Hu, Y., Cheng, K., He, L., Zhang, X., Jiang, B., Jiang, L., Li, C., Wang, G., Yang, Y., & Liu, M. (2021). NMR-Based methods for protein analysis. Analytical Chemistry, 93, 1866–1879.

CAS  PubMed  Google Scholar 

Opella, S. J., & Marassi, F. M. (2017). Applications of NMR to membrane proteins. Archives of Biochemistry and Biophysics, 628, 92–101.

CAS  PubMed  PubMed Central  Google Scholar 

Inomata, K., Ohno, A., Tochio, H., et al. (2009). High-resolution multi-dimensional NMR spectroscopy of proteins in human cells. Nature, 458, 106–109.

CAS  PubMed  Google Scholar 

Alderson, T. R., & Kay, L. E. (2021). NMR spectroscopy captures the essential role of dynamics in regulating biomolecular function. Cell, 184, 577–595.

CAS  PubMed  Google Scholar 

Aboalroub, A. A., Zhang, Z., Keramisanou, D., & Gelis, I. (2017). Backbone resonance assignment of an insect arylalkylamine N-acetyltransferase from Bombyx Mori reveals conformational heterogeneity. Biomol NMR Assign, 11, 105–109.

CAS  PubMed  Google Scholar 

Gelis, I., Keramisanou, D., & Aboalroub, A. (2017). Protein kinase recognition and sorting by the HSP90 Kinome-Specific cochaperone CDC37. Biophys J, 112, 491a.

Google Scholar 

Emwas, A-H., Szczepski, K., Poulson, B. G., Chandra, K., McKay, R. T., Dhahri, M., Alahmari, F., Jaremko, L., Lachowicz, J. I., & Jaremko, M. (2020). NMR as a gold standard method in drug design and discovery. Molecules, 25, 4597.

CAS  PubMed  PubMed Central  Google Scholar 

Maiti, S., Singh, A., Maji, T., Saibo, N. V., & De, S. (2024). Experimental methods to study the structure and dynamics of intrinsically disordered regions in proteins. Curr Res Struct Biol, 7, 100138.

CAS  PubMed  PubMed Central  Google Scholar 

Csizmok, V., Follis, A. V., Kriwacki, R. W., & Forman-Kay, J. D. (2016). Dynamic protein interaction networks and new structural paradigms in signaling. Chemical Reviews, 116, 6424–6462.

CAS  PubMed  PubMed Central  Google Scholar 

Coles, M., Bicknell, W., Watson, A. A., Fairlie, D. P., & Craik, D. J. (1998). THE SOLUTION STRUCTURE OF AMYLOID BETA-PEPTIDE (1–40) IN A WATER-MICELLE ENVIRONMENT. IS THE MEMBRANE-SPANNING DOMAIN WHERE WE THINK IT IS? NMR, 10 STRUCTURES. Worldwide Protein Data Bank. https://doi.org/10.2210/pdb1ba4/pdb

Xie, H., Zhao, Y., Zhao, W., Chen, Y., Liu, M., & Yang, J. (2023). Solid-state NMR structure determination of a membrane protein in E. coli cellular inner membrane. Science Advances. https://doi.org/10.1126/sciadv.adh4168

PubMed  PubMed Central  Google Scholar 

Palmer, A. G. (2015). Enzyme dynamics from NMR spectroscopy. Accounts of Chemical Research, 48, 457–465.

CAS  PubMed  PubMed Central  Google Scholar 

Gadhave, D. G., Sugandhi, V. V., Jha, S. K., Nangare, S. N., Gupta, G., Singh, S. K., Dua, K., Cho, H., Hansbro, P. M., & Paudel, K. R. (2024). Neurodegenerative disorders: Mechanisms of degeneration and therapeutic approaches with their clinical relevance. Ageing Research Reviews, 99, 102357.

CAS  PubMed  Google Scholar 

André, L. M., Ausems, C. R. M., Wansink, D. G., & Wieringa, B. (2018). Abnormalities in skeletal muscle myogenesis, growth, and regeneration in myotonic dystrophy. Frontiers in Neurology. https://doi.org/10.3389/fneur.2018.00368

PubMed  PubMed Central  Google Scholar 

Hussain, R., Zubair, H., Pursell, S., & Shahab, M. (2018). Neurodegenerative diseases: Regenerative mechanisms and novel therapeutic approaches. Brain Sci, 8, 177.

CAS  PubMed  PubMed Central  Google Scholar 

Gaugler, J., James, B., Johnson, T., Reimer, J., Scales, K., Tom, S., Weuve, J., & Yeh, J., (2024). 2024 alzheimer’s disease facts and figures. Alzheimer’s & Dementia, 20, 3708–3821.

Google Scholar 

Murphy, M. P., & LeVine, H. (2010). Alzheimer’s disease and the Amyloid-β peptide. Journal of Alzheimer’s Disease, 19, 311–323.

PubMed  Google Scholar 

Aleksis, R., Oleskovs, F., Jaudzems, K., Pahnke, J., & Biverstål, H. (2017). Structural studies of amyloid-β peptides: Unlocking the mechanism of aggregation and the associated toxicity. Biochimie, 140, 176–192.

CAS  PubMed  Google Scholar 

Kohno, T., Kobayashi, K., Maeda, T., Sato, K., & Takashima, A. (1996). Three-Dimensional structures of the amyloid β peptide (25 – 35) in Membrane-Mimicking environment. Biochemistry, 35, 16094–16104.

CAS  PubMed  Google Scholar 

Poulsen, S-A., Watson, A. A., Fairlie, D. P., & Craik, D. J. (2000). Solution structures in aqueous SDS micelles of two amyloid β peptides of Aβ(1–28) mutated at the α-Secretase cleavage site (K16E, K16F). Journal of Structural Biology, 130, 142–152.

