Associated Papers
Accurate affinity models for SH2 domains from peptide binding assays and free-energy regression.
Gagoski D et al.
Protein Science : a Publication of the Protein Society, 2025
Accurate sequence-to-affinity models for SH2 domains from multi-round peptide binding assays coupled with free-energy regression.
Gagoski D et al.
Biorxiv : the Preprint Server for Biology, 2025
Insights on the Role of α- and β-Tubulin Isotypes in Early Brain Development.
Tantry MSA et al.
Molecular Neurobiology, 2023
Understanding molecular mechanisms and predicting phenotypic effects of pathogenic tubulin mutations.
Attard TJ et al.
Plos Computational Biology, 2022
Complementing the phenotypical spectrum of TUBA1A tubulinopathy and its role in early-onset epilepsies.
Schröter J et al.
European Journal of Human Genetics : Ejhg, 2022
The molecular biology of tubulinopathies: Understanding the impact of variants on tubulin structure and microtubule regulation.
Hoff KJ et al.
Frontiers in Cellular Neuroscience, 2022
Loss-of-Function Plays a Major Role in Early Neurogenesis of Tubulin α-1 A (TUBA1A) Mutation-Related Brain Malformations.
Xie L et al.
Molecular Neurobiology, 2021
Tubulin mutations in neurodevelopmental disorders as a tool to decipher microtubule function.
Fourel G et al.
Febs Letters, 2020
Mutations disrupting neuritogenesis genes confer risk for cerebral palsy.
Jin SC et al.
Nature Genetics, 2020
The mutational and phenotypic spectrum of TUBA1A-associated tubulinopathy.
Hebebrand M et al.
Orphanet Journal of Rare Diseases, 2019
The α-Tubulin gene TUBA1A in Brain Development: A Key Ingredient in the Neuronal Isotype Blend.
Aiken J et al.
Journal of Developmental Biology, 2017
The emerging role of the tubulin code: From the tubulin molecule to neuronal function and disease.
Chakraborti S et al.
Cytoskeleton (hoboken, N.j.), 2016
TUBA1A mutation can cause a hydranencephaly-like severe form of cortical dysgenesis.
Yokoi S et al.
Scientific Reports, 2015
Mutations in α- and β-tubulin encoding genes: implications in brain malformations.
Romaniello R et al.
Brain & Development, 2015
Reproducible Analysis of Post-Translational Modifications in Proteomes--Application to Human Mutations.
Holehouse AS et al.
Plos One, 2015
Mutations in tubulin genes are frequent causes of various foetal malformations of cortical development including microlissencephaly.
Fallet-Bianco C et al.
Acta Neuropathologica Communications, 2014
Microtubules and neurodevelopmental disease: the movers and the makers.
Breuss M et al.
Advances in Experimental Medicine and Biology, 2014
Paclitaxel resistance by random mutagenesis of α-tubulin.
Yin S et al.
Cytoskeleton (hoboken, N.j.), 2013
TUBA1A mutation-associated lissencephaly: case report and review of the literature.
Sohal AP et al.
Pediatric Neurology, 2012
Role of cytoskeletal abnormalities in the neuropathology and pathophysiology of type I lissencephaly.
Friocourt G et al.
Acta Neuropathologica, 2011
Disease-associated mutations in TUBA1A result in a spectrum of defects in the tubulin folding and heterodimer assembly pathway.
Tian G et al.
Human Molecular Genetics, 2010
TUBA1A mutations cause wide spectrum lissencephaly (smooth brain) and suggest that multiple neuronal migration pathways converge on alpha tubulins.
Kumar RA et al.
Human Molecular Genetics, 2010
Human lissencephaly with cerebellar hypoplasia due to mutations in TUBA1A: expansion of the foetal neuropathological phenotype.
Lecourtois M et al.
Acta Neuropathologica, 2010
Neuropathological phenotype of a distinct form of lissencephaly associated with mutations in TUBA1A.
Fallet-Bianco C et al.
Brain : a Journal of Neurology, 2008
Large spectrum of lissencephaly and pachygyria phenotypes resulting from de novo missense mutations in tubulin alpha 1A (TUBA1A).
Poirier K et al.
Human Mutation, 2007