Presentation is loading. Please wait.

Presentation is loading. Please wait.

Modification of the βIII-tubulin C-terminal tail does not affect tubulin polymerization or the cellular proliferation rate. Modification of the βIII-tubulin.

Published byBuddy Preston Fitzgerald Modified over 5 years ago

Similar presentations

Presentation on theme: "Modification of the βIII-tubulin C-terminal tail does not affect tubulin polymerization or the cellular proliferation rate. Modification of the βIII-tubulin."— Presentation transcript:

1 Modification of the βIII-tubulin C-terminal tail does not affect tubulin polymerization or the cellular proliferation rate. Modification of the βIII-tubulin C-terminal tail does not affect tubulin polymerization or the cellular proliferation rate. Representative Western blot (A) and densitometric quantitation (B and C) of the level of polymerized total tubulin (α-tubulin) (B) and polymerized modified βIII-tubulin proteins (GFP) (C) in gene-edited NCI-H460 cells expressing either the full-length βIII-tubulin protein (ZB3) or truncated βIII-tubulin protein (ZB3Δ) compared with the parental cell line (H460), which endogenously expresses βIII-tubulin. Mean ± SEM of four independent experiments, no significant difference. S, soluble fraction; P, polymerized fraction. (D) Cell number for NCI-H460 cells expressing the full-length βIII-tubulin proteins (ZB31 and ZB34), truncated βIII-tubulin protein (ZB3Δ1 and ZB3Δ2), or the βIII-tubulin body with βI-tubulin C-terminal tail (ZB3/CB12 and ZB3/CB13) measured periodically over 96 h by trypan blue dye exclusion and cell counting. Amelia L Parker et al. LSA 2018;1:e © 2018 Parker et al.

Download ppt "Modification of the βIII-tubulin C-terminal tail does not affect tubulin polymerization or the cellular proliferation rate. Modification of the βIII-tubulin."

Similar presentations

The effects of folic acid on global DNA methylation and colonosphere formation in colon cancer cell lines  Nathan Farias, Nelson Ho, Stacey Butler, Leanne.

The effects of folic acid on global DNA methylation and colonosphere formation in colon cancer cell lines  Nathan Farias, Nelson Ho, Stacey Butler, Leanne.
Suppl. Figure 5. Non-sphere vs. sphere cell proliferation in vitro

Suppl. Figure 5. Non-sphere vs. sphere cell proliferation in vitro
Interaction of Stau1 with ribosomal protein P0 (A) Schematic representation of Stau1, showing its dRBDs I–IV (boxes) and PP1 interaction domain (circle),

Interaction of Stau1 with ribosomal protein P0 (A) Schematic representation of Stau1, showing its dRBDs I–IV (boxes) and PP1 interaction domain (circle),
Expression of adenylyl cyclases and miR‐142‐3p in CD4+CD25− T cells and CD4+CD25+ regulatory T cells. Expression of adenylyl cyclases and miR‐142‐3p in.

Expression of adenylyl cyclases and miR‐142‐3p in CD4+CD25− T cells and CD4+CD25+ regulatory T cells. Expression of adenylyl cyclases and miR‐142‐3p in.
DHEA(S) and Allo induced the expression of the antiapoptotic Bcl-2 proteins in serum-deprived PC12 cells. DHEA(S) and Allo induced the expression of the.

DHEA(S) and Allo induced the expression of the antiapoptotic Bcl-2 proteins in serum-deprived PC12 cells. DHEA(S) and Allo induced the expression of the.
Patient neural progenitors show a neurodevelopmental phenotype.

Patient neural progenitors show a neurodevelopmental phenotype.
Everolimus Inhibits SMC Proliferation Through Transcriptional Repression of Telomerase (A) Cell proliferation assay in primary murine vascular smooth muscle.

Everolimus Inhibits SMC Proliferation Through Transcriptional Repression of Telomerase (A) Cell proliferation assay in primary murine vascular smooth muscle.
The β-tubulin C-terminal tail modulates the coordination of microtubule assembly in an isotype-dependent manner. The β-tubulin C-terminal tail modulates.

The β-tubulin C-terminal tail modulates the coordination of microtubule assembly in an isotype-dependent manner. The β-tubulin C-terminal tail modulates.
The β-tubulin C-terminal tail modulates the sensitivity of microtubules to paclitaxel. The β-tubulin C-terminal tail modulates the sensitivity of microtubules.

The β-tubulin C-terminal tail modulates the sensitivity of microtubules to paclitaxel. The β-tubulin C-terminal tail modulates the sensitivity of microtubules.
The DHX15–CMTR1 interaction inhibits translation of a subset of genes.

The DHX15–CMTR1 interaction inhibits translation of a subset of genes.
Figure 3 Mutation carrier–derived lymphoblastoid cell lines (LCLs) show decreased aconitase 2 activity and mitochondrial respiration deficiency compared.

Figure 3 Mutation carrier–derived lymphoblastoid cell lines (LCLs) show decreased aconitase 2 activity and mitochondrial respiration deficiency compared.
BRCA1 PARsylation is required for normal HRR tuning.

BRCA1 PARsylation is required for normal HRR tuning.
The absence of the centrosome changes global microtubule dynamics in a migrating cell. The absence of the centrosome changes global microtubule dynamics.

The absence of the centrosome changes global microtubule dynamics in a migrating cell. The absence of the centrosome changes global microtubule dynamics.
Volume 14, Issue 1, Pages (January 2008)

Volume 14, Issue 1, Pages (January 2008)
STING stimulation in T cells inhibits cell cycle progression.

STING stimulation in T cells inhibits cell cycle progression.
Molecular mechanism of STING-mediated inhibition of the mTORC1 pathway

Molecular mechanism of STING-mediated inhibition of the mTORC1 pathway
KIF18A sNL variants do not accumulate on K-fibers in the center of the spindle. KIF18A sNL variants do not accumulate on K-fibers in the center of the.

KIF18A sNL variants do not accumulate on K-fibers in the center of the spindle. KIF18A sNL variants do not accumulate on K-fibers in the center of the.
Significant differences in translational efficiencies of DNA damage repair pathway genes between patient clusters. Significant differences in translational.

Significant differences in translational efficiencies of DNA damage repair pathway genes between patient clusters. Significant differences in translational.
SUMO-1 Modification Represses Sp3 Transcriptional Activation and Modulates Its Subnuclear Localization  Sarah Ross, Jennifer L Best, Leonard I Zon, Grace.

SUMO-1 Modification Represses Sp3 Transcriptional Activation and Modulates Its Subnuclear Localization  Sarah Ross, Jennifer L Best, Leonard I Zon, Grace.
A and B, CO-1686–resistant NCI-H1975 cell clones, COR1-1 and COR10-1 display a reduced dependence on EGFR signaling for survival. A and B, CO-1686–resistant.

A and B, CO-1686–resistant NCI-H1975 cell clones, COR1-1 and COR10-1 display a reduced dependence on EGFR signaling for survival. A and B, CO-1686–resistant.

Similar presentations

Ads by Google