id="tr_sa194_in_0" /><qual:input qual:qualitativeSpecies="sa198" qual:transitionEffect="none" qual:sign="positive" qual:id="tr_sa194_in_1" /><qual:input qual:qualitativeSpecies="sa207" qual:transitionEffect="none" qual:sign="positive" qual:id="tr_sa194_in_2" /></qual:listOfInputs><qual:listOfOutputs><qual:output qual:qualitativeSpecies="sa194" qual:transitionEffect="assignmentLevel" qual:id="tr_sa194_out" /></qual:listOfOutputs><qual:listOfFunctionTerms><qual:defaultTerm qual:resultLevel="0" /><qual:functionTerm qual:resultLevel="1"><math xmlns="http://www.w3.org/1998/Math/MathML"><apply><or /><apply><and /><apply><eq /><ci>sa195</ci><cn type="integer">1</cn></apply><apply><eq /><ci>sa198</ci><cn type="integer">1</cn></apply></apply><apply><eq /><ci>sa195</ci><cn type="integer">1</cn></apply><apply><eq /><ci>sa207</ci><cn type="integer">1</cn></apply></apply></math></qual:functionTerm></qual:listOfFunctionTerms><notes><html xmlns="http://www.w3.org/1999/xhtml"><head><title /></head><body><p>In a classical view, the renin–angiotensin system (RAS) is considered an endocrine system whose active metabolite, the angiotensin II (Ang II), is produced by enzymatic sequential cleavage from the angiotensinogen substratum of hepatic origin. In the bloodstream, the renin, a highly specifi c protease, converts the circulating angiotensinogen into the decapeptide Ang I, which, in turn is converted to Ang II by the angiotensin-converting enzyme (ACE) action. This enzyme also inactivates bradykinin (BK) and is highly found in the endothelial cells membranes of the pulmonary circulation. PMID:19065996
</p>
<p>SARS-COV-2 infection icreases the level of Angiotesin II in blood plasma. PMID: 32048163
</p>
<p>In a classical view, the renin–angiotensin system (RAS) is considered an endocrine system whose active metabolite, the angiotensin II (Ang II), is produced by enzymatic sequential cleavage from the angiotensinogen substratum of hepatic origin. In the bloodstream, the renin, a highly specifi c protease, converts the circulating angiotensinogen into the decapeptide Ang I, which, in turn is converted to Ang II by the angiotensin-converting enzyme (ACE) action. This enzyme also inactivates bradykinin (BK) and is highly found in the endothelial cells membranes of the pulmonary circulation. PMID:19065996
<p>SARS-COV-2 infection icreases the level of Angiotesin II in blood plasma. PMID:32048163
</p>
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......@@ -2918,20 +2923,15 @@ PMID:15746105
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......@@ -3108,49 +3108,49 @@ Urokinase-type plasminogen activater catalyses plasmin formation from plasminoge
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</p>
<p>Bradykinin stimulates tissue plasminogen activator release in human vasculature. PMID:10373228
</rdf:RDF></annotation></qual:transition><qual:transition qual:id="tr_sa213"><qual:listOfInputs><qual:input qual:qualitativeSpecies="sa225" qual:transitionEffect="none" qual:sign="positive" qual:id="tr_sa213_in_0" /><qual:input qual:qualitativeSpecies="sa224" qual:transitionEffect="none" qual:sign="negative" qual:id="tr_sa213_in_1" /><qual:input qual:qualitativeSpecies="sa402" qual:transitionEffect="none" qual:sign="positive" qual:id="tr_sa213_in_2" /><qual:input qual:qualitativeSpecies="sa194" qual:transitionEffect="none" qual:sign="positive" qual:id="tr_sa213_in_3" /><qual:input qual:qualitativeSpecies="sa400" qual:transitionEffect="none" qual:sign="negative" qual:id="tr_sa213_in_4" /><qual:input qual:qualitativeSpecies="sa205" qual:transitionEffect="none" qual:sign="negative" qual:id="tr_sa213_in_5" /></qual:listOfInputs><qual:listOfOutputs><qual:output qual:qualitativeSpecies="sa213" qual:transitionEffect="assignmentLevel" qual:id="tr_sa213_out" /></qual:listOfOutputs><qual:listOfFunctionTerms><qual:defaultTerm qual:resultLevel="0" /><qual:functionTerm qual:resultLevel="1"><math