Journal: Scientific Reports

Article Title: Unbiased approach to identify and assess efficacy of human SARS-CoV-2 neutralizing antibodies

doi: 10.1038/s41598-022-19780-7

Figure Lengend Snippet: Rapid Discovery of Neutralizing Antibodies. ( A ) The G-MAB phage display library was panned for SARS-CoV-2 Spike S1 subunit-binding scFv fragments. Following confirmation of binding activity and blocking of S1:ACE2 interactions by candidate scFvs, the most potent of these candidates were converted to IgG1 antibodies bearing the LALA Fc modification. Candidate nAbs were characterized for binding of Spike S1 subunit and neutralization of related clinical SARS-CoV-2 isolates. Affinity maturation of potent nAbs was carried out in parallel to biophysical profiling, cell line development, and evaluation of protective efficacy for the parental nAbs, S1D2 and S7E3 to yield STI-2020 and STI-5041, respectively. Artwork credit: William SooHoo. ( B ) Affinity measurements of STI-2020 and STI-5041 for Spike S1 domain from the following isolates and VOCs: USA/WA-1/2020(WA-1) isolate, D614G 2020001 isolate, B.1.1.7 VOC (Alpha), B.1.351 VOC (Beta). The antibody affinities were measured using SPR on a BIAcore T200 instrument using a 1:1 binding model. ( C ) Spike protein derived from the WA-1 and 2020001 (D614G) SARS-CoV-2 isolates were independently expressed on the surface of HEK 293 cells. Serially-diluted STI-2020 or STI-5041 were assayed for Spike protein binding by flow cytometry. To quantify antibody binding, mean fluorescent intensity was measured for each dilution tested and the EC 50 value was calculated for each nAb. Representative replicate experiments are shown. ( D ) STI-2020 and STI-5041 were evaluated in neutralizing test for potency against SARS-CoV-2 USA/WA-1/2020, 2020001 (D614G), B.1.1.7 VOC (Alpha), B.1.351 VOC (Beta) and B.1.617.2 (Delta).

Article Snippet: For the pseudovirus neutralization study, codon optimized SARS-CoV-2 Wuhan Spike carrying the D614G amino acid change (Sino Biological, Cat #VG40589-UT(D614G)) was modified to remove the last 21 amino acids at the C-terminus (SpikeΔ21) and was used as the parental clone.

Techniques: Binding Assay, Activity Assay, Blocking Assay, Modification, Neutralization, Derivative Assay, Protein Binding, Flow Cytometry

Journal: Scientific Reports

Article Title: Unbiased approach to identify and assess efficacy of human SARS-CoV-2 neutralizing antibodies

doi: 10.1038/s41598-022-19780-7

Figure Lengend Snippet: Pharmacokinetic and bioavailability of Neutralizing Antibody. ( A ) Neutralization of SARS-CoV-2 Spike-pseudotyped VSV by STI-2020 and STI-5041. VSVΔG-luciferase was pseudotyped with the indicated spike variant, incubated with STI-2020 or STI-5041 at a range of 0.0005–10 µg/mL for 30 min, then added to 293-ACE2 target cells. Absolute IC 50 was calculated from luciferase values and are indicated. Experiments were performed at least three independent times and data presented as the mean ± SD. ( B ) Epitope binning was performed as described in the Materials and Methods. The sensorgram shows STI-5041 can bind to SARS-CoV-2 S1 and STI-2020 complex (blue line) and indicates that STI-5041 and STI-2020 bind to distinct epitopes. ( C–H ) Biodistribution: Concentration of STI-2020 ( C , D ) or 5041 ( E , F ) in serum and lung lavage or lysates of spleens, lungs, small intestines, and large intestines collected from female CD-1 mice administered STI-2020 IV at doses of 0.5 mg/kg (Dark blue circle), 0.05 mg/kg (Sky blue circle), or 0.005 mg/kg (light blue circle) or IN at doses of 2.5 mg/kg (black circle), 0.5 mg/kg (Maroon circle), 0.05 mg/kg (Red Circle), and 0.005 mg/kg (Rose circle) or STI-5041 administered IV at doses of 2 mg/kg (Dark blue circle), 0.2 mg/kg (Sky blue circle), and 0.02 mg/kg (light blue circle) or IN at doses of 10 mg/kg (Black circle), 2 mg/kg (Maroon circle), 0.2 mg/kg (Red circle), and 0.02 mg/kg (Rose circle) at 24 h post-administration as compared to samples collected from untreated mice. Values represent mean ± SEM (n = 3 animals no treatment group, n = 5 in treatment groups). Significant differences are denoted by * p < 0.05; ** p < 0.01; *** p < 0.001, **** p < 0.0001. Pharmacokinetics: Concentration of STI-2020 ( G ) or STI-5041 ( H ) in lungs and isolated serum collected from female CD-1 mice administered STI-2020 or STI-5041 intranasally (IN) at a dose of 5 mg/kg or 20 mg/kg, respectively. Samples from treated mice were collected at the indicated timepoint post-administration; antibody concentrations were quantified by ELISA and compared to samples collected from untreated mice. Overlay of antibody concentrations in lung tissue vs. serum following IN administration of a 5 mg/kg or 20 mg/kg dose. Values represent mean ± SD (n = 3 animals no treatment group, n = 6 per time point in treatment groups).

