Microtubule dynamics as a target in oncology

AL Risinger, FJ Giles, SL Mooberry - Cancer treatment reviews, 2009 - Elsevier
Drugs that affect microtubule dynamics, including the taxanes and vinca alkaloids, have
been a mainstay in the treatment of leukemias and solid tumors for decades. New, more …

Tubulin post-translational modifications: the elusive roles of acetylation

B Carmona, HS Marinho, CL Matos, S Nolasco… - Biology, 2023 - mdpi.com
Simple Summary Microtubules (MTs) are dynamic structures that compose part of the cell
cytoskeleton. They play important roles in various cellular functions, such as intracellular …

[HTML][HTML] Quantitative proteomics reveals the function of unconventional ubiquitin chains in proteasomal degradation

P Xu, DM Duong, NT Seyfried, D Cheng, Y Xie… - Cell, 2009 - cell.com
All seven lysine residues in ubiquitin contribute to the synthesis of polyubiquitin chains on
protein substrates. Whereas K48-linked chains are well established as mediators of …

Transcriptomic and genomic evolution under constant cold in Antarctic notothenioid fish

Z Chen, CHC Cheng, J Zhang, L Cao… - Proceedings of the …, 2008 - National Acad Sciences
The antifreeze glycoprotein-fortified Antarctic notothenioid fishes comprise the predominant
fish suborder in the isolated frigid Southern Ocean. Their ecological success undoubtedly …

[PDF][PDF] Identification and characterization of factors required for microtubule growth and nucleation in the early C. elegans embryo

M Srayko, A Kaya, J Stamford, AA Hyman - Developmental cell, 2005 - cell.com
Microtubules (MTs) are dynamic polymers that undergo cell cycle and position-sensitive
regulation of polymerization and depolymerization. Although many different factors that …

[HTML][HTML] Structure and function of a protein folding machine: the eukaryotic cytosolic chaperonin CCT

JM Valpuesta, J Martı́n-Benito, P Gómez-Puertas… - FEBS letters, 2002 - Elsevier
Chaperonins are large oligomers made up of two superimposed rings, each enclosing a
cavity used for the folding of other proteins. Among the chaperonins, the eukaryotic cytosolic …

Is protein folding a thermodynamically unfavorable, active, energy-dependent process?

I Sorokina, AR Mushegian, EV Koonin - International journal of molecular …, 2022 - mdpi.com
The prevailing current view of protein folding is the thermodynamic hypothesis, under which
the native folded conformation of a protein corresponds to the global minimum of Gibbs free …

Significant conservation of synthetic lethal genetic interaction networks between distantly related eukaryotes

SJ Dixon, Y Fedyshyn, JLY Koh… - Proceedings of the …, 2008 - National Acad Sciences
Synthetic lethal genetic interaction networks define genes that work together to control
essential functions and have been studied extensively in Saccharomyces cerevisiae using …

Chaperonins: two rings for folding

H Yébenes, P Mesa, IG Muñoz, G Montoya… - Trends in biochemical …, 2011 - cell.com
Chaperonins are ubiquitous chaperones found in Eubacteria, eukaryotic organelles (group
I), Archaea and the eukaryotic cytosol (group II). They all share a common structure and a …

A hypothesis on the origin and evolution of tubulin

RF Ludueña - International review of cell and molecular biology, 2013 - Elsevier
Tubulin, the protein subunit of microtubules (MTs), is an α/β heterodimer. In this chapter, a
hypothesis on the evolution of the tubulin molecule is proposed, based in part on recent …