Results 11 to 20 of about 436,730 (400)
The tubulin code at a glance [PDF]
Journal of Cell Science, 2017 ABSTRACT Microtubules are key cytoskeletal elements of all eukaryotic cells and are assembled of evolutionarily conserved α-tubulin–β-tubulin heterodimers. Despite their uniform structure, microtubules fulfill a large diversity of functions.
Carsten Janke +7 more
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Molecules, 2016 Tubulin inhibitors are effective anticancer agents, however, there are many limitations to the use of available tubulin inhibitors in the clinic, such as multidrug resistance, severe side-effects, and generally poor bioavailability.
Mengqi Dong +4 more
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Recent Advances of Tubulin Inhibitors Targeting the Colchicine Binding Site for Cancer Therapy
Biomolecules, 2022 Cancer accounts for numerous deaths each year, and it is one of the most common causes of death worldwide, despite many breakthroughs in the discovery of novel anticancer candidates.
Mohammed Hawash
semanticscholar +1 more source
The Tubulin Code and Tubulin-Modifying Enzymes in Autophagy and Cancer [PDF]
Cancers, 2021 Microtubules are key components of the cytoskeleton of eukaryotic cells. Microtubule dynamic instability together with the “tubulin code” generated by the choice of different α- and β- tubulin isoforms and tubulin post-translational modifications have essential roles in the control of a variety of cellular processes, such as cell shape, cell motility ...
Trisciuoglio Daniela, Degrassi Francesca
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Frontiers in Cell and Developmental Biology, 2022 Microtubules (MTs) support a variety of neuronal functions, such as maintenance of cell structure, transport, and synaptic plasticity. Neuronal MTs are highly heterogeneous due to several tubulin isotypes and the presence of multiple post-translational ...
José Martínez-Hernández +13 more
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Autopalmitoylation of tubulin [PDF]
Protein Science, 2000 AbstractPure rat brain tubulin is readily palmitoylated in vitro using [3H]palmitoyl CoA but no added enzymes. A maximum of approximately six palmitic acids are added per dimer in 2–3 h at 36–37 °C under native conditions. Both α and β tubulin are labeled, and 63–73% of the label was hydroxylamine‐labile, presumed thioesters.
P. J. Britto +3 more
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Chemomechanical simulation of microtubule dynamics with explicit lateral bond dynamics [PDF]
Front. Phys. 9:673875 (2021), 2021 We introduce and parameterize a chemomechanical model of microtubule dynamics on the dimer level, which is based on the allosteric tubulin model and includes attachment, detachment and hydrolysis of tubulin dimers as well as stretching of lateral bonds, bending at longitudinal junctions, and the possibility of lateral bond rupture and formation.
arxiv +1 more source
Cells, 2021 Higher plants represent a large group of eukaryotes where centrosomes are absent. The functions of γ-tubulin small complexes (γ-TuSCs) and γ-tubulin ring complexes (γ-TuRCs) in metazoans and fungi in microtubule nucleation are well established and the ...
Jana Chumová +4 more
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Biomolecules, 2023 Tubulin is a protein that plays a critical role in maintaining cellular structure and facilitating cell division. Inhibiting tubulin polymerization has been shown to be an effective strategy for inhibiting the proliferation of cancer cells.
Harutyun Khachatryan +4 more
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Biomolecules, 2023 An important post-translational modification (PTM) of α-tubulin is the removal of amino acids from its C-terminus. Removal of the C-terminal tyrosine residue yields detyrosinated α-tubulin, and subsequent removal of the penultimate glutamate residue ...
Takashi Hotta +8 more
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