Search Results (450)

Figure 1
<p>The structure and proteins of HIV. Created with BioRender.com.</p> Full article ">Figure 2
<p>HIV-1 gp41 peptide target sites.</p> Full article ">Figure 3
<p>The steps of gp120 emergence for the initiation and regulation of HIV-1 infection. Glycoprotein gp160 is cleaved into gp120 and gp41 despite being attached in a trimeric form on the viral surface. The gp41 <span class="html-italic">C</span>-terminal subunit undergoes a conformational change necessary for viral fusion, while the gp120 <span class="html-italic">N</span>-terminal subunit extends outside the viral membrane. Gp120 can be structurally organized into five conserved regions (C1–C5) and five variable regions (V1–V5). The interaction between the host receptor CD4 and specific residues in the conserved regions of gp120, along with the co-receptor CCR5 binding to a GPGR/Q motif, is critical. The variable regions of gp120 and a significant amount of carbohydrates contribute to extracellular interactions and cover the protein’s surface [<a href="#B22-molecules-29-04951" class="html-bibr">22</a>]. <a href="#molecules-29-04951-f003" class="html-fig">Figure 3</a> was created with BioRender.com.</p> Full article ">Figure 4
<p>Anti-HIV peptide-based entry inhibitors.</p> Full article ">Figure 5
<p>Enfuvirtide (ENF) and albuvirtide: peptide-based drugs designed to inhibit HIV entry. The chemical structure of ENF is shown in detail.</p> Full article ">Figure 6
<p>Sequences of LP-83 and LP-86.</p> Full article ">Figure 7
<p>(<b>A</b>) Structures of an α-amino acid residue, the corresponding β³ residue analog, and cyclic β-residues ACPC and APC. (<b>B</b>) Primary sequences of α-peptides (adopted from [<a href="#B42-molecules-29-04951" class="html-bibr">42</a>]).</p> Full article ">Figure 8
<p>The amino acid sequence of the two L- and D- (shown in <span class="html-italic">italics</span>) peptides corresponds to the full length of the V3 loop of gp120 of HIV-1 89.6 strain. The cyclization is done through a disulfide bond between the two cysteines.</p> Full article ">Figure 9
<p>Chemical structure of cPTs AAR029b and FITC-AAR0.29b and linear hexapeptide triazole UM15.</p> Full article ">Figure 10
<p>The chemical structures of TB-CP-6.9a and TBP-CP-6.9f-m.</p> Full article ">

Figure 1
<p>Proposed clinical application of Elecsys^® HCV Duo immunoassay. HCV, hepatitis C virus; anti-HCV, HCV antibodies; HCV-Ag, HCV core antigen.</p> Full article ">

Figure 1
<p>Structure of enfuvirtide.</p> Full article ">

Figure 1
<p>HIV life cycle. The participation of viral encoded proteins during the unique steps of HIV replication: reverse transcription by reverse transcriptase (RT) in cytoplasm, 3′-processing of proviral DNA by integrase (IN) in cytoplasm, integration of proviral DNA into host genome by IN in nucleus, viral protein processing by viral protease (PR). p53 is localized in cytoplasm, mitochondria, and nucleus. See the manuscript text for details.</p> Full article ">Figure 2
<p>Schematics of functional domains of p53. Functional domains are indicated below the diagram.</p> Full article ">Figure 3
<p>The possible biological outcomes of p53-mediated error correction activities in HIV-infected cells and the consequences of the excision of wrong nucleotides or nucleoside analogs from DNA by p53 protein. See the manuscript text for details.</p> Full article ">Figure 4
<p>The potential consequences of the removal of incorporated nucleoside analogs (NAs) into DNA in HIV-infected cells by the p53 protein. The excision of NAs by p53 from proviral DNA incorporated by HIV-1 RT in cytoplasm leads to resistance to drugs (negative effect). In mitochondria, the removal of NAs by p53 from mitochondrial DNA (mitDNA) incorporated by DNA pol γ may reduce the potential of chain termination and mitochondrial toxicity (positive effect).</p> Full article ">

Figure 1
<p>Healthy pregnancy versus preeclampsia. This image depicts the regulation of inflammation during a healthy pregnancy in comparison to the dysregulation observed during preeclampsia and the associated outcomes of this dysregulation (Created using <a href="http://BioRender.com" target="_blank">BioRender.com</a>).</p> Full article ">Figure 2
<p>The role of interleukin-10 in Human Immunodefiency Virus (HIV) infection. This flow diagram depicts the double-edged role Interleukin-10’s anti-inflammatory properties play in HIV infection.</p> Full article ">

