pbluescript sk(ii) rna expression vector Search Results


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OriGene shrna vectors
<t>Bnip3</t> cooperates with AIF to induce apoptosis and cavitation. (A) 4-d AIF y/+ and AIF y/− EBs were analyzed by immunoblotting for AIF. Actin was used as a loading control. (B) EBs were cultured for 1–4 d and analyzed by immunoblotting for cleaved caspase-3 (cas-3) and actin. Ablation of AIF inhibited caspase-3 activation. (C) Live-phase micrographs show cavitation delay in AIF y/− EBs cultured for 4, 5, and 7 d. After 10 d, most of the AIF y/− EBs were cavitated similar to AIF y/+ EBs. Bars, 100 µm. (D) 4-d EBs were immunostained for cleaved caspase-3. F-actin was stained with rhodamine-phalloidin to show the apical actin belt. Ablation of AIF inhibited apoptosis of the core cells. 5-d EBs were immunostained for the apical marker MUPP1. Apical polarization of the AIF y/− epiblast was not affected despite delayed lumen clearance. (E) AIF y/− ES cells were stably transfected with Bnip3 <t>shRNA</t> (Bnip3 knockdown [KD]) or GFP. 5-d EBs were analyzed by immunoblotting for Bnip3 and cleaved caspase-3. Bnip3 silencing in AIF y/− EBs further inhibited caspase-3 activation. (F) AIF y/+ EBs expressing GFP and AIF y/− EBs stably transfected with Bnip3 shRNA or GFP were cultured for 4, 5, and 7 d. EB cavitation was quantitated by phase microscopy. EB cavitation was significantly delayed in the absence of AIF. Knockdown of Bnip3 in AIF y/− EBs nearly blocked cavitation. n = 6 independent experiments with a total of 529–808 EBs counted for each group. Error bars represent the mean ± SD. *, P < 0.01 versus AIF y/+ GFP; # , P < 0.01 versus AIF y/− GFP.
Shrna Vectors, supplied by OriGene, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/pbluescript+sk%28ii%29+rna+expression+vector/pmc03392936-240-2-22?v=OriGene
Average 90 stars, based on 1 article reviews
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Becton Dickinson rnai-ready psiren-retroq-dsred-express retrovirus vector
<t>Bnip3</t> cooperates with AIF to induce apoptosis and cavitation. (A) 4-d AIF y/+ and AIF y/− EBs were analyzed by immunoblotting for AIF. Actin was used as a loading control. (B) EBs were cultured for 1–4 d and analyzed by immunoblotting for cleaved caspase-3 (cas-3) and actin. Ablation of AIF inhibited caspase-3 activation. (C) Live-phase micrographs show cavitation delay in AIF y/− EBs cultured for 4, 5, and 7 d. After 10 d, most of the AIF y/− EBs were cavitated similar to AIF y/+ EBs. Bars, 100 µm. (D) 4-d EBs were immunostained for cleaved caspase-3. F-actin was stained with rhodamine-phalloidin to show the apical actin belt. Ablation of AIF inhibited apoptosis of the core cells. 5-d EBs were immunostained for the apical marker MUPP1. Apical polarization of the AIF y/− epiblast was not affected despite delayed lumen clearance. (E) AIF y/− ES cells were stably transfected with Bnip3 <t>shRNA</t> (Bnip3 knockdown [KD]) or GFP. 5-d EBs were analyzed by immunoblotting for Bnip3 and cleaved caspase-3. Bnip3 silencing in AIF y/− EBs further inhibited caspase-3 activation. (F) AIF y/+ EBs expressing GFP and AIF y/− EBs stably transfected with Bnip3 shRNA or GFP were cultured for 4, 5, and 7 d. EB cavitation was quantitated by phase microscopy. EB cavitation was significantly delayed in the absence of AIF. Knockdown of Bnip3 in AIF y/− EBs nearly blocked cavitation. n = 6 independent experiments with a total of 529–808 EBs counted for each group. Error bars represent the mean ± SD. *, P < 0.01 versus AIF y/+ GFP; # , P < 0.01 versus AIF y/− GFP.
Rnai Ready Psiren Retroq Dsred Express Retrovirus Vector, supplied by Becton Dickinson, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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<t>Bnip3</t> cooperates with AIF to induce apoptosis and cavitation. (A) 4-d AIF y/+ and AIF y/− EBs were analyzed by immunoblotting for AIF. Actin was used as a loading control. (B) EBs were cultured for 1–4 d and analyzed by immunoblotting for cleaved caspase-3 (cas-3) and actin. Ablation of AIF inhibited caspase-3 activation. (C) Live-phase micrographs show cavitation delay in AIF y/− EBs cultured for 4, 5, and 7 d. After 10 d, most of the AIF y/− EBs were cavitated similar to AIF y/+ EBs. Bars, 100 µm. (D) 4-d EBs were immunostained for cleaved caspase-3. F-actin was stained with rhodamine-phalloidin to show the apical actin belt. Ablation of AIF inhibited apoptosis of the core cells. 5-d EBs were immunostained for the apical marker MUPP1. Apical polarization of the AIF y/− epiblast was not affected despite delayed lumen clearance. (E) AIF y/− ES cells were stably transfected with Bnip3 <t>shRNA</t> (Bnip3 knockdown [KD]) or GFP. 5-d EBs were analyzed by immunoblotting for Bnip3 and cleaved caspase-3. Bnip3 silencing in AIF y/− EBs further inhibited caspase-3 activation. (F) AIF y/+ EBs expressing GFP and AIF y/− EBs stably transfected with Bnip3 shRNA or GFP were cultured for 4, 5, and 7 d. EB cavitation was quantitated by phase microscopy. EB cavitation was significantly delayed in the absence of AIF. Knockdown of Bnip3 in AIF y/− EBs nearly blocked cavitation. n = 6 independent experiments with a total of 529–808 EBs counted for each group. Error bars represent the mean ± SD. *, P < 0.01 versus AIF y/+ GFP; # , P < 0.01 versus AIF y/− GFP.