Article Snippet: For the pseudovirus neutralization study, codon optimized SARS-CoV-2 Wuhan Spike carrying the D614G amino acid change (Sino Biological, Cat #VG40589-UT(D614G)) was modified to remove the last 21 amino acids at the C-terminus (SpikeΔ21) and was used as the parental clone.

Techniques: Neutralization, Luciferase, Variant Assay, Incubation, Concentration Assay, Isolation, Enzyme-linked Immunosorbent Assay

Journal: Scientific Reports

Article Title: Unbiased approach to identify and assess efficacy of human SARS-CoV-2 neutralizing antibodies

doi: 10.1038/s41598-022-19780-7

Figure Lengend Snippet: Efficacy of Intravenous (IV) Delivery of Neutralizing Antibodies in the golden (Syrian) Hamster Model of COVID-19. Female hamsters were inoculated with SARS-CoV-2 USA/WA-1/2020 ( A , B ) or SARS-CoV-2 Beta variant ( C , D ) on day 0. One-hour post-infection, animals were administered a single intravenous dose of Isotype control IgG (500 µg) or, For A and B, STI-2020 (100 µg, 300 µg, or 500 µg); For C and D, Isotype control IgG (1,000 µg) or STI-5041 (500 µg, or 1,000 µg). Weight changes were recorded for up to 11 days. ( A ) Average % weight change ± SEM was plotted for each group. Days in which there was a significant difference in average % weight change compared to Isotype control IgG 500 µg-treated animals are denoted by * ( p -value < 0.05). ( B ) Lung tissues collected from five animals per group and virus titers were determined on day 5. A broken line indicates the detection limit of the assay (< 1.5 TCID 50 /g). ( C ) Average % weight change ± SEM was plotted for each group. Days in which there was a significant difference in average % weight change for STI-5041 at 500 µg or 1,000 µg compared to Isotype control IgG 1000 µg-treated animals are denoted by * ( p -value < 0.05). ( D ) Lung tissues collected from five animals per group administered Isotype control IgG (1,000 µg) or STI-5041 (500 µg or 1,000 µg) and virus titers were determined on day 5.

Article Snippet: For the pseudovirus neutralization study, codon optimized SARS-CoV-2 Wuhan Spike carrying the D614G amino acid change (Sino Biological, Cat #VG40589-UT(D614G)) was modified to remove the last 21 amino acids at the C-terminus (SpikeΔ21) and was used as the parental clone.

Techniques: Variant Assay, Infection, Control, Virus

Journal: Scientific Reports

Article Title: Unbiased approach to identify and assess efficacy of human SARS-CoV-2 neutralizing antibodies

doi: 10.1038/s41598-022-19780-7

Figure Lengend Snippet: Efficacy of Intranasal (IN) Delivery of Neutralizing Antibodies in the golden (Syrian) Hamster Model of COVID-19. ( A , B ) Female hamsters were inoculated with SARS-CoV-2 USA/WA-1/2020, and then administrated with 500 µg or 400 µg Isotype control antibody or 500 µg or 400 µg STI-2020 intranasally at 12 h post-infection. ( A ) Average % weight change ± SEM was plotted for each group. Days in which there was a significant difference in average % weight change for STI-5020 at 500 µg compared to Isotype control IgG 500 µg-treated animals are denoted by * ( p -value < 0.05). ( B ) Upper panels show representative figures of nasal turbinates and nasal septum at 5 d.p.i. Average ± SEM of OE thickness on the nasal septum in the lower graph for STI-5020 at 400 µg compared to Isotype control IgG 400 µg-treated animals are denoted with * ( p -value < 0.05). ( C ) Hamsters were inoculated with SARS-CoV-2 Beta variant, and then administrated with 500 µg Isotype control antibody or 100 µg, 300 µg, or 500 µg STI-5041 intranasally at 12 h post-infection. Average % weight change ± SEM was plotted for each group.

