Establishment of a rhabdoid tumor cell line with a specific chromosomal abnormality, 46,XY,t(11;22)(p15.5;q11.23)

1991 ◽  
Vol 56 (1) ◽  
pp. 31-38 ◽  
Author(s):  
Pamela S. Karnes ◽  
Tuan N. Tran ◽  
Mei Ying Cui ◽  
Emil Bogenmann ◽  
Hiroyuki Shimada ◽  
...  
Author(s):  
Tohru Sugimoto ◽  
Hajime Hosoi ◽  
Yoshihiro Horii ◽  
Hiroyuki Ishida ◽  
Hiroshi Mine ◽  
...  

2019 ◽  
Vol 6 ◽  
Author(s):  
Elizaveta Fasler-Kan ◽  
Nijas Aliu ◽  
Frank-Martin Haecker ◽  
Natalia Maltsev ◽  
Sabrina Ruggiero ◽  
...  

2021 ◽  
Author(s):  
Natalia Milosevich ◽  
Chelsea Wilson ◽  
Tyler Brown ◽  
Aktan Alpsoy ◽  
Sijie Wang ◽  
...  

Methyllysine reader proteins bind to methylated lysine residues and alter gene transcription by changing the compaction state of chromatin or by the recruitment of other multiprotein complexes. The polycomb paralog family of methyllysine readers bind to trimethylated lysine on the tail of histone 3 via a highly conserved aromatic cage located in their chromodomains. Each of the polycomb paralogs are implicated in several disease states. CBX6 and CBX8 are members of the polycomb paralog family with two structurally similar chromodomains. By exploring the structure-activity relationships of a previously reported CBX6 inhibitor we have discovered more potent and cell permeable analogs. Our current report includes potent, dual-selective inhibitors of CBX6 and CBX8. We have shown that the –2 position in our scaffold is an important residue for selectivity amongst the polycomb paralogs. Preliminary cell-based studies show that the new inhibitors impact cell proliferation in a rhabdoid tumor cell line. This report includes data on inhibitor design, inhibitor synthesis, compound characterization by LCMS, compound activity by fluorescence polarization, analysis of structure-activity relationships, rhabdoid tumor cell line activity.


1989 ◽  
Vol 41 (2) ◽  
pp. 276-277 ◽  
Author(s):  
P.S. Karnes ◽  
T.N. Tran ◽  
H.Y. Ho ◽  
D.T. Boquiren ◽  
M.Y. Cui ◽  
...  

2018 ◽  
Vol 2 (3) ◽  
Author(s):  
Emily Kunce Stroup ◽  
Yunku Yeu ◽  
Albert Budhipramono ◽  
Tae Hyun Hwang ◽  
Dinesh Rakheja ◽  
...  

2021 ◽  
Author(s):  
Natalia Milosevich ◽  
Chelsea Wilson ◽  
Tyler Brown ◽  
Aktan Alpsoy ◽  
Sijie Wang ◽  
...  

Methyllysine reader proteins bind to methylated lysine residues and alter gene transcription by changing the compaction state of chromatin or by the recruitment of other multiprotein complexes. The polycomb paralog family of methyllysine readers bind to trimethylated lysine on the tail of histone 3 via a highly conserved aromatic cage located in their chromodomains. Each of the polycomb paralogs are implicated in several disease states. CBX6 and CBX8 are members of the polycomb paralog family with two structurally similar chromodomains. By exploring the structure-activity relationships of a previously reported CBX6 inhibitor we have discovered more potent and cell permeable analogs. Our current report includes potent, dual-selective inhibitors of CBX6 and CBX8. We have shown that the –2 position in our scaffold is an important residue for selectivity amongst the polycomb paralogs. Preliminary cell-based studies show that the new inhibitors impact cell proliferation in a rhabdoid tumor cell line. This report includes data on inhibitor design, inhibitor synthesis, compound characterization by LCMS, compound activity by fluorescence polarization, analysis of structure-activity relationships, rhabdoid tumor cell line activity.


1983 ◽  
Vol 48 (2) ◽  
pp. 377-383 ◽  
Author(s):  
E Knust ◽  
W Dietrich ◽  
B Fleckenstein ◽  
W Bodemer

2019 ◽  
Vol 26 (09) ◽  
pp. 1950058
Author(s):  
SADEQ H. LAFTA ◽  
ALI ABDULRAHMAN TAHA ◽  
MUHAMMAD M. FARHAN ◽  
SHAIMA Y. ABDULFATTAH

Nanoparticles of alpha ferric oxide ([Formula: see text]-Fe2O3) were prepared by the hydrothermal method. Structural properties of [Formula: see text]-Fe2O3 were determined by XRD, SEM and AFM measurements. The particles had a good matching with standard pattern. Average particle size was about 90[Formula: see text]nm and the distribution extended from about 20[Formula: see text]nm to 120[Formula: see text]nm. Biocompatibility study of ferric oxide nanoparticles against bacteria, parasites, tumor cell line and normal cells was determined. No antibacterial activity was observed for the concentration, of ferric oxide nanoparticles in distilled water, up to 1.5[Formula: see text]mg/ml vs. E. coli and S. aureus. Moreover, MTT assay was used to determine the cytotoxicity against parasites and cells. Intermediate cytotoxicity (53.30%) of 1.5[Formula: see text]mg/ml of prepared nanoparticles was noted against L. tropica, while weak cytotoxicity of 5.20% was observed against L. donovani at the same concentration of ferric oxide nanoparticles. On the other hand, the prepared nanoparticles revealed low cytotoxicity (47.28%) against SR tumor cell line, while no cytotoxicity was shown against lymphocytes, as a model of normal cells.


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