CAS  PubMed  Google Scholar 

Crescenzi, O., Tomaselli, S., Guerrini, R., Salvadori, S., D’Ursi, A. M., Temussi, P. A., & Picone, D. (2002). Solution structure of the alzheimer amyloid β-peptide (1–42) in an apolar microenvironment. European Journal of Biochemistry, 269, 5642–5648.

CAS  PubMed  Google Scholar 

Coles, M., Bicknell, W., Watson, A. A., Fairlie, D. P., & Craik, D. J. (1998). Solution structure of amyloid β-Peptide(1 – 40) in a Water – Micelle environment. is? the Membrane-Spanning domain where we think it is??. Biochemistry, 37, 11064–11077.

CAS  PubMed  Google Scholar 

Vivekanandan, S., Brender, J. R., Lee, S. Y., & Ramamoorthy, A. (2011). A partially folded structure of amyloid-beta(1–40) in an aqueous environment. Biochemical and Biophysical Research Communications, 411, 312–316.

CAS  PubMed  PubMed Central  Google Scholar 

Loquet, A., El Mammeri, N., Stanek, J., Berbon, M., Bardiaux, B., Pintacuda, G., & Habenstein, B. (2018). 3D structure determination of amyloid fibrils using solid-state NMR spectroscopy. Methods, 138–139, 26–38.

PubMed  Google Scholar 

Paravastu, A. K., Leapman, R. D., Yau, W-M., & Tycko, R. (2008). Molecular structural basis for polymorphism in Alzheimer’s β-amyloid fibrils. Proceedings of the National Academy of Sciences 105:18349–18354.

Fändrich, M., Nyström, S., Nilsson, K. P. R., Böckmann, A., LeVine, H., & Hammarström, P. (2018). Amyloid fibril polymorphism: A challenge for molecular imaging and therapy. Journal of Internal Medicine, 283, 218–237.

PubMed  PubMed Central  Google Scholar 

Yang, X., Wang, B., Hoop, C. L., Williams, J. K., & Baum, J. (2021). NMR unveils an N-terminal interaction interface on acetylated-α-synuclein monomers for recruitment to fibrils. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.2017452118

Google Scholar 

Fawzi, N. L., Ying, J., Ghirlando, R., Torchia, D. A., & Clore, G. M. (2011). Atomic-resolution dynamics on the surface of amyloid-β protofibrils probed by solution NMR. Nature, 480, 268–272.

CAS  PubMed  PubMed Central  Google Scholar 

Yang, Y., Arseni, D., Zhang, W. (2022). Cryo-EM structures of amyloid-β 42 filaments from human brains. Science (1979) 375:167–172.

Kollmer, M., Close, W., Funk, L., Rasmussen, J., Bsoul, A., Schierhorn, A., Schmidt, M., Sigurdson, C. J., Jucker, M., & Fändrich, M. (2019). Cryo-EM structure and polymorphism of Aβ amyloid fibrils purified from alzheimer’s brain tissue. Nature Communications, 10, 4760.

PubMed  PubMed Central  Google Scholar 

Tian, Y., Liang, R., Kumar, A., Szwedziak, P., & Viles, J. H. (2021). 3D-visualization of amyloid-β oligomer interactions with lipid membranes by cryo-electron tomography. Chemical Science, 12, 6896–6907.

CAS  PubMed  PubMed Central  Google Scholar 

Shi, Y., Murzin, A. G., Falcon, B., et al. (2021). Cryo-EM structures of Tau filaments from alzheimer’s disease with PET ligand APN-1607. Acta Neuropathologica, 141, 697–708.

CAS  PubMed  PubMed Central  Google Scholar 

Di Lorenzo, D. (2024). Tau Protein and Tauopathies: Exploring Tau Protein–Protein and Microtubule Interactions, Cross-Interactions and Therapeutic Strategies. ChemMedChem. https://doi.org/10.1002/cmdc.202400180

Barbier, P., Zejneli, O., Martinho, M., Lasorsa, A., Belle, V., Smet-Nocca, C., Tsvetkov, P., Devred, F., & Landrieu, I. (2019). Role of Tau as a Microtubule-Associated protein: Structural and functional aspects. Frontiers in Aging Neuroscience. https://doi.org/10.3389/fnagi.2019.00204

PubMed  PubMed Central  Google Scholar 

Kitoka, K., Skrabana, R., Gasparik, N., Hritz, J., & Jaudzems, K. (2021). NMR studies of Tau protein in tauopathies. Front Mol Biosci. https://doi.org/10.3389/fmolb.2021.761227

PubMed  PubMed Central  Google Scholar 

Boutajangout, A., Sigurdsson, M., & Krishnamurthy, E. K. P (2011). Tau as a therapeutic target for alzheimers disease. Current Alzheimer Research, 8, 666–677.

CAS  PubMed  PubMed Central  Google Scholar 

Harbison, N. W., Bhattacharya, S., & Eliezer, D. (2012). Assigning backbone NMR resonances for full length Tau isoforms: Efficient compromise between manual assignments and reduced dimensionality. PLoS One, 7, e34679.

CAS  PubMed  PubMed Central  Google Scholar 

Kadavath, H., Hofele, R. V., Biernat, J., Kumar, S., Tepper, K., Urlaub, H., Mandelkow, E., & Zweckstetter, M. (2015). Tau stabilizes microtubules by binding at the interface between tubulin heterodimers. Proceedings of the National Academy of Sciences, 112, 7501–7506.

CAS  Google Scholar 

Kadavath, H., Jaremko, M., Jaremko, Ł., Biernat, J., Mandelkow, E., &