Article Snippet: For the pseudovirus neutralization study, codon optimized SARS-CoV-2 Wuhan Spike carrying the D614G amino acid change (Sino Biological, Cat #VG40589-UT(D614G)) was modified to remove the last 21 amino acids at the C-terminus (SpikeΔ21) and was used as the parental clone.

Techniques: Control, Infection, Variant Assay

Journal: Frontiers in Immunology

Article Title: Indoleamine 2, 3-Dioxygenase 1 Mediates Survival Signals in Chronic Lymphocytic Leukemia via Kynurenine/Aryl Hydrocarbon Receptor-Mediated MCL1 Modulation

doi: 10.3389/fimmu.2022.832263

Figure Lengend Snippet: CLL cells up-regulate IDO1 in response to stimuli that mimic microenvironmental signals. (A) Purified leukemic CD19 + cells from CLL patients were serum starved for 1 h. Then the basal level of IDO1 was inspected by Western blot (n = 8) and illustrated by a bar diagram. (B) Flow cytometric histograms represent a high IDO1 level in CD19 + cells treated for 24 h with IFN-γ compared to the untreated control sample and isotype sample. (C) Bar diagram represents IDO1 expression in CD19 + CLL measured by real-time PCR. Samples were treated for 4 h with one of microenvironment stimuli individually (Student paired t test, *p < 0.05, **p < 0.01; n = 5). (D) Immunoblots represent IDO1 protein induction after 24 h of stimulation with the abovementioned factors. Histograms below represent the densitometric quantifications (Student paired t test, *p < 0.05, **p < 0.01; n = 5).

Article Snippet: Briefly, 5 × 10 6 CD19 + CLL cells were transfected with 10 μg of IDO1 plasmid vector (Cat# HG11650-NF) or the corresponding empty vector pCMV3-Negative Control (Cat# CV020) (all from Sino Biological Inc., Shanghai, China).

Techniques: Purification, Western Blot, Expressing, Real-time Polymerase Chain Reaction

Journal: Frontiers in Immunology

Article Title: Indoleamine 2, 3-Dioxygenase 1 Mediates Survival Signals in Chronic Lymphocytic Leukemia via Kynurenine/Aryl Hydrocarbon Receptor-Mediated MCL1 Modulation

doi: 10.3389/fimmu.2022.832263

Figure Lengend Snippet: IDO1 protein induction and activity can be regulated by IFN-γ in CLL. (A) Purified CLL cells were pretreated with two doses (0.1–1 μM) of INCB018424 for 1 h prior to IFN-γ stimulation for 24 h. Immunoblots depict IDO1, tSTAT1, and pSTAT1 protein levels in a representative case. Histograms on the right represent the densitometric quantifications of IDO1 and pSTAT1/tSTAT1 in 5 CLL samples (Student paired t test, *p < 0.05; n = 5). (B) Immunofluorescence staining shows the ability of INCB018424 1 μM to reduce IDO1 expression induced by IFN-γ. Scale bar is 20 µm. Box plots summarize the fluorescent levels in DMSO, IFN-γ, or IFN-γ + INCB018424-treated CLL cells (Student paired t test, *p < 0.05; n = 9). (C) Conditioned media were collected after INCB018424 pretreatment (or not) and IFN-γ incubation for 24 h. Dot plots on the left represent the mean of the Kyn concentration measured by LC-MS/MS analytical technique in 5 separated experiments (Student paired t test, *p < 0.05, **p < 0.01; n = 5). The central dot plots represent the mean of the Trp concentration (Student paired t test, *p < 0.05, ***p < 0.001; n = 5). The resultant [Kyn]/[Trp] ratio calculated is depicted in the right dot plot (Student paired t test, *p < 0.05, **p < 0.01; n = 5).

Article Snippet: Briefly, 5 × 10 6 CD19 + CLL cells were transfected with 10 μg of IDO1 plasmid vector (Cat# HG11650-NF) or the corresponding empty vector pCMV3-Negative Control (Cat# CV020) (all from Sino Biological Inc., Shanghai, China).