Figure 1
<p>Lamellarins found in nature.</p> Full article ">Figure 2
<p>Lamellarin’s related compounds with biological interest.</p> Full article ">Scheme 1
<p>Synthesis of lamellarin G trimethyl ether (<b>5</b>).</p> Full article ">Scheme 2
<p>Synthesis of lamellarin framework <b>15</b>.</p> Full article ">Scheme 3
<p>Total synthesis of ningalin A (<b>22</b>).</p> Full article ">Scheme 4
<p>Total synthesis of ningalin B (<b>34</b>).</p> Full article ">Scheme 5
<p>Total synthesis of lamellarin L (<b>43</b>).</p> Full article ">Scheme 6
<p>Total synthesis of ningalin B (<b>34</b>).</p> Full article ">Scheme 7
<p>Synthesis of ningalin B hexamethyl ether (<b>33</b>).</p> Full article ">Scheme 8
<p>Synthesis of ningalin B hexamethyl ether (<b>33</b>) and lamellarin G trimethyl ether (<b>5</b>).</p> Full article ">Scheme 9
<p>Synthesis of lamellarin G trimethyl ether (<b>5</b>).</p> Full article ">Scheme 10
<p>Synthesis of lamellarin D (<b>84</b>).</p> Full article ">Scheme 11
<p>Synthesis of lamellarins D (<b>84</b>), L (<b>43</b>), and N (<b>100</b>).</p> Full article ">Scheme 12
<p>Synthesis of lamellarin α 20-sulfate (<b>112</b>).</p> Full article ">Scheme 13
<p>Synthesis of ningalin B (<b>34</b>), lamellarin G (<b>123</b>), and lamellarin K (<b>124</b>).</p> Full article ">Scheme 14
<p>Synthesis of lamellarin G trimethyl ether (<b>5</b>) and ningalin B hexamethyl ether (<b>33</b>).</p> Full article ">Scheme 15
<p>Synthesis of <b>140</b> and <b>144a</b>–<b>h</b>, analogues of lamellarin D.</p> Full article ">Scheme 16
<p>Synthesis of lamellarin α (<b>158</b>) and lamellarin α 13-sulfate (<b>155</b>), 20-sulfate (<b>112</b>), and 13,20-disulfate (<b>159</b>).</p> Full article ">Scheme 16 Cont.
<p>Synthesis of lamellarin α (<b>158</b>) and lamellarin α 13-sulfate (<b>155</b>), 20-sulfate (<b>112</b>), and 13,20-disulfate (<b>159</b>).</p> Full article ">Scheme 17
<p>Synthesis of lamellarin G trimethyl ether (<b>5</b>) and lamellarin S (<b>175</b>).</p> Full article ">Scheme 18
<p>Synthesis of lamellarins D (<b>84</b>) and H (<b>181</b>) and ningalin B (<b>34</b>).</p> Full article ">Scheme 19
<p>Synthesis of lamellarins L (<b>43</b>) and N (<b>100</b>).</p> Full article ">Scheme 20
<p>Synthesis of lamellarins I (<b>199a</b>) and C (<b>199b</b>).</p> Full article ">Scheme 21
<p>Synthesis of lamellarin G trimethyl ether (<b>5</b>).</p> Full article ">Scheme 22
<p>Synthesis of lamellarin L (<b>43</b>) and lamellarin N (<b>100</b>).</p> Full article ">Scheme 23
<p>Synthesis of lamellarin D trimethyl ether (<b>218</b>) and lamellarin H (<b>181</b>).</p> Full article ">Scheme 24
<p>Synthesis of lamellarins η (<b>224a</b>), D (<b>84</b>), N (<b>100</b>), and α (<b>158</b>) and 5,6-dehydrolamellarin Y (<b>224b</b>).</p> Full article ">Scheme 25
<p>Synthesis of lamellarin D (<b>84</b>), lamellarin H (<b>181</b>), and lamellarin analogues <b>236</b> and <b>239</b>.</p> Full article ">Scheme 26
<p>Synthesis of lamellarins H (<b>181</b>) and η (<b>224a</b>), dihydrolamellarin η (<b>250</b>), lamellarin G trimethyl ether (<b>5</b>), lamellarin D trimethyl ether (<b>218</b>), and tris-desmethyl lamellarin G (<b>246</b>).</p> Full article ">Scheme 27
<p>Synthesis of lamellarin U (<b>256</b>).</p> Full article ">Scheme 28
<p>Synthesis of lamellarin D (<b>84</b>) using puruvic acid orthoester.</p> Full article ">Scheme 29