Mirvanatm Rna Isolation Kit, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 97/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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<t>Bnip3</t> cooperates with AIF to induce apoptosis and cavitation. (A) 4-d AIF y/+ and AIF y/− EBs were analyzed by immunoblotting for AIF. Actin was used as a loading control. (B) EBs were cultured for 1–4 d and analyzed by immunoblotting for cleaved caspase-3 (cas-3) and actin. Ablation of AIF inhibited caspase-3 activation. (C) Live-phase micrographs show cavitation delay in AIF y/− EBs cultured for 4, 5, and 7 d. After 10 d, most of the AIF y/− EBs were cavitated similar to AIF y/+ EBs. Bars, 100 µm. (D) 4-d EBs were immunostained for cleaved caspase-3. F-actin was stained with rhodamine-phalloidin to show the apical actin belt. Ablation of AIF inhibited apoptosis of the core cells. 5-d EBs were immunostained for the apical marker MUPP1. Apical polarization of the AIF y/− epiblast was not affected despite delayed lumen clearance. (E) AIF y/− ES cells were stably transfected with Bnip3 <t>shRNA</t> (Bnip3 knockdown [KD]) or GFP. 5-d EBs were analyzed by immunoblotting for Bnip3 and cleaved caspase-3. Bnip3 silencing in AIF y/− EBs further inhibited caspase-3 activation. (F) AIF y/+ EBs expressing GFP and AIF y/− EBs stably transfected with Bnip3 shRNA or GFP were cultured for 4, 5, and 7 d. EB cavitation was quantitated by phase microscopy. EB cavitation was significantly delayed in the absence of AIF. Knockdown of Bnip3 in AIF y/− EBs nearly blocked cavitation. n = 6 independent experiments with a total of 529–808 EBs counted for each group. Error bars represent the mean ± SD. *, P < 0.01 versus AIF y/+ GFP; # , P < 0.01 versus AIF y/− GFP.
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<t>Bnip3</t> cooperates with AIF to induce apoptosis and cavitation. (A) 4-d AIF y/+ and AIF y/− EBs were analyzed by immunoblotting for AIF. Actin was used as a loading control. (B) EBs were cultured for 1–4 d and analyzed by immunoblotting for cleaved caspase-3 (cas-3) and actin. Ablation of AIF inhibited caspase-3 activation. (C) Live-phase micrographs show cavitation delay in AIF y/− EBs cultured for 4, 5, and 7 d. After 10 d, most of the AIF y/− EBs were cavitated similar to AIF y/+ EBs. Bars, 100 µm. (D) 4-d EBs were immunostained for cleaved caspase-3. F-actin was stained with rhodamine-phalloidin to show the apical actin belt. Ablation of AIF inhibited apoptosis of the core cells. 5-d EBs were immunostained for the apical marker MUPP1. Apical polarization of the AIF y/− epiblast was not affected despite delayed lumen clearance. (E) AIF y/− ES cells were stably transfected with Bnip3 <t>shRNA</t> (Bnip3 knockdown [KD]) or GFP. 5-d EBs were analyzed by immunoblotting for Bnip3 and cleaved caspase-3. Bnip3 silencing in AIF y/− EBs further inhibited caspase-3 activation. (F) AIF y/+ EBs expressing GFP and AIF y/− EBs stably transfected with Bnip3 shRNA or GFP were cultured for 4, 5, and 7 d. EB cavitation was quantitated by phase microscopy. EB cavitation was significantly delayed in the absence of AIF. Knockdown of Bnip3 in AIF y/− EBs nearly blocked cavitation. n = 6 independent experiments with a total of 529–808 EBs counted for each group. Error bars represent the mean ± SD. *, P < 0.01 versus AIF y/+ GFP; # , P < 0.01 versus AIF y/− GFP.
Exosomal Rna Purification Mini Kit, supplied by Norgen Biotek, used in various techniques. Bioz Stars score: 96/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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<t>Bnip3</t> cooperates with AIF to induce apoptosis and cavitation. (A) 4-d AIF y/+ and AIF y/− EBs were analyzed by immunoblotting for AIF. Actin was used as a loading control. (B) EBs were cultured for 1–4 d and analyzed by immunoblotting for cleaved caspase-3 (cas-3) and actin. Ablation of AIF inhibited caspase-3 activation. (C) Live-phase micrographs show cavitation delay in AIF y/− EBs cultured for 4, 5, and 7 d. After 10 d, most of the AIF y/− EBs were cavitated similar to AIF y/+ EBs. Bars, 100 µm. (D) 4-d EBs were immunostained for cleaved caspase-3. F-actin was stained with rhodamine-phalloidin to show the apical actin belt. Ablation of AIF inhibited apoptosis of the core cells. 5-d EBs were immunostained for the apical marker MUPP1. Apical polarization of the AIF y/− epiblast was not affected despite delayed lumen clearance. (E) AIF y/− ES cells were stably transfected with Bnip3 <t>shRNA</t> (Bnip3 knockdown [KD]) or GFP. 5-d EBs were analyzed by immunoblotting for Bnip3 and cleaved caspase-3. Bnip3 silencing in AIF y/− EBs further inhibited caspase-3 activation. (F) AIF y/+ EBs expressing GFP and AIF y/− EBs stably transfected with Bnip3 shRNA or GFP were cultured for 4, 5, and 7 d. EB cavitation was quantitated by phase microscopy. EB cavitation was significantly delayed in the absence of AIF. Knockdown of Bnip3 in AIF y/− EBs nearly blocked cavitation. n = 6 independent experiments with a total of 529–808 EBs counted for each group. Error bars represent the mean ± SD. *, P < 0.01 versus AIF y/+ GFP; # , P < 0.01 versus AIF y/− GFP.