xmlns="http://www.w3.org/1998/Math/MathML"><apply><or /><apply><and /><apply><or /><apply><eq /><ci>sa402</ci><cn type="integer">1</cn></apply><apply><eq /><ci>sa194</ci><cn type="integer">1</cn></apply></apply><apply><eq /><ci>sa225</ci><cn type="integer">1</cn></apply><apply><eq /><ci>sa224</ci><cn type="integer">0</cn></apply><apply><eq /><ci>sa400</ci><cn type="integer">0</cn></apply><apply><eq /><ci>sa205</ci><cn type="integer">0</cn></apply></apply><apply><eq /><ci>sa402</ci><cn type="integer">1</cn></apply></apply></math></qual:functionTerm></qual:listOfFunctionTerms><notes><html xmlns="http://www.w3.org/1999/xhtml"><head><title /></head><body><p>Bradykinin stimulates tissue plasminogen activator release in human vasculature. PMID:10373228
Plasminogen activator inhibitor-1 is the Primary inhibitor of tissue-type plasminogen activator in pregnancy plasma. PMID:3124286
Ang II increased PAI-1 and tissue plasminogen activator (t-PA) release, while its metabolite angiotensin-(1-7) (Ang-(1-7)) amino acid fragment decreased them. PMID:12091055
Bovine-activated protein C also decreased PAI activity of whole blood and of serum. In contrast to the bovine molecule, human-activated protein C was much less profibrinolytic in these clot lysis assay systems and much less potent in causing the neutralization of PAI. This species specificity of activated protein C in clot lysis assays reflect the known in vivo profibrinolytic species specificity. a major mechanism for bovine protein C-dependent fibrinolysis in in vitro clot lysis assays involves a direct neutralization of PAI by activated protein C. PMID:3096399
</p>
</body></html></notes><annotation><rdf:RDF><rdf:Description rdf:about="#re372">
<p>In vivo data suggest that infusion of bradykinin results in an increase in circulating t-PA levels without an effect on PAI-1. PMID: 9066005
</p>
</body></html></notes><annotation><rdf:RDF><rdf:Description rdf:about="#re180">
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......@@ -3276,32 +3276,32 @@ Kallikrein digests KNG1 to release bradykinin. PMID: 4627469
</rdf:Bag>
</bqbiol:isDescribedBy>
</rdf:Description>
</rdf:RDF></annotation></qual:transition><qual:transition qual:id="tr_sa251"><qual:listOfInputs><qual:input qual:qualitativeSpecies="sa167" qual:transitionEffect="none" qual:sign="positive" qual:id="tr_sa251_in_0" /><qual:input qual:qualitativeSpecies="sa165" qual:transitionEffect="none" qual:sign="positive" qual:id="tr_sa251_in_1" /><qual:input qual:qualitativeSpecies="csa11" qual:transitionEffect="none" qual:sign="positive" qual:id="tr_sa251_in_2" /></qual:listOfInputs><qual:listOfOutputs><qual:output qual:qualitativeSpecies="sa251" qual:transitionEffect="assignmentLevel" qual:id="tr_sa251_out" /></qual:listOfOutputs><qual:listOfFunctionTerms><qual:defaultTerm qual:resultLevel="0" /><qual:functionTerm qual:resultLevel="1"><math xmlns="http://www.w3.org/1998/Math/MathML"><apply><or /><apply><and /><apply><eq /><ci>sa167</ci><cn type="integer">1</cn></apply><apply><eq /><ci>sa165</ci><cn type="integer">1</cn></apply></apply><apply><eq /><ci>csa11</ci><cn type="integer">1</cn></apply></apply></math></qual:functionTerm></qual:listOfFunctionTerms><notes><html xmlns="http://www.w3.org/1999/xhtml"><head><title /></head><body><p>Prekallikrein is cleaved by factor XII to form kallikrein, which then cleaves factor XII first to alpha-factor XIIa and then trypsin cleaves it to beta-factor XIIa. Alpha-factor XIIa activates factor XI to factor XIa. PMID:21304106
</p>
<p>Factor XIIa converts prekallikrein to kallikrein. PMID: 6768384