Techniques: Activity Assay, Purification, Western Blot, Immunofluorescence, Staining, Expressing, Incubation, Concentration Assay, Liquid Chromatography with Mass Spectroscopy

Journal: Frontiers in Immunology

Article Title: Indoleamine 2, 3-Dioxygenase 1 Mediates Survival Signals in Chronic Lymphocytic Leukemia via Kynurenine/Aryl Hydrocarbon Receptor-Mediated MCL1 Modulation

doi: 10.3389/fimmu.2022.832263

Figure Lengend Snippet: CLL cell survival is promoted by IDO1 overexpression. (A) CLL cells were transfected with an IDO1-expressing vector or an empty vector. After 24 h from transfection, the IDO1 protein level was measured by Western blot. Bar diagrams represent the densitometric quantifications of IDO1 (Student paired t test, *p < 0.05; n = 5). (B) Conditioned media were collected 24 h post transfection with the IDO1 vector or empty vector. Dot plots on the left represent the mean of the Kyn concentration measured by HPLC in 8 separated experiments (Student paired t test, **p < 0.01; n = 8). The central dot plots represent the mean of the Trp concentration (Student paired t test, *p < 0.05; n = 8). The resultant [Kyn]/[Trp] ratio calculated is depicted in the right dot plot (Student paired t test, **p < 0.01; n = 8). (C) Box plots represent the percentage of viable CLL cells after 24 h of transfection with IDO1-expressing vector or empty vector (Student paired t test, *p < 0.05; n = 5). (D) Box plots represent the percentage of CLL cell viability measured after 48 h of stimulation with Kyn 100 µM (Student paired t test, **p < 0.01; n = 6).

Article Snippet: Briefly, 5 × 10 6 CD19 + CLL cells were transfected with 10 μg of IDO1 plasmid vector (Cat# HG11650-NF) or the corresponding empty vector pCMV3-Negative Control (Cat# CV020) (all from Sino Biological Inc., Shanghai, China).

Techniques: Over Expression, Transfection, Expressing, Plasmid Preparation, Western Blot, Concentration Assay

Journal: Frontiers in Immunology

Article Title: Indoleamine 2, 3-Dioxygenase 1 Mediates Survival Signals in Chronic Lymphocytic Leukemia via Kynurenine/Aryl Hydrocarbon Receptor-Mediated MCL1 Modulation

doi: 10.3389/fimmu.2022.832263

Figure Lengend Snippet: The activity of IDO1/Kyn/AHR axis impairs CLL cells response to ABT-199. (A) Histograms show comparison on viability rate of CLL cells treated with 1 nM ABT-199 for 5 h after overnight stimulation with 100 µM Kyn (repeated-measure two-way ANOVA with Kyn and CH-223191 treatment groups as the two factors; n = 11). (B) CLL cells were pretreated for 90 min with 10 µM CH-223191 and cultured overnight with Kyn. Then, 1 nM ABT-199 was added to culture for 5 h prior to cell viability assessment. Histograms illustrate the synergistic effect of CH-223191 with ABT-199 in CLL cells (repeated-measure three-way ANOVA with Kyn, ABT-199, and CH-223191 treatment groups as the three factors; n = 7). (C) CD19+ cells were cultured overnight with 100 µM Kyn, and then 100 or 300 nM AMG-176 was added to culture for 5 h. Cell viability was measured and depicted in histograms (repeated-measure two-way ANOVA with Kyn and AMG-176 treatment groups as the two factors; n = 12).

Article Snippet: Briefly, 5 × 10 6 CD19 + CLL cells were transfected with 10 μg of IDO1 plasmid vector (Cat# HG11650-NF) or the corresponding empty vector pCMV3-Negative Control (Cat# CV020) (all from Sino Biological Inc., Shanghai, China).

Techniques: Activity Assay, Cell Culture

Journal: Biochemical and biophysical research communications

Article Title: Characterization of an anti-FLAG antibody binding protein in V. cholerae

doi: 10.1016/j.bbrc.2020.05.169

Figure Lengend Snippet: (A) Construction of 3×FLAG tag fusion proteins. 3×FLAG peptide was fused after N-terminus signal sequences of Protein A and B, or at C-terminus region of Protein C for quantification of protein levels. (B) Detection of non-specific protein by anti-FLAG antibody in both wild type and 3×FLAG fusion strains (C) Growth phase dependent induction of anti-FLAG antibody binding protein. Lag, lag phase; Log, exponential phase; Sta, stationary phase.