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<t>Bnip3</t> cooperates with AIF to induce apoptosis and cavitation. (A) 4-d AIF y/+ and AIF y/− EBs were analyzed by immunoblotting for AIF. Actin was used as a loading control. (B) EBs were cultured for 1–4 d and analyzed by immunoblotting for cleaved caspase-3 (cas-3) and actin. Ablation of AIF inhibited caspase-3 activation. (C) Live-phase micrographs show cavitation delay in AIF y/− EBs cultured for 4, 5, and 7 d. After 10 d, most of the AIF y/− EBs were cavitated similar to AIF y/+ EBs. Bars, 100 µm. (D) 4-d EBs were immunostained for cleaved caspase-3. F-actin was stained with rhodamine-phalloidin to show the apical actin belt. Ablation of AIF inhibited apoptosis of the core cells. 5-d EBs were immunostained for the apical marker MUPP1. Apical polarization of the AIF y/− epiblast was not affected despite delayed lumen clearance. (E) AIF y/− ES cells were stably transfected with Bnip3 <t>shRNA</t> (Bnip3 knockdown [KD]) or GFP. 5-d EBs were analyzed by immunoblotting for Bnip3 and cleaved caspase-3. Bnip3 silencing in AIF y/− EBs further inhibited caspase-3 activation. (F) AIF y/+ EBs expressing GFP and AIF y/− EBs stably transfected with Bnip3 shRNA or GFP were cultured for 4, 5, and 7 d. EB cavitation was quantitated by phase microscopy. EB cavitation was significantly delayed in the absence of AIF. Knockdown of Bnip3 in AIF y/− EBs nearly blocked cavitation. n = 6 independent experiments with a total of 529–808 EBs counted for each group. Error bars represent the mean ± SD. *, P < 0.01 versus AIF y/+ GFP; # , P < 0.01 versus AIF y/− GFP.
Qiaamp Viral Rna Mini Kit, supplied by Qiagen, used in various techniques. Bioz Stars score: 99/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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<t>Bnip3</t> cooperates with AIF to induce apoptosis and cavitation. (A) 4-d AIF y/+ and AIF y/− EBs were analyzed by immunoblotting for AIF. Actin was used as a loading control. (B) EBs were cultured for 1–4 d and analyzed by immunoblotting for cleaved caspase-3 (cas-3) and actin. Ablation of AIF inhibited caspase-3 activation. (C) Live-phase micrographs show cavitation delay in AIF y/− EBs cultured for 4, 5, and 7 d. After 10 d, most of the AIF y/− EBs were cavitated similar to AIF y/+ EBs. Bars, 100 µm. (D) 4-d EBs were immunostained for cleaved caspase-3. F-actin was stained with rhodamine-phalloidin to show the apical actin belt. Ablation of AIF inhibited apoptosis of the core cells. 5-d EBs were immunostained for the apical marker MUPP1. Apical polarization of the AIF y/− epiblast was not affected despite delayed lumen clearance. (E) AIF y/− ES cells were stably transfected with Bnip3 <t>shRNA</t> (Bnip3 knockdown [KD]) or GFP. 5-d EBs were analyzed by immunoblotting for Bnip3 and cleaved caspase-3. Bnip3 silencing in AIF y/− EBs further inhibited caspase-3 activation. (F) AIF y/+ EBs expressing GFP and AIF y/− EBs stably transfected with Bnip3 shRNA or GFP were cultured for 4, 5, and 7 d. EB cavitation was quantitated by phase microscopy. EB cavitation was significantly delayed in the absence of AIF. Knockdown of Bnip3 in AIF y/− EBs nearly blocked cavitation. n = 6 independent experiments with a total of 529–808 EBs counted for each group. Error bars represent the mean ± SD. *, P < 0.01 versus AIF y/+ GFP; # , P < 0.01 versus AIF y/− GFP.
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<t>Bnip3</t> cooperates with AIF to induce apoptosis and cavitation. (A) 4-d AIF y/+ and AIF y/− EBs were analyzed by immunoblotting for AIF. Actin was used as a loading control. (B) EBs were cultured for 1–4 d and analyzed by immunoblotting for cleaved caspase-3 (cas-3) and actin. Ablation of AIF inhibited caspase-3 activation. (C) Live-phase micrographs show cavitation delay in AIF y/− EBs cultured for 4, 5, and 7 d. After 10 d, most of the AIF y/− EBs were cavitated similar to AIF y/+ EBs. Bars, 100 µm. (D) 4-d EBs were immunostained for cleaved caspase-3. F-actin was stained with rhodamine-phalloidin to show the apical actin belt. Ablation of AIF inhibited apoptosis of the core cells. 5-d EBs were immunostained for the apical marker MUPP1. Apical polarization of the AIF y/− epiblast was not affected despite delayed lumen clearance. (E) AIF y/− ES cells were stably transfected with Bnip3 <t>shRNA</t> (Bnip3 knockdown [KD]) or GFP. 5-d EBs were analyzed by immunoblotting for Bnip3 and cleaved caspase-3. Bnip3 silencing in AIF y/− EBs further inhibited caspase-3 activation. (F) AIF y/+ EBs expressing GFP and AIF y/− EBs stably transfected with Bnip3 shRNA or GFP were cultured for 4, 5, and 7 d. EB cavitation was quantitated by phase microscopy. EB cavitation was significantly delayed in the absence of AIF. Knockdown of Bnip3 in AIF y/− EBs nearly blocked cavitation. n = 6 independent experiments with a total of 529–808 EBs counted for each group. Error bars represent the mean ± SD. *, P < 0.01 versus AIF y/+ GFP; # , P < 0.01 versus AIF y/− GFP.
Allprep Dna Rna Mini Kit, supplied by Qiagen, used in various techniques. Bioz Stars score: 99/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Clinical Information and Resistance-Related Amino Acid Substitutions of Patients Who Harbored Primary Resistance to Antiretroviral Drugs
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Clinical Information and Resistance-Related Amino Acid Substitutions of Patients Who Harbored Primary Resistance to Antiretroviral Drugs
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FIGURE 1 Global analysis and distribution of <t>miRNA-seq</t> in RA and SSc monocytes. Heatmap of significantly dysregulated miRNA in RA (A) and SSc (B) monocytes compared to HC. Principal component analysis (PCA) plot of global miRNA distribution in RA (green), SSc (blue) and HC (red) monocytes (C). Enrichment analysis of abundantly expressed miRNA regulating selected genes involved in immune pathways in RA (D) and SSc monocytes (E). Heatmap analysis of selected miRNA in RA (F) and SSc (G) monocytes compared to HC.
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Image Search Results


