Výsledky vyhledávání - "Keelan Z. Guiley"

Akademický článek

The MuvB complex binds and stabilizes nucleosomes downstream of the transcription start site of cell-cycle dependent genes

Autor: Anushweta Asthana, Parameshwaran Ramanan, Alexander Hirschi, Keelan Z. Guiley, Tilini U. Wijeratne, Robert Shelansky, Michael J. Doody, Haritha Narasimhan, Hinrich Boeger, Sarvind Tripathi, Gerd A. Müller, Seth M. Rubin

Publikováno v: Nature Communications, Vol 13, Iss 1, Pp 1-15 (2022)

The MuvB protein complex regulates genes that are differentially expressed through the cell cycle, yet its precise molecular function has remained unclear. Here the authors reveal MuvB associates with the nucleosome adjacent to the transcription star

Externí odkaz: https://doaj.org/article/f0c4fe55cb71405cb91f1d9f5b878250

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Akademický článek

A long lost key opens an ancient lock: Drosophila Myb causes a synthetic multivulval phenotype in nematodes

Autor: Paul J. Vorster, Paul Goetsch, Tilini U. Wijeratne, Keelan Z. Guiley, Laura Andrejka, Sarvind Tripathi, Braden J. Larson, Seth M. Rubin, Susan Strome, Joseph S. Lipsick

Publikováno v: Biology Open, Vol 9, Iss 5 (2020)

The five-protein MuvB core complex is highly conserved in animals. This nuclear complex interacts with RB-family tumor suppressor proteins and E2F-DP transcription factors to form DREAM complexes that repress genes that regulate cell cycle progressio

Externí odkaz: https://doaj.org/article/5af2d70fe94a4b07b07a96c7fd3de521

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Supplementary Figure 2 from A Small Molecule Reacts with the p53 Somatic Mutant Y220C to Rescue Wild-type Thermal Stability

Autor: Kevan M. Shokat, Keelan Z. Guiley

Supplementary Figure S2: Differential scanning fluorimetry (A) Carbazole series plot of average values from differential scanning fluorimetry. (B) Indole series plot of average values from differential scanning fluorimetry. (C) Azaindole series plot

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b805e24073f0f441ab6f04be5a0008f5
https://doi.org/10.1158/2159-8290.22541697.v1

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Supplementary Figure 4 from A Small Molecule Reacts with the p53 Somatic Mutant Y220C to Rescue Wild-type Thermal Stability

Autor: Kevan M. Shokat, Keelan Z. Guiley

Supplementary Figure S4: Ligand electron density maps (A) 1σ 2Fo-Fc electron density map and 1.5σ Fo-Fc simulated annealing omit density map for KG3. (B) 1σ 2Fo-Fc electron density map and 1.5σ Fo-Fc simulated annealing omit density map for KG6.

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::23bea8b629c85527cff6bdb7873aba26
https://doi.org/10.1158/2159-8290.22541691

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Supplementary Figure 3 from A Small Molecule Reacts with the p53 Somatic Mutant Y220C to Rescue Wild-type Thermal Stability

Autor: Kevan M. Shokat, Keelan Z. Guiley

Supplementary Figure S3: Example LC/MS spectra from carbazole and indole series (A) LC/MS spectra from p53 WT-CL or p53 Y220C-CL labeling with KG1. (B) LC/MS spectra from p53 WT or p53 Y220C labeling with KG5. (C) LC/MS spectra from p53 WT or p53 Y22

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::403d8bd66f1e7c288bd7455ca7048b6b
https://doi.org/10.1158/2159-8290.22541694

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Supplementary Figure 1 from A Small Molecule Reacts with the p53 Somatic Mutant Y220C to Rescue Wild-type Thermal Stability

Autor: Kevan M. Shokat, Keelan Z. Guiley

Supplementary Figure S1: p53 hotspot mutations (A) Crystal structure of p53 bound to DNA PDB 1TUP with structural and DNA-contact mutations highlighted. (B) Frequency of hotspot mutations out of total p53 alterations based upon data generated by the

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::bb2eddc5b7afbe2bb328919d420f41d1
https://doi.org/10.1158/2159-8290.22541700

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Supplementary Figure 7 from A Small Molecule Reacts with the p53 Somatic Mutant Y220C to Rescue Wild-type Thermal Stability

Autor: Kevan M. Shokat, Keelan Z. Guiley

Supplementary Figure S7: Extended p53 Y220C KG13 cellular activity (A) Western blot for isogenic cell panel treated with 10 μM Nutlin-3a constant or 10 μM KG13 for 1 hr at 28°C, washed out, then moved to 37°C for 8hr. (B) ChIP p53 enrichment for

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7638721e187588fd71e05c697b506d78
https://doi.org/10.1158/2159-8290.22541682

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Supplementary Figure 5 from A Small Molecule Reacts with the p53 Somatic Mutant Y220C to Rescue Wild-type Thermal Stability

Autor: Kevan M. Shokat, Keelan Z. Guiley

Supplementary Figure S5: CDKN1A EMSA gels and intensity plots (A) EMSA for p53 WT-CL. (B) EMSA for p53 Y220C-CL. (C) EMSA for p53 Y220C-CL complexed with KG13. (D) EMSA for p53 R273C-CL. (E) Upper band intensities plotted for each protein construct.

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1c0825bf5e76e2b5a6a70436b3f93451
https://doi.org/10.1158/2159-8290.22541688

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Supplementary Figure 6 from A Small Molecule Reacts with the p53 Somatic Mutant Y220C to Rescue Wild-type Thermal Stability

Autor: Kevan M. Shokat, Keelan Z. Guiley

Supplementary Figure S6: Western blots and for 28°C IP and CETSA (A) H1299 cells stably expressing p53 Y220C or p53 R273C were transferred from 37°C to 28°C and p21/MDM2 levels were monitored by western blot at the indicated time points. (B) U2OS

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::28472bb75b353072cce342fd8970c9ef
https://doi.org/10.1158/2159-8290.22541685.v1

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