Article Snippet: Wild type V. cholerae and 3×FLAG tag+ ProteinA fusion strains were grown in LB medium to mid-logarithmic phase (at an OD 600 ~0.5) and then 20 ml cell cultures were spun down at 4830 rcf for 10 min.

Techniques: Binding Assay

Journal: Biochemical and biophysical research communications

Article Title: Characterization of an anti-FLAG antibody binding protein in V. cholerae

doi: 10.1016/j.bbrc.2020.05.169

Figure Lengend Snippet: (A-B) Silver-stained (A) or zinc-stained (B) protein gel demonstrating effective IP with FLAG antibody resin. (C) Western Blot showing excision of non-specific protein-containing region from the gel in (B). Each half volume of eluted sample from IP was loaded in two wells of 10% SDS-PAGE gel; one for positive control of western blotting and the other for in-gel tryptic digestion. (D) Venn diagram showing number of detected total proteins from IP/LC-MS/MS of the size-selected gel band in wild type and 3×FLAG fusion strain.

Article Snippet: Wild type V. cholerae and 3×FLAG tag+ ProteinA fusion strains were grown in LB medium to mid-logarithmic phase (at an OD 600 ~0.5) and then 20 ml cell cultures were spun down at 4830 rcf for 10 min.

Techniques: Staining, Western Blot, SDS Page, Positive Control, Liquid Chromatography with Mass Spectroscopy

Journal: Biochemical and biophysical research communications

Article Title: Characterization of an anti-FLAG antibody binding protein in V. cholerae

doi: 10.1016/j.bbrc.2020.05.169

Figure Lengend Snippet: (A) Construction of overexpression vectors for 6xHis tag fusion proteins. A 6xHis tag was fused to the N-terminus region of all proteins (OmpA, Porin4, VxrB, ShyA, and Bacillus subtilis MntR) and overproduced in E. coli followed by detection via anti-His and anti-Flag Western Blot. Vec, empty vector. Black stars or red stars indicate bands recognized by anti-His antibody or anti-FLAG antibody, respectively. Blue star presents the band detected by both antibodies. (B) Amino acid sequence alignment between 3×FLAG tag and the relevant parts of Porin4 protein reveals the putatively FLAG-antibody-reactive Porin4 tag. Identical residues are highlighted yellow.

Article Snippet: Wild type V. cholerae and 3×FLAG tag+ ProteinA fusion strains were grown in LB medium to mid-logarithmic phase (at an OD 600 ~0.5) and then 20 ml cell cultures were spun down at 4830 rcf for 10 min.

Techniques: Over Expression, Western Blot, Plasmid Preparation, Sequencing

Journal: bioRxiv

Article Title: H3.3K4M destabilizes enhancer epigenomic writers MLL3/4 and impairs adipose tissue development

doi: 10.1101/301986

Figure Lengend Snippet: (a) Schematic of lox-STOP-lox-H3.3K4M (LSL-K4M) transgene and breeding scheme. The LSL-K4M transgene consists of the following elements from 5’ to 3’: a CAG promoter, quadruple copies of SV40 stop signals flanked by two loxP sites, H3.3K4M with C-terminal FLAG and HA tags, and polyadenylation signal. LSL-K4M transgenic mice were crossed with Myf5 - Cre to generate mice expressing ectopic H3.3K4M in brown adipose tissue (BAT) and muscle. The locations of PCR genotyping primers P1 and P2 are indicated by arrows. (b) PCR genotyping of LSL-K4M transgenic mice. (c) Genotype of progeny from crossing between LSL-K4M and Myf5 - Cre at 3 weeks age, new born pups (P0) and E18.5 embryos. LSL-K4M; Myf5 - Cre mice died soon after birth from breathing malfunction due to defects in muscles of the rib cage. (d) Representative morphology of P0 pups. (e) Representative morphology of E18.5 embryos. (f) Histological analysis of E18.5 embryos. Sagittal sections of cervical/thoracic area were stained with H&E (left panels) or with antibodies against the BAT (B) marker UCP1 (green) and the muscle (M) marker Myosin (red) (right panels). Scale bar = 80 μm.