Bnip3 cooperates with AIF to induce apoptosis and cavitation. (A) 4-d AIF y/+ and AIF y/− EBs were analyzed by immunoblotting for AIF. Actin was used as a loading control. (B) EBs were cultured for 1–4 d and analyzed by immunoblotting for cleaved caspase-3 (cas-3) and actin. Ablation of AIF inhibited caspase-3 activation. (C) Live-phase micrographs show cavitation delay in AIF y/− EBs cultured for 4, 5, and 7 d. After 10 d, most of the AIF y/− EBs were cavitated similar to AIF y/+ EBs. Bars, 100 µm. (D) 4-d EBs were immunostained for cleaved caspase-3. F-actin was stained with rhodamine-phalloidin to show the apical actin belt. Ablation of AIF inhibited apoptosis of the core cells. 5-d EBs were immunostained for the apical marker MUPP1. Apical polarization of the AIF y/− epiblast was not affected despite delayed lumen clearance. (E) AIF y/− ES cells were stably transfected with Bnip3 shRNA (Bnip3 knockdown [KD]) or GFP. 5-d EBs were analyzed by immunoblotting for Bnip3 and cleaved caspase-3. Bnip3 silencing in AIF y/− EBs further inhibited caspase-3 activation. (F) AIF y/+ EBs expressing GFP and AIF y/− EBs stably transfected with Bnip3 shRNA or GFP were cultured for 4, 5, and 7 d. EB cavitation was quantitated by phase microscopy. EB cavitation was significantly delayed in the absence of AIF. Knockdown of Bnip3 in AIF y/− EBs nearly blocked cavitation. n = 6 independent experiments with a total of 529–808 EBs counted for each group. Error bars represent the mean ± SD. *, P < 0.01 versus AIF y/+ GFP; # , P < 0.01 versus AIF y/− GFP.

