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Image Search Results
Journal: bioRxiv
Article Title: The nuclear oncoprotein SET is necessary for MLL/KMT2A binding and transcriptional elongation
doi: 10.64898/2026.02.26.708410
Figure Lengend Snippet: A: IGV snapshot depicting ChIP profiles of Mll-N, H3K4me3, RNAPolII (total), RNAPolII-Ser5P, and RNAPolII-Ser2P at the promoter of the Set target Med23 . B: Metagene plots across all Set activated genes reveal a specific loss of Mll and elongating RNA polymerase from chromatin after Set depletion. C: Only promoter recruited PP2A can repress the MLL responsive human Meis1 promoter. The reporter construct was co-transfected with expression constructs as indicated and luciferase results were determined in triplicate experiments. D: Recruitment of Set and PP2A to the endogenous Meis1 promoter in myeloid precursor cells. Effectors were targeted to the murine Meis1 promoter in MLL-ENL transformed cells by a fusion with catalytically inactive Cas9 (dCas9) in combination either with a non-targeting (vec) or two Meis1 promoter specific sgRNAs. Meis1 output was measured by RT-qPCR in triplicates.
Article Snippet: Set : Invitrogen (#MA5-35772); MLL: CST (#8178) mixed 1:1 with anti-MLLN, Upstate (Temecula, CA, #05-764) 10 μl AB-mix per 5×10e6 cells, H3K4me3: CST (#9751), RNAPolymeraseII: CST (#14958),
Techniques: Construct, Transfection, Expressing, Luciferase, Transformation Assay, Quantitative RT-PCR
Journal: PLOS Pathogens
Article Title: Mutations accumulated in the Spike of SARS-CoV-2 Omicron allow for more efficient counteraction of the restriction factor BST2/Tetherin
doi: 10.1371/journal.ppat.1011912
Figure Lengend Snippet: Resources.
Article Snippet: Mouse mAb anti-SARS-CoV-2 S (S1-NTD) ,
Techniques: Virus, Variant Assay, Recombinant, Plasmid Preparation, In Vitro, Transfection, cDNA Synthesis, Lysis, Magnetic Beads, Enzyme-linked Immunosorbent Assay, SYBR Green Assay, Software
Journal: The Journal of Biological Chemistry
Article Title: PAM forms an atypical SCF ubiquitin ligase complex that ubiquitinates and degrades NMNAT2
doi: 10.1074/jbc.RA118.002176
Figure Lengend Snippet: FBXO45 facilitates assembly of a ubiquitin ligase complex containing SKP1 and PAM. A and B, schematics for different constructs tested for PAM (A) and FBXO45 (B). Annotated and highlighted in color are domains in PAM and FBXO45. C, coIP from transfected 293 cells showing HA–SKP1 binds GFP–FBXO45 but fails to bind GFP–PAM N-terminal (-term), GFP–PAM central, and GFP–PAM C-terminal constructs. D, coIP of HA–SKP1 with GFP–PAM D5 only occurs in the presence of FLAG–FBXO45 (upper coIP panel). HA–SKP1 coIPs with FLAG–FBXO45 in the presence or absence of GFP–PAM D5 (lower coIP panel). E, HA–SKP1 does not coIP with full-length GFP–PAM, but binding occurs in the presence of FLAG–FBXO45 (upper coIP panel). HA–SKP1 coIPs with FLAG–FBXO45 in the presence or absence of GFP–PAM (lower coIP panel). F, coIP showing HA–SKP1 binds the F-box domain of FBXO45. GFP–PAM (G) and FLAG–FBXO45 (H) fail to coIP with MYC–CUL1. I, summary showing interactions between SKP1, FBXO45, and PAM. C–H, shown are representatives of at least three independent experiments IP, immunoprecipitation.
Article Snippet: We thank Dr. Manfred Gessler for HA–SKP1 plasmid, Dr. Aaron DiAntonio for NMNAT2–MYC-HIS 6 plasmid, and Dr. Ning Zheng for
Techniques: Ubiquitin Proteomics, Construct, Transfection, Binding Assay, Immunoprecipitation
Journal: The Journal of Biological Chemistry
Article Title: PAM forms an atypical SCF ubiquitin ligase complex that ubiquitinates and degrades NMNAT2
doi: 10.1074/jbc.RA118.002176
Figure Lengend Snippet: Comparison of noncanonical PAM/FBXO45/SKP1 complex with traditional SCF ubiquitin ligase complex. A, summary of biochemistry underpinning formation of the PAM/FBXO45/SKP1 complex, which ubiquitinates NMNAT2 and targets it for proteasomal degradation. The F-box protein FBXO45 binds directly to the FBD1 domain of PAM and recognizes NMNAT2 as a target for ubiquitination. SKP1 acts as an auxiliary component that increases FBXO45 binding to NMNAT2. B, diagram of traditional SCF complex formed by RBX1/CUL1/SKP1/SKP2 (adapted from Zheng et al. (8)).
Article Snippet: We thank Dr. Manfred Gessler for HA–SKP1 plasmid, Dr. Aaron DiAntonio for NMNAT2–MYC-HIS 6 plasmid, and Dr. Ning Zheng for
Techniques: Comparison, Ubiquitin Proteomics, Binding Assay