Search Results - "McAlear, Thomas"
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The mitotic spindle protein CKAP2 potently increases formation and stability of microtubules
Published in eLife (14-01-2022)“…Cells increase microtubule dynamics to make large rearrangements to their microtubule cytoskeleton during cell division. Changes in microtubule dynamics are…”
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The spindle protein CKAP2 regulates microtubule dynamics and ensures faithful chromosome segregation
Published in Proceedings of the National Academy of Sciences - PNAS (27-02-2024)“…Regulation of microtubule dynamics by microtubule-associated proteins (MAPs) is essential for mitotic spindle assembly and chromosome segregation. Altered…”
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The Golgi Outpost Protein TPPP Nucleates Microtubules and Is Critical for Myelination
Published in Cell (19-09-2019)“…Oligodendrocytes extend elaborate microtubule arbors that contact up to 50 axon segments per cell, then spiral around myelin sheaths, penetrating from outer to…”
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The inner junction complex of the cilia is an interaction hub that involves tubulin post-translational modifications
Published in eLife (17-01-2020)“…Microtubules are cytoskeletal structures involved in stability, transport and organization in the cell. The building blocks, the α- and β-tubulin heterodimers,…”
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EML2-S constitutes a new class of proteins that recognizes and regulates the dynamics of tyrosinated microtubules
Published in Current biology (26-09-2022)“…Tubulin post-translational modifications (PTMs) alter microtubule properties by affecting the binding of microtubule-associated proteins (MAPs). Microtubule…”
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Crystal structure of human PACRG in complex with MEIG1 reveals roles in axoneme formation and tubulin binding
Published in Structure (London) (03-06-2021)“…The Parkin co-regulated gene protein (PACRG) binds at the inner junction between doublet microtubules of the axoneme, a structure found in flagella and cilia…”
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The Inner Junction Complex of the Cilia is an Interaction Hub that Involves Tubulin Post-translational Modifications
Published in Biophysical journal (07-02-2020)Get full text
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