Journal: The Journal of Cell Biology

Article Title: Bnip3 and AIF cooperate to induce apoptosis and cavitation during epithelial morphogenesis

doi: 10.1083/jcb.201111063

Figure Lengend Snippet: Bnip3 cooperates with AIF to induce apoptosis and cavitation. (A) 4-d AIF y/+ and AIF y/− EBs were analyzed by immunoblotting for AIF. Actin was used as a loading control. (B) EBs were cultured for 1–4 d and analyzed by immunoblotting for cleaved caspase-3 (cas-3) and actin. Ablation of AIF inhibited caspase-3 activation. (C) Live-phase micrographs show cavitation delay in AIF y/− EBs cultured for 4, 5, and 7 d. After 10 d, most of the AIF y/− EBs were cavitated similar to AIF y/+ EBs. Bars, 100 µm. (D) 4-d EBs were immunostained for cleaved caspase-3. F-actin was stained with rhodamine-phalloidin to show the apical actin belt. Ablation of AIF inhibited apoptosis of the core cells. 5-d EBs were immunostained for the apical marker MUPP1. Apical polarization of the AIF y/− epiblast was not affected despite delayed lumen clearance. (E) AIF y/− ES cells were stably transfected with Bnip3 shRNA (Bnip3 knockdown [KD]) or GFP. 5-d EBs were analyzed by immunoblotting for Bnip3 and cleaved caspase-3. Bnip3 silencing in AIF y/− EBs further inhibited caspase-3 activation. (F) AIF y/+ EBs expressing GFP and AIF y/− EBs stably transfected with Bnip3 shRNA or GFP were cultured for 4, 5, and 7 d. EB cavitation was quantitated by phase microscopy. EB cavitation was significantly delayed in the absence of AIF. Knockdown of Bnip3 in AIF y/− EBs nearly blocked cavitation. n = 6 independent experiments with a total of 529–808 EBs counted for each group. Error bars represent the mean ± SD. *, P < 0.01 versus AIF y/+ GFP; # , P < 0.01 versus AIF y/− GFP.