<p>Synthesis of ningalin B (<b>34</b>) and lamellarins S (<b>175</b>) and Z (<b>277</b>).</p> Full article ">Scheme 30
<p>Total synthesis of lamellarins S (<b>175</b>), Z (<b>277</b>), L (<b>43</b>), G (<b>123</b>), and N (<b>100</b>).</p> Full article ">Scheme 31
<p>Synthesis of lamellarin D (<b>84</b>).</p> Full article ">Scheme 32
<p>Total synthesis of lamellarins L (<b>43</b>), J (<b>307</b>), G (<b>123</b>), and Z (<b>277</b>).</p> Full article ">Scheme 33
<p>Total synthesis of lamellarins U (<b>256</b>) and A3 (<b>318</b>).</p> Full article ">Scheme 34
<p>Synthesis of lamellarins D (<b>84</b>) and H (<b>181</b>) and lamellarin analogue <b>336</b>.</p> Full article ">Scheme 35
<p>Total synthesis of lamellarin K (<b>124</b>).</p> Full article ">Scheme 36
<p>Total synthesis of lamellarin G trimethyl ether (<b>5</b>).</p> Full article ">Scheme 37
<p>Synthesis of lamellarins I (<b>199a</b>) and K (<b>124</b>).</p> Full article ">Scheme 38
<p>Synthesis of lamellarin D analogues.</p> Full article ">Scheme 39
<p>Synthesis of lamellarin H (<b>181</b>), lamellarin α (<b>158</b>), and lamellarin α 13,20-disulfate (<b>159</b>).</p> Full article ">Scheme 40
<p>Synthesis of lamellarin alkaloids via metal–halogen exchange.</p> Full article ">Scheme 41
<p>Synthesis of lamellarins U (<b>256</b>) and L (<b>43</b>).</p> Full article ">Scheme 42
<p>Synthesis of lamellarins L (<b>43</b>) and K (<b>124</b>).</p> Full article ">Scheme 43
<p>Synthesis of lamellarin D <b>(84</b>) and lamellarin 501 (<b>378</b>) derivatives.</p> Full article ">Scheme 44
<p>Synthesis of lamellarin D triester derivatives with aminoacids.</p> Full article ">Scheme 45
<p>Synthesis of lamellarin U (<b>256</b>) and its derivatives, and lamellarin L (<b>43</b>) by solid-phase procedure.</p> Full article ">Scheme 46
<p>Synthesis of lamellarins by polymer-supported reagents.</p> Full article ">Scheme 47
<p>Synthesis of lamellarin skeleton by 1,5-electrocyclization of azomethine ylides.</p> Full article ">Scheme 48
<p>Synthesis of lamellarins G trimethyl ether (<b>5</b>), L (<b>43</b>), G (<b>123</b>), K (<b>124</b>), I (<b>199a</b>), C (<b>199b</b>), dihydro η (<b>250</b>), U (<b>256</b>), J (<b>307</b>), X (<b>404</b>), Y (<b>405</b>), T (<b>406</b>), F (<b>407</b>), and E (<b>408</b>).</p> Full article ">Scheme 49
<p>Synthesis of lamellarins D (<b>84</b>), N (<b>100</b>), α (<b>158</b>), η (<b>224a</b>), 5,6-dehydro Y (<b>224b</b>), 5,6-dehydro G trimethyl ether (<b>411</b>), 5,6-dehydro G (<b>412</b>), M (<b>413</b>), ζ (<b>414</b>), B (<b>415</b>), 5,6-dehydro J (<b>416</b>), W (<b>417</b>), ε (<b>418</b>), and X (<b>419</b>).</p> Full article ">Scheme 50
<p>Synthesis of lamellarin U (<b>256</b>) and lamellarin G trimethyl ether (<b>5</b>).</p> Full article ">Scheme 51
<p>Synthesis of lamellarin G trimethyl ether (<b>5</b>), lamellarin η (<b>224a</b>), and dihydrolamellarin η (<b>250</b>).</p> Full article ">Scheme 52
<p>Synthesis of lamellarin G trimethyl ether (<b>5</b>).</p> Full article ">Scheme 53
<p>Synthesis of lamellarin G trimethyl ether (<b>5</b>), lamellarin A4 or trisdesmethyllamellarin G (<b>246</b>), lamellarin D trimethyl ether (<b>218</b>), and lamellarin H (<b>181</b>).</p> Full article ">Scheme 54
<p>Synthesis of lamellarin D trimethyl ether (<b>218</b>), lamellarin D (<b>84</b>), and lamellarin analogues.</p> Full article ">Scheme 55