Article Snippet: To generate LSL-K4M transgenic mice, H3.3K4M and a 3’ FLAG tag (H3.3K4M-FLAG) were fused downstream of CAG promoter with a loxP-STOP-loxP cassette in the middle of the pBT346.6 plasmid (AST-3029, Applied StemCell) ( ).

Techniques: Transgenic Assay, Expressing, Staining, Marker

Journal: bioRxiv

Article Title: H3.3K4M destabilizes enhancer epigenomic writers MLL3/4 and impairs adipose tissue development

doi: 10.1101/301986

Figure Lengend Snippet: Immortalized LSL-K4M; Cre - ER brown preadipocytes were treated with 4-hydroxytamoxifen (4OHT) to induce ectopic H3.3K4M expression, followed by adipogenesis assay. (a–b) H3.3K4M destabilizes MLL3/4 proteins. Histone extracts (a) or nuclear extracts (b) were analyzed by Western blot using antibodies indicated on the left. (c–e) H3.3K4M prevents adipogenesis and induction of adipocyte genes. (c) Cell growth rates. 5 × 10 5 preadipocytes were plated at D0 and the cumulative cell numbers were determined every day for 5 days. (d) Oil red O staining at day 7 (D7) of adipogenesis. (e) qRT-PCR of H3.3K4M-FLAG, Pparg , Cebpa , Fabp4 and Ucp1 expression at D0 and D7 of adipogenesis. (f-h) RNA-seq analyses were performed at D7 of adipogenesis. (f-g) Identification (f) and heat map (g) of down- or up-regulated genes in H3.3K4M-expressing cells. The cut-off for differential expression is 2.5- fold. (h) Gene ontology (GO) analysis of gene groups defined in (f).

Article Snippet: To generate LSL-K4M transgenic mice, H3.3K4M and a 3’ FLAG tag (H3.3K4M-FLAG) were fused downstream of CAG promoter with a loxP-STOP-loxP cassette in the middle of the pBT346.6 plasmid (AST-3029, Applied StemCell) ( ).

Techniques: Expressing, Western Blot, Staining, Quantitative RT-PCR, RNA Sequencing Assay

Journal: bioRxiv

Article Title: H3.3K4M destabilizes enhancer epigenomic writers MLL3/4 and impairs adipose tissue development

doi: 10.1101/301986

Figure Lengend Snippet: 4OHT-treated LSL-K4M; Cre - ER brown preadipocytes were collected at D4 of adipogenesis for ChIP-seq of H3K4me1 and H3K27ac (a-b), ChIP of MLL4, H3K4me1, H3K27ac, BRD4, MEDI and Pol II, and qRT-PCR of eRNAs (c-e). (a-b) Heat maps (a) and average profiles (b) around MLL4 + active enhancers during adipogenesis. (c) Genome browser view of H3K4me1 and H3K27ac on Pparg and Cebpa gene loci during adipogenesis with schematic of genomic locations of representative MLL4+ active enhancers (e1-e5). MLL4 binding data were obtained from . (d) ChIP-qPCR analyses of indicated factors are shown on enhancers e1-e5 at D0 and D4 of adipogenesis. An enhancer of constitutively expressed gene Jak1 was chosen as negative control (n). (e) qRT-PCR of eRNA transcription on enhancers e1-e5 at D0 and D4 of adipogenesis. (f) Proposed model showing that H3.3K4M prevents enhancer activation in adipogenesis by destabilizing MLL3/4.

Article Snippet: To generate LSL-K4M transgenic mice, H3.3K4M and a 3’ FLAG tag (H3.3K4M-FLAG) were fused downstream of CAG promoter with a loxP-STOP-loxP cassette in the middle of the pBT346.6 plasmid (AST-3029, Applied StemCell) ( ).

Techniques: ChIP-sequencing, Quantitative RT-PCR, Binding Assay, Negative Control, Activation Assay

Journal: Cell

Article Title: Replication Fork Activation Is Enabled by a Single-Stranded DNA Gate in CMG Helicase

doi: 10.1016/j.cell.2019.06.032

Figure Lengend Snippet: EXPERIMENTAL MODEL AND SUBJECT DETAILS

Article Snippet: 3 x Flag-tag , EZBiolab , Cat# cp7204.

Techniques: Virus, Recombinant, Protease Inhibitor, Recombinase Polymerase Amplification, Purification, Plasmid Preparation, Software