Article Snippet: Four pGFP-V-RS–based shRNA vectors targeting to mouse Bnip3 and four pRFP-V-RS–based vectors targeting to Bim together with scrambled controls were purchased from OriGene.

Techniques: Western Blot, Cell Culture, Activation Assay, Staining, Marker, Stable Transfection, Transfection, shRNA, Expressing, Microscopy

Clinical Information and Resistance-Related Amino Acid Substitutions of Patients Who Harbored Primary Resistance to Antiretroviral Drugs

Journal: AIDS Research and Human Retroviruses

Article Title: Transmitted Antiretroviral Drug Resistance and Thumb Subdomain Polymorphisms Among Newly HIV Type 1 Diagnosed Patients Infected with CRF01_AE and CRF07_BC Virus in Guangdong Province, China

doi: 10.1089/aid.2011.0320

Figure Lengend Snippet: Clinical Information and Resistance-Related Amino Acid Substitutions of Patients Who Harbored Primary Resistance to Antiretroviral Drugs

Article Snippet: HIV-1 RNA was extracted from 200 μl of HIV-1-positive plasma using the DaAn Gene nucleotide extraction kit (DaAn Gene Diagnostic Center of Sun Yat-sen University, Guangzhou, China) according to the manufacturer's instructions.

Techniques: Cell Counting

The phylogenetic tree was created based on the neighbor-joining method and the Kimura two-parameter distance estimation method with the protease (PR) and reverse transcriptase (RT) sequences of HIV-1 obtained from newly diagnosed drug-naive patients in this study. The reference sequences of recombinant types used in the comparative phylogenetic analysis were CRF01_AE: U51188, AF197340, and AF197341; CRF_07BC: AF286226, AF03396, and AF286230. The simian immunodeficiency virus sequence AF103818 was used as the outgroup sequence. ▲ represents the sequences of CRF01_AE; △ represents the sequences of CRF_07BC. The bootstrap values (1025 replicates) over 70% are marked at the major branches of the tree. The scale bar represents 0.02 nucleotide substitution per site between the sequences.

Journal: AIDS Research and Human Retroviruses

Article Title: Transmitted Antiretroviral Drug Resistance and Thumb Subdomain Polymorphisms Among Newly HIV Type 1 Diagnosed Patients Infected with CRF01_AE and CRF07_BC Virus in Guangdong Province, China

doi: 10.1089/aid.2011.0320

Figure Lengend Snippet: The phylogenetic tree was created based on the neighbor-joining method and the Kimura two-parameter distance estimation method with the protease (PR) and reverse transcriptase (RT) sequences of HIV-1 obtained from newly diagnosed drug-naive patients in this study. The reference sequences of recombinant types used in the comparative phylogenetic analysis were CRF01_AE: U51188, AF197340, and AF197341; CRF_07BC: AF286226, AF03396, and AF286230. The simian immunodeficiency virus sequence AF103818 was used as the outgroup sequence. ▲ represents the sequences of CRF01_AE; △ represents the sequences of CRF_07BC. The bootstrap values (1025 replicates) over 70% are marked at the major branches of the tree. The scale bar represents 0.02 nucleotide substitution per site between the sequences.

Article Snippet: HIV-1 RNA was extracted from 200 μl of HIV-1-positive plasma using the DaAn Gene nucleotide extraction kit (DaAn Gene Diagnostic Center of Sun Yat-sen University, Guangzhou, China) according to the manufacturer's instructions.

Techniques: Reverse Transcription, Recombinant, Virus, Sequencing

FIGURE 1 Global analysis and distribution of miRNA-seq in RA and SSc monocytes. Heatmap of significantly dysregulated miRNA in RA (A) and SSc (B) monocytes compared to HC. Principal component analysis (PCA) plot of global miRNA distribution in RA (green), SSc (blue) and HC (red) monocytes (C). Enrichment analysis of abundantly expressed miRNA regulating selected genes involved in immune pathways in RA (D) and SSc monocytes (E). Heatmap analysis of selected miRNA in RA (F) and SSc (G) monocytes compared to HC.