<p>Synthesis of lamellarin analogues via 1,3-dipolar cycloaddition reaction of isoquinolinium ylides to nitrostilbenes.</p> Full article ">Scheme 56
<p>Synthesis of lamellarin G trimethyl ether (<b>5</b>) from 3-bromo-4-(3,4-dimethoxybenzoyl)-6,7-dimethoxychroman-2-one (<b>459</b>).</p> Full article ">Scheme 57
<p>Synthesis of lamellarin scaffold <b>239</b> from 2-phenylchromeno[3,4-<span class="html-italic">b</span>]pyrrol-4(3<span class="html-italic">H</span>)-one (<b>470d</b>).</p> Full article ">Scheme 58
<p>Synthesis of lamellarin D trimethyl ether (<b>218</b>), lamellarin H (<b>181</b>), and the lamellarin analogues <b>479</b> and <b>480</b>.</p> Full article ">Scheme 59
<p>Synthesis of lamellarin D trimethyl ether (<b>218</b>) and lamellarin H (<b>181</b>).</p> Full article ">Scheme 60
<p>Synthesis of lamellarin D (<b>84</b>) and 501 (<b>378</b>) and tribenzyl ether of lamellarin D (<b>98</b>).</p> Full article ">Scheme 61
<p>Synthesis of ningalin B (<b>34</b>).</p> Full article ">Scheme 62
<p>Synthesis of isolamellarins A <b>494a</b>,<b>b</b>.</p> Full article ">Scheme 63
<p>Synthesis of pentacyclic compound <b>498</b>.</p> Full article ">Scheme 64
<p>Synthesis of isolamellarin A <b>505</b> and isolamellarins B <b>507a</b>,<b>b</b>.</p> Full article ">Scheme 65
<p>Synthesis of isolamellarin A <b>505</b> and isolamellarin B <b>507a</b> under Ru(II)-catalysis.</p> Full article ">Scheme 66
<p>Synthesis of isoazacoumestan <b>518</b>.</p> Full article ">Scheme 67
<p>Synthesis of azacoumestans <b>520a</b>,<b>b</b>.</p> Full article ">Scheme 68
<p>Synthesis of isoazacoumestans <b>524a</b>,<b>b</b>.</p> Full article ">Scheme 69
<p>Synthesis of azacoumestrol (<b>529</b>).</p> Full article ">Scheme 70
<p>Pd-catalyzed synthesis of azacoumestan <b>533</b>.</p> Full article ">Scheme 71
<p>Synthesis of azacoumestan <b>533</b> and isoazacoumestan <b>536</b>.</p> Full article ">Scheme 72
<p>Synthesis of azacoumestan <b>540</b> and isoazacoumestan <b>544</b>.</p> Full article ">Scheme 73
<p>Pd-catalyzed synthesis of azacoumestanes <b>520a</b> and <b>549</b>.</p> Full article ">Scheme 74
<p>Synthesis of azacoumestans <b>553a</b>–<b>h</b> by the Cadogan reaction.</p> Full article ">Scheme 75
<p>Pd-catalyzed synthesis of azacoumestans <b>533</b> and <b>557a</b>–<b>f</b>.</p> Full article ">Scheme 76
<p>Pd-catalyzed synthesis of azacoumestans <b>520a</b> and <b>559a</b>–<b>d</b>.</p> Full article ">Scheme 77
<p>Pd-catalyzed synthesis of azacoumestans <b>520a</b> and <b>559a</b>–<b>z</b> (without base).</p> Full article ">Scheme 78
<p>Pd-catalyzed synthesis of azacoumestans <b>520a</b> and <b>559e</b>,<b>I</b>,<b>j</b>,<b>v</b>,<b>w</b>,<b>aa</b>–<b>ae</b> under MW.</p> Full article ">Scheme 79
<p>Pd-catalyzed synthesis of azacoumestans from alkynes under carbonylation.</p> Full article ">Scheme 80
<p>Synthesis of azacoumestan derivatives <b>573</b>, <b>574</b>, and <b>576</b>–<b>579</b>.</p> Full article ">Scheme 81
<p>Synthesis of isoazacoumestns <b>581a</b>–<b>s</b>.</p> Full article ">Scheme 82
<p>Synthesis of azacoumestans <b>533 and 584a</b>–<b>j</b>.</p> Full article ">Scheme 83
<p>Synthesis of “E-ring free” lamellarin analogues <b>587a</b>–<b>c</b>.</p> Full article ">Scheme 84
<p>Synthesis of pentacycle isoazacoumestan analogues <b>592a</b>,<b>b</b>.</p> Full article ">