</rdf:RDF></annotation></qual:transition><qual:transition qual:id="tr_sa251"><qual:listOfInputs><qual:input qual:qualitativeSpecies="csa11" qual:transitionEffect="none" qual:sign="positive" qual:id="tr_sa251_in_0" /><qual:input qual:qualitativeSpecies="sa167" qual:transitionEffect="none" qual:sign="positive" qual:id="tr_sa251_in_1" /><qual:input qual:qualitativeSpecies="sa165" qual:transitionEffect="none" qual:sign="positive" qual:id="tr_sa251_in_2" /></qual:listOfInputs><qual:listOfOutputs><qual:output qual:qualitativeSpecies="sa251" qual:transitionEffect="assignmentLevel" qual:id="tr_sa251_out" /></qual:listOfOutputs><qual:listOfFunctionTerms><qual:defaultTerm qual:resultLevel="0" /><qual:functionTerm qual:resultLevel="1"><math xmlns="http://www.w3.org/1998/Math/MathML"><apply><or /><apply><eq /><ci>csa11</ci><cn type="integer">1</cn></apply><apply><and /><apply><eq /><ci>sa167</ci><cn type="integer">1</cn></apply><apply><eq /><ci>sa165</ci><cn type="integer">1</cn></apply></apply></apply></math></qual:functionTerm></qual:listOfFunctionTerms><notes><html xmlns="http://www.w3.org/1999/xhtml"><head><title /></head><body><p>Factor XIIa converts prekallikrein to kallikrein. PMID: 6768384
Kallikrein digests KNG1 to release bradykinin. PMID: 4627469
</p>
</body></html></notes><annotation><rdf:RDF><rdf:Description rdf:about="#re329">
<p>Prekallikrein is cleaved by factor XII to form kallikrein, which then cleaves factor XII first to alpha-factor XIIa and then trypsin cleaves it to beta-factor XIIa. Alpha-factor XIIa activates factor XI to factor XIa. PMID:21304106
</p>
</body></html></notes><annotation><rdf:RDF><rdf:Description rdf:about="#CDMT00119">
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......@@ -3310,24 +3310,29 @@ Kallikrein digests KNG1 to release bradykinin. PMID: 4627469
</rdf:Bag>
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</rdf:Description>
</rdf:RDF></annotation></qual:transition><qual:transition qual:id="tr_sa253"><qual:listOfInputs><qual:input qual:qualitativeSpecies="sa212" qual:transitionEffect="none" qual:sign="positive" qual:id="tr_sa253_in_0" /><qual:input qual:qualitativeSpecies="sa207" qual:transitionEffect="none" qual:sign="positive" qual:id="tr_sa253_in_1" /><qual:input qual:qualitativeSpecies="sa314" qual:transitionEffect="none" qual:sign="positive" qual:id="tr_sa253_in_2" /><qual:input qual:qualitativeSpecies="csa35" qual:transitionEffect="none" qual:sign="positive" qual:id="tr_sa253_in_3" /><qual:input qual:qualitativeSpecies="csa27" qual:transitionEffect="none" qual:sign="positive" qual:id="tr_sa253_in_4" /></qual:listOfInputs><qual:listOfOutputs><qual:output qual:qualitativeSpecies="sa253" qual:transitionEffect="assignmentLevel" qual:id="tr_sa253_out" /></qual:listOfOutputs><qual:listOfFunctionTerms><qual:defaultTerm qual:resultLevel="0" /><qual:functionTerm qual:resultLevel="1"><math xmlns="http://www.w3.org/1998/Math/MathML"><apply><or /><apply><eq /><ci>sa212</ci><cn type="integer">1</cn></apply><apply><eq /><ci>sa207</ci><cn type="integer">1</cn></apply><apply><and /><apply><or /><apply><eq /><ci>csa35</ci><cn type="integer">1</cn></apply><apply><eq /><ci>csa27</ci><cn type="integer">1</cn></apply></apply><apply><eq /><ci>sa314</ci><cn type="integer">1</cn></apply></apply></apply></math></qual:functionTerm></qual:listOfFunctionTerms><notes><html xmlns="http://www.w3.org/1999/xhtml"><head><title /></head><body><p>In an arterial thrombosis model, plasminogen activator administration increased C5a levels. PMID: 27077125
</p>
<p>The elevated circulatory levels of C5a were also reported in severe cases of COVID-19. PMCID:PMC7260598
</p>
<p>The first step requires cleavage of C5 into the small anaphylatoxin C5a and the large fragment C5b by the C5 convertase. PMID: 30083158