Journal: Frontiers in immunology

Article Title: Circulating miRNA-19b as a biomarker of disease progression and treatment response to baricitinib in rheumatoid arthritis patients through miRNA profiling of monocytes.

doi: 10.3389/fimmu.2023.980247

Figure Lengend Snippet: FIGURE 1 Global analysis and distribution of miRNA-seq in RA and SSc monocytes. Heatmap of significantly dysregulated miRNA in RA (A) and SSc (B) monocytes compared to HC. Principal component analysis (PCA) plot of global miRNA distribution in RA (green), SSc (blue) and HC (red) monocytes (C). Enrichment analysis of abundantly expressed miRNA regulating selected genes involved in immune pathways in RA (D) and SSc monocytes (E). Heatmap analysis of selected miRNA in RA (F) and SSc (G) monocytes compared to HC.

Article Snippet: Circulating miRNA validation in RA and SSc sera and RA synovial fluids The volume of 300 μl of sera or plasma from SSc (n=10), RA (n=44) patients and and HC (n=37) patients was used to isolate circulating miRNA using NucleoSpin® miRNA plasma/serum (Macherey–Nagel, Germany) according to the manufacturer’s protocol.

Techniques:

FIGURE 2 The level of circulating miRNA in RA and SSc patients. The level of miRNA-19b-3p (A), miRNA-29c-5p (B), miRNA-374a-5p (C), miRNA-503-5p (D), miRNA-589-5p (E), miRNA-3614-5p (F) in sera of RA and SSc patients compared to HC. P-values were expressed as follows: ns for not significant; 0.05 > P > 0.01 as *; 0.01 > P > 0.001 as **; P < 0.001 as ***, P <0.0001 as ****.

Journal: Frontiers in immunology

Article Title: Circulating miRNA-19b as a biomarker of disease progression and treatment response to baricitinib in rheumatoid arthritis patients through miRNA profiling of monocytes.

doi: 10.3389/fimmu.2023.980247

Figure Lengend Snippet: FIGURE 2 The level of circulating miRNA in RA and SSc patients. The level of miRNA-19b-3p (A), miRNA-29c-5p (B), miRNA-374a-5p (C), miRNA-503-5p (D), miRNA-589-5p (E), miRNA-3614-5p (F) in sera of RA and SSc patients compared to HC. P-values were expressed as follows: ns for not significant; 0.05 > P > 0.01 as *; 0.01 > P > 0.001 as **; P < 0.001 as ***, P <0.0001 as ****.

Article Snippet: Circulating miRNA validation in RA and SSc sera and RA synovial fluids The volume of 300 μl of sera or plasma from SSc (n=10), RA (n=44) patients and and HC (n=37) patients was used to isolate circulating miRNA using NucleoSpin® miRNA plasma/serum (Macherey–Nagel, Germany) according to the manufacturer’s protocol.

Techniques:

FIGURE 3 The levels of circulating miRNA in body fluids of eRA and aRA patients. The levels of miRNA-19b-3p (A), miRNA-29c-5p (B), miRNA-374a-5p (C), miRNA-503-5p (D), miRNA-589-5p (E), miRNA-3614-5p (F) in sera or eRA and aRA and SF of aRA patients compared to HC. P-values were expressed as follows: ns for not significant; 0.05 > P > 0.01 as *; 0.01 > P > 0.001 as **; P < 0.001 as ***, P <0.0001 as ****.

Journal: Frontiers in immunology

Article Title: Circulating miRNA-19b as a biomarker of disease progression and treatment response to baricitinib in rheumatoid arthritis patients through miRNA profiling of monocytes.

doi: 10.3389/fimmu.2023.980247

Figure Lengend Snippet: FIGURE 3 The levels of circulating miRNA in body fluids of eRA and aRA patients. The levels of miRNA-19b-3p (A), miRNA-29c-5p (B), miRNA-374a-5p (C), miRNA-503-5p (D), miRNA-589-5p (E), miRNA-3614-5p (F) in sera or eRA and aRA and SF of aRA patients compared to HC. P-values were expressed as follows: ns for not significant; 0.05 > P > 0.01 as *; 0.01 > P > 0.001 as **; P < 0.001 as ***, P <0.0001 as ****.