Figure 1
<p>Structure, expression and receptor binding characteristics of IOS-1002. (<b>A</b>) Schematic representation of the IOS-1002 molecule constructed through the ligation of HLA-B57^(A46E/V97R) on N-terminus of human IgG4 Fc domain. (<b>B</b>) The topological structure of HLA-B57:01:01 including the B2m molecule. Mutation site residues A46 and V97 highlighted as spheres (PDB: 5VUF). (<b>C</b>) SEC-HPLC profile of purified IOS-1002. (<b>D</b>) Thermal unfolding profile of IOS-1002, determined by DSF. (<b>E</b>) Quantification of the binding affinities of IOS-1002 to LILRB1 (<span class="html-italic">n</span> = 4), LILRB2 (<span class="html-italic">n</span> = 5) and KIR3DL1 (<span class="html-italic">n</span> = 1) surface receptors determined by SPR. Red line represents raw data and black line represents the fit of 1:1 binding. RU: response units; K_D: binding constant represented as mean ± standard deviation. (<b>F</b>) The topological structure of the HLA-B57:01:01 interaction site generated by superimposing the HLA-B57 structure (PDB: 2HJK) onto LILRB1/HLA-G and LILRB2/HLA-G. The residues lining the binding interfaces between HLA-B57-B2m:LILRB1 and HLA-B57-B2m:LILRB2 are highlighted under the dashed circles and displayed as sticks. The crystal structure of HLA-B57:01 and KIR3DL1 allotype 015 (PDB: 5B39), which describes a separate epitope on the HLA-B57 α1-helix, incorporating residues 77–83, known as the Bw4 motif. Structural images generated using PyMOL. (<b>G</b>) Quantification of the binding affinity of IOS-1002 to FcγRI determined by SPR (<span class="html-italic">n</span> = 1). The specified <span class="html-italic">n</span> indicates the number of independent experiments.</p> Full article ">Figure 2
<p>IOS-1002 binds to target receptors on human primary cells and inhibits the associated downstream signaling. (<b>A</b>) CHO cells were transduced with LILRB1, LILRB2 and CD64 FcγRI and interaction of AF488 labeled molecules was measured by flow cytometry (<span class="html-italic">n</span> = 2). Mean ± standard deviation is presented. MFI: median of fluorescence intensity. (<b>B</b>) Dose-dependent binding of IOS-1002 on human primary monocytes and the monocyte-derived macrophages isolated from PBMCs (<span class="html-italic">n</span> = 4). Mean ± standard deviation is presented. MFI: mean of fluorescence intensity. The non-linear regression curve and EC₅₀ (95% Confidential Interval) were calculated using the model agonist vs. response variable slope (four parameters) in A and B. (<b>C</b>) Competition between IOS-1002, anti-LILRB1, anti-LILRB2, dual anti-LILRB1/2 and anti-CD64 antibody for cell surface epitopes on monocytes. Fold change of background-subtracted MFI relative to the cells pre-treated with IgG1 null antibody is presented, (<span class="html-italic">n</span> = 4). Mean ± standard deviation is presented. Statistical analysis of various conditions against IgG1 null control was performed using one-sample <span class="html-italic">t</span>-test (hypothetical mean = 1) and pre-treatment of combined dual anti-LILRB1/2 and anti-CD64 antibodies against anti-LILRB1/2 or anti-CD64 antibodies was analyzed by one-way ANOVA with Bonferroni multiple comparisons test. (<b>D</b>) Simple Western analysis showing expression and phosphorylation of ITIM-associated phosphatases, SHP-1 and SHP-2 in human primary monocytes-derived macrophages (<span class="html-italic">n</span> = 5). Quantification of phosphorylation over total protein relative to isotype control is presented in the graph on the right. Mean ± standard deviation is presented. Stars indicate the statistical significance against IgG4 control (one-sample <span class="html-italic">t</span>-test, hypothetical mean = 1). * <span class="html-italic">p</span> &lt; 0.05; ** <span class="html-italic">p</span> &lt; 0.01; **** <span class="html-italic">p</span> &lt; 0.0001. ns, non-significant. In (<b>A</b>) <span class="html-italic">n</span> indicates the number of independent experiments, in (<b>B</b>–<b>D</b>) <span class="html-italic">n</span> indicates the number of independent donors.</p> Full article ">Figure 3
<p>IOS-1002 affects the differentiation of monocytes toward MDSCs and enhances phagocytosis of monocyte-derived macrophages. (<b>A</b>) Scheme of different monocyte-derived immune cell-based assays performed. (<b>B</b>,<b>C</b>) The effect of IOS-1002 on the differentiation potential of monocytes toward MDSCs (<span class="html-italic">n</span> = 3) (<b>B</b>) and M2 macrophages (<span class="html-italic">n</span> = 4) (<b>C</b>) is presented and compared with anti-LILRB2 antibody. Mean ± standard deviation is presented. In C, stars indicate the statistical significance toward IgG4 control. (<b>D</b>) Macrophage phagocytosis in the presence of different concentrations of IOS-1002 toward H460 (NSCLC cell line) (<span class="html-italic">n</span> = 4). Mean ± standard deviation of 3 technical replicates is presented. A 4P-L curve was interpolated for quantification of the EC₅₀. (<b>E</b>) Macrophage phagocytosis in the presence of IOS-1002 on different Fc backbones toward H460 cell line (<span class="html-italic">n</span> = 2). Mean ± standard deviation is presented. Statistical analysis was performed using one-way ANOVA and Dunnett’s multiple comparisons test. Unless mentioned otherwise, all indicated compounds were used at a concentration of 20ug/mL. * <span class="html-italic">p</span>  &lt;  0.05, ** <span class="html-italic">p</span>  &lt;  0.01, *** <span class="html-italic">p</span>  &lt;  0.001. The specified <span class="html-italic">n</span> indicates the number of independent donors.</p> Full article ">Figure 4
<p>IOS-1002 activates T and NK cells and demonstrates efficacy in ex vivo patient samples. (<b>A</b>) Isolated human primary NK cells were incubated with HCT116 colon cancer cell line in a cell-cell contact manner and the percentage of cancer cell killing was measured for 60 h. Area under the curve (AUC) of the percent cytotoxicity over time was calculated and is represented in the graph (<span class="html-italic">n</span> = 4). Different colors represent independent donors. Statistical analysis was performed using RM one-way ANOVA with Dunnett’s multiple comparisons test. (<b>B</b>) Non-activated T cells were incubated with MIA PaCa-2 (pancreatic carcinoma, <span class="html-italic">n</span> = 2) and H1703 (NSCLC, <span class="html-italic">n</span> = 2) cancer cell lines in a cell-cell contact manner and co-cultures were monitored for 72 h; left, the T cells number at endpoint (72 h) is presented in fold changes over timepoint 0; right, the number of dead cancer cells at 72 h, expressed in percentage, is represented. Mean ± standard deviation is shown. Statistical analysis was performed using two-way ANOVA with Dunnet’s multiple comparisons. (<b>C</b>) TNFa levels in cell supernatant of PBMCs incubated with H1703 in a cell-cell contact manner for 48 h. TNFa concentration (pg/mL) for each individual donor is represented (<span class="html-italic">n</span> = 6). Every donor is color-coded throughout the treatments. Statistical analysis was performed using RM one-way ANOVA with Dunnett’s multiple comparisons test. Paired <span class="html-italic">t</span>-test analysis was used to compare activated PBMCs monoculture and PBS control co-culture. Act.: Activated, N. Act.: Non-activated. (<b>D</b>,<b>E</b>) Relative total tumoroid area normalized against the untreated sample and shown for individual patient samples (<b>D</b>) and in total cohort (<b>E</b>) upon different treatments. Each reported measurement is a median of up to 8 technical replicates. Imun15 sample has no SEA control recorded due to the technical error in the experiment. * <span class="html-italic">p</span>  &lt;  0.05, ** <span class="html-italic">p</span>  &lt;  0.01, *** <span class="html-italic">p</span>  &lt;  0.001. ns, non-significant. The specified <span class="html-italic">n</span> indicates the number of independent donors.</p> Full article ">

