Journal: Oncogene

Article Title: Interaction between HIV-1 Tat and pRb2/p130: a possible mechanism in the pathogenesis of AIDS-related neoplasms.

doi: 10.1038/sj.onc.1206637

Figure Lengend Snippet: Figure 1 Tat and pRb2/p130 interact through the pocket region of p130. (a) The product of pRb2/130 deleted of the carboxyl- terminal domain is still able to bind to Tat. (b) The protein deleted of the amino-terminus of pRb2/p130 still retains its ability to interact with Tat. (c) WB with an anti-Tat antibody of the sample immunoprecipitated with anti-Tat. DC: pRb2/p130 deleted of the carboxyl-terminal domain. DN: pRb2/p130 deleted of the amino- terminal domain. NRS: normal rabbit serum; CE: cell extract; IP: immunoprecipitated sample

Article Snippet: Western blotting (WB) was performed with both monoclonal anti-pRb2/p130 antibody (Transduction Laboratory, UK) at a dilution of 1 : 400 and polyclonal anti-pRb2/p130 (Rockland) at a dilution of 1 : 400.

Techniques: Immunoprecipitation

Journal: Oncogene

Article Title: Interaction between HIV-1 Tat and pRb2/p130: a possible mechanism in the pathogenesis of AIDS-related neoplasms.

doi: 10.1038/sj.onc.1206637

Figure Lengend Snippet: Figure 2 RB2/p130 mRNA increases in the presence of Tat, In 293 cells transfected with Tat, mRNA levels for pRb2/p130 dramatically increase if compared to the wild-type cells, suggesting that Tat alters the transcription/translation rate for pRb2/p130

Article Snippet: Western blotting (WB) was performed with both monoclonal anti-pRb2/p130 antibody (Transduction Laboratory, UK) at a dilution of 1 : 400 and polyclonal anti-pRb2/p130 (Rockland) at a dilution of 1 : 400.

Techniques: Transfection

Journal: Oncogene

Article Title: Interaction between HIV-1 Tat and pRb2/p130: a possible mechanism in the pathogenesis of AIDS-related neoplasms.

doi: 10.1038/sj.onc.1206637

Figure Lengend Snippet: Figure 3 The phosphorylation status of pRb2/p130 is not altered in the presence of Tat. 293 cells treated with extracellular Tat were monitored for the phosphorylation status of pRb2/p130. No significant difference was observed after Tat treatment if compared to the untreated cells

Article Snippet: Western blotting (WB) was performed with both monoclonal anti-pRb2/p130 antibody (Transduction Laboratory, UK) at a dilution of 1 : 400 and polyclonal anti-pRb2/p130 (Rockland) at a dilution of 1 : 400.

Techniques: Phospho-proteomics

Journal: Oncogene

Article Title: Interaction between HIV-1 Tat and pRb2/p130: a possible mechanism in the pathogenesis of AIDS-related neoplasms.

doi: 10.1038/sj.onc.1206637

Figure Lengend Snippet: Figure 4 Tat inhibits the growth control exerted by pRb2/p130. T98G cells transfected with Tat and pRb2/p130, alone or in combination, were positively selected for resistance to G-418. The addition of Tat to the culture determines the loss of the growth control mediated by pRb2/p130. The number of colonies observed in the sample, which overexpress both Tat and pRb2/p130, was comparable to those of the negative control containing the empty vector

Article Snippet: Western blotting (WB) was performed with both monoclonal anti-pRb2/p130 antibody (Transduction Laboratory, UK) at a dilution of 1 : 400 and polyclonal anti-pRb2/p130 (Rockland) at a dilution of 1 : 400.

Techniques: Control, Transfection, Negative Control, Plasmid Preparation

Journal: Oncogene

Article Title: Interaction between HIV-1 Tat and pRb2/p130: a possible mechanism in the pathogenesis of AIDS-related neoplasms.

doi: 10.1038/sj.onc.1206637

Figure Lengend Snippet: Figure 5 Tat does not compete with E2F-4 in binding to pRb2/ p130. A luciferase assay was performed on samples transfected with Tat and pRb2/p130, alone or in combination. Cotransfection of pRb2/p130 and Tat did not result in an increase in the activation of a promoter responsive to E2F-4, suggesting that E2F-4 is not released in the presence of Tat alone

Article Snippet: Western blotting (WB) was performed with both monoclonal anti-pRb2/p130 antibody (Transduction Laboratory, UK) at a dilution of 1 : 400 and polyclonal anti-pRb2/p130 (Rockland) at a dilution of 1 : 400.

Techniques: Binding Assay, Luciferase, Transfection, Cotransfection, Activation Assay

Journal: The EMBO Journal

Article Title: Micropeptide hSPAR regulates glutamine levels and suppresses mammary tumor growth via a TRIM21-P27KIP1-mTOR axis

doi: 10.1038/s44318-024-00359-z

Figure Lengend Snippet: Reagents and tools table

Article Snippet: The membranes were blocked in 5% BSA (Sangon, China) for 1 h at room temperature, and then incubated at 4 °C overnight with primary antibody GAPDH (Proteintech, USA, 60004-1-Ig), hSPAR (HuaBio, China), Flag (Abcam, UK, ab205606), β-Tubulin (Proteintech, USA, 10068-1-AP), FIBRILLARIN (Proteintech, USA, 16021-1-AP), ATPV1A (Proteintech, USA, 14418-1-AP), LAMP2 (CST, USA, 49067), TRIM21 (Proteintech, USA, 67136-1-Ig), P27KIP1 (Proteintech, USA, 25614-1-AP), phospho-P27KIP1 (Abcam, USA, ab75908), SKP2 (Proteintech, USA, 15010-1-AP), SLC7A1 (Proteintech, USA, 14195-1-AP), SLC7A5 (Proteintech, USA, 28670-1-AP), phospho-mTOR (CST, USA, 5536), mTOR (CST, USA, 2983), phospho-S6K (CST, USA, 9234), S6K (CST, USA, 2708), phospho-S6 (CST, USA, 2211), S6 (CST, USA, 2217), phospho-AKT (CST, USA, 4060), AKT (CST, USA, 9272), Ubiquitin (Abcam, UK, ab134953), SLC38A2 (ImmunoWay, USA, YT4354), LAMTOR1(CST, USA, 8975), LAMTOR2 (CST, USA, 8145), LAMTOR3 (Proteintech, USA, 14492-1-AP), LAMTOR4 (CST, USA, 13140), LAMTOR5 (Proteintech, USA,11937-1-AP), RagA (CST, USA, 4357S) and TAT (Abcam, UK, ab42359).

Techniques: Recombinant, Sequencing, Modification, Membrane, Lysis, Transfection, Magnetic Beads, Software, Cytometry, In Vitro, cDNA Synthesis, Plasmid Preparation, Isolation, Mutagenesis, Silver Staining