</rdf:RDF></annotation></qual:transition><qual:transition qual:id="tr_sa253"><qual:listOfInputs><qual:input qual:qualitativeSpecies="sa314" qual:transitionEffect="none" qual:sign="positive" qual:id="tr_sa253_in_0" /><qual:input qual:qualitativeSpecies="csa35" qual:transitionEffect="none" qual:sign="positive" qual:id="tr_sa253_in_1" /><qual:input qual:qualitativeSpecies="csa27" qual:transitionEffect="none" qual:sign="positive" qual:id="tr_sa253_in_2" /><qual:input qual:qualitativeSpecies="sa207" qual:transitionEffect="none" qual:sign="positive" qual:id="tr_sa253_in_3" /><qual:input qual:qualitativeSpecies="sa212" qual:transitionEffect="none" qual:sign="positive" qual:id="tr_sa253_in_4" /></qual:listOfInputs><qual:listOfOutputs><qual:output qual:qualitativeSpecies="sa253" qual:transitionEffect="assignmentLevel" qual:id="tr_sa253_out" /></qual:listOfOutputs><qual:listOfFunctionTerms><qual:defaultTerm qual:resultLevel="0" /><qual:functionTerm qual:resultLevel="1"><math xmlns="http://www.w3.org/1998/Math/MathML"><apply><or /><apply><and /><apply><or /><apply><eq /><ci>csa35</ci><cn type="integer">1</cn></apply><apply><eq /><ci>csa27</ci><cn type="integer">1</cn></apply></apply><apply><eq /><ci>sa314</ci><cn type="integer">1</cn></apply></apply><apply><eq /><ci>sa207</ci><cn type="integer">1</cn></apply><apply><eq /><ci>sa212</ci><cn type="integer">1</cn></apply></apply></math></qual:functionTerm></qual:listOfFunctionTerms><notes><html xmlns="http://www.w3.org/1999/xhtml"><head><title /></head><body><p>The first step requires cleavage of C5 into the small anaphylatoxin C5a and the large fragment C5b by the C5 convertase. PMID: 30083158
Kinetic parameters revealed that the soluble form of the enzyme (C4b,C2a) cleaved C5 at a catalytic rate similar to that of the surface-bound form (EAC1,C4b,C2a). PMID: 12878586
When the density of C3b molecules on the cell surface becomes sufficiently high, the existing C3 convertases (C4b2a and C3bBb) gain the ability to cleave C5, leading to formation of C5a and C5b. PMID: 30083158
The first step requires cleavage of C5 into the small anaphylatoxin C5a and the large fragment C5b by the C5 convertase. C6 binds the labile C5b intermediate, resulting in a stable C5b6 complex. C7 binds C5b6, anchoring the newly formed C5b7 complex to the membrane surface. C8, a heterotrimeric protein composed of C8α, C8β and C8γ, is incorporated into the assembly precursor forming C5b8 and marking the first membrane penetrating event. Finally, multiple copies of C9 join the assembly and span membrane, resulting in the final membrane attack complex (MAC). PMID: 28630159
</p>
</body></html></notes><annotation><rdf:RDF><rdf:Description rdf:about="#re343">
<p>The elevated circulatory levels of C5a were also reported in severe cases of COVID-19. PMCID:PMC7260598
</p>
<p>In an arterial thrombosis model, plasminogen activator administration increased C5a levels. PMID: 27077125
</p>
</body></html></notes><annotation><rdf:RDF><rdf:Description rdf:about="#re262">
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......@@ -3343,59 +3348,54 @@ The first step requires cleavage of C5 into the small anaphylatoxin C5a and the
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<p>C5b-9 deposits were present in 78.6% of thrombotic microangiopathy cases and in 39.6% of controls (n=53), but the staining pattern differed between cases and controls. PMID: 25573909
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</p>
<p>Deposits of C4d, mannose-binding lectin, C1q, IgM, and C5b-9 were scored in the glomeruli, peritubular capillaries, and arterioles. Notably, C4d deposits were present in 88.1% of TMA cases, and the various clinical conditions had distinct staining patterns within the various compartments of the renal vasculature. Classical pathway activation was observed in 90.5% of TMA cases. Complement activation has a major role in thrombotic microangiopathy (TMA), a disorder that can occur in a variety of clinical conditions. PMID: 25573909
<p>The effects of IL-1β, IL-6 and IL-8 at low physiological levels, representative of chronic inflammation, by using scanning electron microscopy and thromboelastography were investigated. All three interleukins caused the viscoelastic properties to display an increased hypercoagulability of whole blood and pathology of both erythrocytes and platelets. The most pronounced changes were noted where all three cytokines caused platelet hyper-activation and spreading. PMID: 27561337