Figure 1
<p>(<b>A</b>) The co-culture assay showed relatively increased HIV-1 RT activity at day 21 compared to day 14. (<b>B</b>) Viability of PBMCs exposed to different concentrations of crocodile serum showed no significant cytotoxicity. (<b>C</b>) The % inhibition of crocodile serum pre- and post-infection of HIV-1 in the PBMC culture system at different serum concentration (0.5 and 0.25% <span class="html-italic">v</span>/<span class="html-italic">v</span>). Nevirapine (1250 µg/mL) was used as a positive control with 91.02 ± 3.45% combined inhibitory activity in both pre- and post-infection.</p> Full article ">

Figure 1
<p>Metabolic parameters in Naïve HIV patients (n = 33) compared to patients treated with cART (combined antiretroviral therapy) based on TDF/FTC/EFV for more than one year (n = 29). (<b>A</b>) Plasma glucose values; (<b>B</b>) Total Cholesterol values; (<b>C</b>) LDL: LDL-Cholesterol values; (<b>D</b>) HDL: HDL-Cholesterol values; (<b>E</b>) TG: Triglycerides levels; (<b>F</b>) Total bilirubin levels; (<b>G</b>) Indirect bilirubin levels; (<b>H</b>) GGT: Gamma-glutamyl transferase values; (<b>I</b>) ALP: Alkaline phosphatase values; (<b>J</b>) LDH: Lactate Dehydrogenase values. Box and whiskers plots showing median, minimum, and maximum values. # <span class="html-italic">p</span>-value = (0.05–0.1), * <span class="html-italic">p</span>-value &lt; 0.05, ** <span class="html-italic">p</span>-value &lt; 0.01, *** <span class="html-italic">p</span>-value &lt; 0.001.</p> Full article ">Figure 2
<p>Mitochondrial parameters in Naïve HIV patients (n = 33) compared to patients treated with cART (combined antiretroviral therapy) based on TDF/FTC/EFV for more than one year (n = 29). (<b>A</b>) PBMC-mtDNA: Peripheral blood mononuclear cells mitochondrial DNA; (<b>B</b>) Plasma-mtDNA: Plasma mitochondrial DNA levels; (<b>C</b>) CoQ: Coenzyme Q values; (<b>D</b>); VDAC: Voltage-Dependent Anion-selective Channel vs. β-actin ratio; (<b>E</b>) COX-II: Cytochrome c oxidase subunit II vs. β-actin ratio; (<b>F</b>) COX IV: Cytochrome c oxidase subunit IV vs. β-actin ratio; (<b>G</b>) COX-II/COX-IV ratio; (<b>H</b>) COX-II/VDAC ratio; (<b>I</b>) COX-IV/VDAC ratio. Box and whiskers plots showing median, minimum, and maximum values. # <span class="html-italic">p</span>-value = (0.05–0.1), * <span class="html-italic">p</span>-value &lt; 0.05, ** <span class="html-italic">p</span>-value &lt; 0.01. (<b>J</b>) Representative Western Blot bands for proteins quantification in PBMC from two Naïve HIV patients compared to two patients treated with TDF/EFV/EFV STR for more than one year: β-actin (47 kDa), VDAC (31 kDa), COX-II (25.6 kDa) and COX-VI (15 kDa).</p> Full article ">Figure 3
<p>Inflammatory and soluble mediators in Naïve HIV patients (n = 15) compared to patients treated with cART (combined antiretroviral therapy) based on TDF/FTC/EFV for more than one year (n = 10). (<b>A</b>) TNFα: Tumor Necrosis Factor α levels. (<b>B</b>) IL6: Interleukin 6 values; (<b>C</b>) IL8: Interleukin 8 values; (<b>D</b>) MCP-1: Monocyte Chemoattractant protein 1 levels; (<b>E</b>) NGF: Nerve Growth Factor values; (<b>F</b>) Leptin: Serum Leptin levels; (<b>G</b>) HGF: Hepatocyte Growth Factor levels; (<b>H</b>) FGF21: Fibroblast Growth Factor 21 levels. Box and whiskers plots showing median, minimum, and maximum values. # <span class="html-italic">p</span>-value = (0.05–0.1) * <span class="html-italic">p</span>-value &lt; 0.05.</p> Full article ">Figure 4
<p>Significant correlations between virologic and metabolic parameters with mitochondrial biomarkers in both cohorts. Linear regression line (solid line) and 95% confidence band of the best-fit line (dotted line) are shown. (<b>A</b>) Correlation between mitochondrial DNA content in PBMCs (PBMC-mtDNA) vs. patient viral load; (<b>B</b>) Correlation between PBMC-mtDNA vs. total cholesterol values; (<b>C</b>) Correlation between PBMC-mtDNA vs. LDL values; (<b>D</b>) Correlation between PBMC-mtDNA vs. alkaline phosphatase (ALP) values; (<b>E</b>) Correlation between PBMC-mtDNA vs. Creatine Kinase values. * <span class="html-italic">p</span>-value &lt; 0.05, ** <span class="html-italic">p</span>-value &lt; 0.01.</p> Full article ">Figure 5
<p>Significant correlations between virologic and mitochondrial parameters with inflammatory biomarkers in both cohorts. Linear regression line (solid line) and 95% confidence band of the best-fit line (dotted line) are shown. (<b>A</b>) Correlation between TNFα vs. viral load; (<b>B</b>) Correlation between Tumor Necrosis Factor α (TNFα) vs. IL-8 values; (<b>C</b>) Correlation between TNFα vs. Monocyte Chemoattractant protein 1 (MCP-1) values; (<b>D</b>) Correlation between TNFα vs. mitochondrial DNA in PBMCs; (<b>E</b>) Correlation between IL-6 vs. mitochondrial DNA in plasma. * <span class="html-italic">p</span>-value &lt; 0.05, ** <span class="html-italic">p</span>-value &lt; 0.01, *** <span class="html-italic">p</span>-value &lt; 0.0001.</p> Full article ">