Article Snippet: Circulating miRNA validation in RA and SSc sera and RA synovial fluids The volume of 300 μl of sera or plasma from SSc (n=10), RA (n=44) patients and and HC (n=37) patients was used to isolate circulating miRNA using NucleoSpin® miRNA plasma/serum (Macherey–Nagel, Germany) according to the manufacturer’s protocol.

Techniques:

FIGURE 4 KEGG pathway analysis of selected 6 miRNA candidates and their potential target genes. The identification of specific pathways (A) and their downstream genes (B) including HLA-DOA and HLA-DQA1, which were predicted to be negatively regulated by significantly changed miRNA in RA patients, using the Diana-miPath tool. The fold change analysis of expression level of HLA class II genes between HC and RA monocytes from RNA- seq (B) based of FDR < 0.01 and p-values < 0.05.

Journal: Frontiers in immunology

Article Title: Circulating miRNA-19b as a biomarker of disease progression and treatment response to baricitinib in rheumatoid arthritis patients through miRNA profiling of monocytes.

doi: 10.3389/fimmu.2023.980247

Figure Lengend Snippet: FIGURE 4 KEGG pathway analysis of selected 6 miRNA candidates and their potential target genes. The identification of specific pathways (A) and their downstream genes (B) including HLA-DOA and HLA-DQA1, which were predicted to be negatively regulated by significantly changed miRNA in RA patients, using the Diana-miPath tool. The fold change analysis of expression level of HLA class II genes between HC and RA monocytes from RNA- seq (B) based of FDR < 0.01 and p-values < 0.05.

Article Snippet: Circulating miRNA validation in RA and SSc sera and RA synovial fluids The volume of 300 μl of sera or plasma from SSc (n=10), RA (n=44) patients and and HC (n=37) patients was used to isolate circulating miRNA using NucleoSpin® miRNA plasma/serum (Macherey–Nagel, Germany) according to the manufacturer’s protocol.

Techniques: Expressing, RNA Sequencing

FIGURE 5 The levels of circulating miRNA in HC and RA patients upon baricitinib therapy. The levels of miRNA-19b-3p (A), miRNA-29c-5p (B), miRNA-374a-5p (C), miRNA-503-5p (D), miRNA-589-5p (E), miRNA-3614-5p (F) before and 3 months after baricitinib treatment in RA patients compared to HC. ROC analysis of changes/delta in miRNA-19b-3p and miRNA-503-5p expression and CRP level upon JAKi therapy (G). Correlation analysis between the expression of delta miRNA-19b-3p and delta DAS28 in baricitinib-treated RA patients (H). P-values were expressed as follows: ns for not significant; 0.05 > P > 0.01 as *; 0.01 > P > 0.001 as **; P < 0.001 as ***, P <0.0001 as ****.

Journal: Frontiers in immunology

Article Title: Circulating miRNA-19b as a biomarker of disease progression and treatment response to baricitinib in rheumatoid arthritis patients through miRNA profiling of monocytes.

doi: 10.3389/fimmu.2023.980247

Figure Lengend Snippet: FIGURE 5 The levels of circulating miRNA in HC and RA patients upon baricitinib therapy. The levels of miRNA-19b-3p (A), miRNA-29c-5p (B), miRNA-374a-5p (C), miRNA-503-5p (D), miRNA-589-5p (E), miRNA-3614-5p (F) before and 3 months after baricitinib treatment in RA patients compared to HC. ROC analysis of changes/delta in miRNA-19b-3p and miRNA-503-5p expression and CRP level upon JAKi therapy (G). Correlation analysis between the expression of delta miRNA-19b-3p and delta DAS28 in baricitinib-treated RA patients (H). P-values were expressed as follows: ns for not significant; 0.05 > P > 0.01 as *; 0.01 > P > 0.001 as **; P < 0.001 as ***, P <0.0001 as ****.

Article Snippet: Circulating miRNA validation in RA and SSc sera and RA synovial fluids The volume of 300 μl of sera or plasma from SSc (n=10), RA (n=44) patients and and HC (n=37) patients was used to isolate circulating miRNA using NucleoSpin® miRNA plasma/serum (Macherey–Nagel, Germany) according to the manufacturer’s protocol.

Techniques: Expressing