</p>
<p>VWF-mediated process is involved in platelet aggregation in stenotic arteries leading to acute thrombotic occlusion. PMID: 3500650
<p>TNFα accelerates thrombus formation in an in vivo model of arteriolar thrombosis. PMID: 23079185
</p>
<p>Plasma concentration of C-reactive protein was correlated with a risk of developing peripheral vascular disease. PMID: 9490235
<p>The effects of IL-1β, IL-6 and IL-8 at low physiological levels, representative of chronic inflammation, by using scanning electron microscopy and thromboelastography were investigated. All three interleukins caused the viscoelastic properties to display an increased hypercoagulability of whole blood and pathology of both erythrocytes and platelets. The most pronounced changes were noted where all three cytokines caused platelet hyper-activation and spreading. PMID: 27561337
</p>
<p>Patients who had thrombotic events displayed higher monocyte CD25 (IL2RA) levels (6.2%) than those without symptoms (1.3%) and controls (2.6%), p=0.0006. PMID:20483636
</p>
<p>The effects of IL-1β, IL-6 and IL-8 at low physiological levels, representative of chronic inflammation, by using scanning electron microscopy and thromboelastography were investigated. All three interleukins caused the viscoelastic properties to display an increased hypercoagulability of whole blood and pathology of both erythrocytes and platelets. The most pronounced changes were noted where all three cytokines caused platelet hyper-activation and spreading. PMID: 27561337
<p>Plasma concentration of C-reactive protein was correlated with a risk of developing peripheral vascular disease. PMID: 9490235
</p>
<p>TNFα accelerates thrombus formation in an in vivo model of arteriolar thrombosis. PMID: 23079185
<p>VWF-mediated process is involved in platelet aggregation in stenotic arteries leading to acute thrombotic occlusion. PMID: 3500650
</p>
<p>The effects of IL-1β, IL-6 and IL-8 at low physiological levels, representative of chronic inflammation, by using scanning electron microscopy and thromboelastography were investigated. All three interleukins caused the viscoelastic properties to display an increased hypercoagulability of whole blood and pathology of both erythrocytes and platelets. The most pronounced changes were noted where all three cytokines caused platelet hyper-activation and spreading. PMID: 27561337
<p>Deposits of C4d, mannose-binding lectin, C1q, IgM, and C5b-9 were scored in the glomeruli, peritubular capillaries, and arterioles. Notably, C4d deposits were present in 88.1% of TMA cases, and the various clinical conditions had distinct staining patterns within the various compartments of the renal vasculature. Classical pathway activation was observed in 90.5% of TMA cases. Complement activation has a major role in thrombotic microangiopathy (TMA), a disorder that can occur in a variety of clinical conditions. PMID: 25573909
</p>
<p>The effects of IL-1β, IL-6 and IL-8 at low physiological levels, representative of chronic inflammation, by using scanning electron microscopy and thromboelastography were investigated. All three interleukins caused the viscoelastic properties to display an increased hypercoagulability of whole blood and pathology of both erythrocytes and platelets. The most pronounced changes were noted where all three cytokines caused platelet hyper-activation and spreading. PMID: 27561337
<p>C5b-9 deposits were present in 78.6% of thrombotic microangiopathy cases and in 39.6% of controls (n=53), but the staining pattern differed between cases and controls. PMID: 25573909
</p>
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<p>Angiotensin II induced hypertension is accompanied by enhanced microvascular thrombosis in arterioles. PMID:20975035
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......@@ -3404,10 +3404,10 @@ The first step requires cleavage of C5 into the small anaphylatoxin C5a and the