Figure 1
<p>Dose-dependent antiviral activity of fucoidan <b>3</b> (LIF) on syncytia formation in HIV-infected MT-4 cells (pre-treatment of virus). (<b>A</b>) Concentration 25 µg/mL; (<b>B</b>) concentration 50 µg/mL; (<b>C</b>) concentration 100 µg/mL; (<b>D</b>) concentration 150 µg/mL; (<b>E</b>) virus control; (<b>F</b>) cell control.</p> Full article ">Figure 1 Cont.
<p>Dose-dependent antiviral activity of fucoidan <b>3</b> (LIF) on syncytia formation in HIV-infected MT-4 cells (pre-treatment of virus). (<b>A</b>) Concentration 25 µg/mL; (<b>B</b>) concentration 50 µg/mL; (<b>C</b>) concentration 100 µg/mL; (<b>D</b>) concentration 150 µg/mL; (<b>E</b>) virus control; (<b>F</b>) cell control.</p> Full article ">Figure 2
<p>Anti-HIV-1 activity of studied fucoidans in various schemes of treatment with compound. (<b>A</b>) Pre-treatment of the virus; (<b>B</b>) pre-treatment of cells; (<b>C</b>) simultaneous treatment; (<b>D</b>) treatment of infected cells; <b>1</b>—AmF3; <b>2</b>—AoF3; <b>3</b>—LIF; <b>4</b>—ScF; <b>5</b>—SgF2; <b>6</b>—1TbF1.</p> Full article ">Figure 2 Cont.
<p>Anti-HIV-1 activity of studied fucoidans in various schemes of treatment with compound. (<b>A</b>) Pre-treatment of the virus; (<b>B</b>) pre-treatment of cells; (<b>C</b>) simultaneous treatment; (<b>D</b>) treatment of infected cells; <b>1</b>—AmF3; <b>2</b>—AoF3; <b>3</b>—LIF; <b>4</b>—ScF; <b>5</b>—SgF2; <b>6</b>—1TbF1.</p> Full article ">

