ArticleJournal of biomolecular NMR2013
Efficient protocol for backbone and side-chain assignments of large, intrinsically disordered proteins: transient secondary structure analysis of 49.2 kDa microtubule associated protein 2c.
Article in Journal of biomolecular NMR, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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23 citing papers in PubMed, 42 citations in OpenAlex.
- Characterization of multiple binding sites on microtubule associated protein 2c recognized by dimeric and monomeric 14-3-3ζ.The FEBS journal · 2025Article
- MAP2 phosphorylation: mechanisms, functional consequences, and emerging insights.Frontiers in cellular neuroscience · 2025Review
- Structural basis of binding the unique N-terminal domain of microtubule-associated protein 2c to proteins regulating kinases of signaling pathways.The Journal of biological chemistry · 2024Article
- Review
- MAP2 is differentially phosphorylated in schizophrenia, altering its function.Molecular psychiatry · 2021Article
- Choice of Force Field for Proteins Containing Structured and Intrinsically Disordered Regions.Biophysical journal · 2020Article
- Structure and Functions of Microtubule Associated Proteins Tau and MAP2c: Similarities and Differences.Biomolecules · 2019Review
- A CON-based NMR assignment strategy for pro-rich intrinsically disordered proteins with low signal dispersion: the C-terminal domain of histone H1.0 as a case study.Journal of biomolecular NMR · 2018Article
- Transient Secondary Structures as General Target-Binding Motifs in Intrinsically Disordered Proteins.International journal of molecular sciences · 2018Review
- Functionally specific binding regions of microtubule-associated protein 2c exhibit distinct conformations and dynamics.The Journal of biological chemistry · 2018Article
- Troubleshooting Guide to Expressing Intrinsically Disordered Proteins for Use in NMR Experiments.Frontiers in molecular biosciences · 2018Review
- Triple resonance ¹⁵Ν NMR relaxation experiments for studies of intrinsically disordered proteins.Journal of biomolecular NMR · 2017Article
- Quantitative mapping of microtubule-associated protein 2c (MAP2c) phosphorylation and regulatory protein 14-3-3ζ-binding sites reveals key differences between MAP2c and its homolog Tau.The Journal of biological chemistry · 2017Article
- The Eighth Central European Conference "Chemistry towards Biology": Snapshot.Molecules (Basel, Switzerland) · 2016Article
- Five and four dimensional experiments for robust backbone resonance assignment of large intrinsically disordered proteins: application to Tau3x protein.Journal of biomolecular NMR · 2016Article
- Amino acid recognition for automatic resonance assignment of intrinsically disordered proteins.Journal of biomolecular NMR · 2016Article
- HN-NCA heteronuclear TOCSY-NH experiment for (1)H(N) and (15)N sequential correlations in ((13)C, (15)N) labelled intrinsically disordered proteins.Journal of biomolecular NMR · 2015Article
- (13)C-detected NMR experiments for automatic resonance assignment of IDPs and multiple-fixing SMFT processing.Journal of biomolecular NMR · 2015Article
- A six-dimensional alpha proton detection-based APSY experiment for backbone assignment of intrinsically disordered proteins.Journal of biomolecular NMR · 2014Article
- "CON-CON" assignment strategy for highly flexible intrinsically disordered proteins.Journal of biomolecular NMR · 2014Article
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Microtubule-associated proteins (MAPs) are abundantly present in axons and dendrites, and have been shown to play crucial role during the neuronal morphogenesis. The period of main dendritic outgrowth and synaptogenesis coincides with high expression levels of one of MAPs, the MAP2c, in rats. The MAP2c is a 49.2 kDa intrinsically disordered protein. To achieve an atomic resolution characterization of such a large protein, we have developed a protocol based on the acquisition of two five-dimensional (13)C-directly detected NMR experiments. Our previously published 5D CACONCACO experiment (Nováček et al. in J Biomol NMR 50(1):1-11, 2011) provides the sequential assignment of the backbone resonances, which is not interrupted by the presence of the proline residues in the amino acid sequence. A novel 5D HC(CC-TOCSY)CACON experiment facilitates the assignment of the aliphatic side chain resonances. To streamline the data analysis, we have developed a semi-automated procedure for signal assignments. The obtained data provides the first atomic resolution insight into the conformational state of MAP2c and constitutes a model for further functional studies of MAPs.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.