Figure 1
<p>Changes in four inflammatory markers during three visits. V1, V2, and V3 are the 1st, 2nd, and 3rd visits. Dot plots showing changes in (<b>A</b>) plasma T-Gal9 levels, (<b>B</b>) plasma FL-Gal9 levels, (<b>C</b>) plasma OPN levels, and (<b>D</b>) plasma CRP levels in seronegative and seropositive groups at V1 (baseline), V2 (month 2), and V3 (end of treatment). <span class="html-italic">p</span> values showing significant changes in the levels are indicated as *** (<span class="html-italic">p</span> &lt; 0.001) and **** (<span class="html-italic">p</span> &lt; 0.0001). ns; not significant.</p> Full article ">Figure 2
<p>Changes in inflammatory markers after therapy. (<b>A</b>) Percent changes in the levels of the markers at the end of antituberculosis treatment in seropositive and seronegative groups. (<b>B</b>) The INS of seronegative and seropositive groups. * (<span class="html-italic">p</span> &lt; 0.05).</p> Full article ">

Figure 1
<p>Seven subsets of Th effector cells are currently known, namely Th1, Th2, Th9, Th17, Th22, Tfh, and Tregs. Differentiation into each subtype depends on the cytokine environment present during antigen recognition. In naïve CD4+ T helper cells, these cytokines promote the production of specific transcription factors that determine differentiation into effector cells (Th1, Th2, …). The function of each Th effector cell depends on the production of specific cytokines or direct interaction with other immune cells.</p> Full article ">

Figure 1
<p>Nuclear STAT1 expression in non-parenchymal cells of liver biopsies from people living with HIV with diagnosed metabolic dysfunction-associated steatotic liver disease (different disease groups: steatosis &gt; 30%, steatohepatitis and fibrosis &gt; 0). Representative images of STAT1 immunohistochemistry in hepatic sections from patients with identified liver injury receiving RPV-free or RPV-based therapy. Black arrows indicate positive non-parenchymal cells. Scale bar = 0.1 mm.</p> Full article ">

Figure 1
<p>Geographic Distribution of Hepatitis E Virus (HEV) Seroprevalence in Greece.</p> Full article ">

Figure 1
<p>Patients’ distribution by SARS-CoV-2 serologic status and vaccination/infection history. The classification was based on the presence or absence of SARS-CoV-2 serological markers and self-declared vaccine history.</p> Full article ">Figure 2
<p>Antibody responses according to SARS-CoV-2 infection/vaccination status. V = SARS-CoV-2 vaccinated; I = SARS-CoV-2 infected; V + I = SARS-CoV-2 vaccinated and infected (with hybrid immunity).</p> Full article ">Figure 3
<p>Correlation between anti-S IgG and CD4/CD8 (3A) and between anti-S IgA and CD4/CD8 (3B).</p> Full article ">Figure 4
<p>SARS-CoV-2-specific T-cell responses in HIV-positive subjects. (<b>A</b>). Number of IFN-γ SFU per 10⁶ PBMCs by CD4 counts following stimulation with recombinant SARS-CoV-2 BA.4/BA.5 S1 protein. (<b>B</b>). Correlation between CD4/CD8 ratio in individuals infected with HIV with their total SARS-CoV-2 responses. The non-parametric Spearman test was used for correlation analysis.</p> Full article ">