HSP40 proteins use class-specific regulation to drive HSP70 functional diversity
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DOI: 10.1038/s41586-020-2906-4
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Cited by:
- Lorea Velasco-Carneros & Jorge Cuéllar & Leire Dublang & César Santiago & Jean-Didier Maréchal & Jaime Martín-Benito & Moisés Maestro & José Ángel Fernández-Higuero & Natalia Orozco & Fernando Moro & , 2023. "The self-association equilibrium of DNAJA2 regulates its interaction with unfolded substrate proteins and with Hsc70," Nature Communications, Nature, vol. 14(1), pages 1-16, December.
- Jaime Carrasco & Rosa Antón & Alejandro Valbuena & David Pantoja-Uceda & Mayur Mukhi & Rubén Hervás & Douglas V. Laurents & María Gasset & Javier Oroz, 2023. "Metamorphism in TDP-43 prion-like domain determines chaperone recognition," Nature Communications, Nature, vol. 14(1), pages 1-15, December.
- Yan Chen & Bin Tsai & Ningning Li & Ning Gao, 2022. "Structural remodeling of ribosome associated Hsp40-Hsp70 chaperones during co-translational folding," Nature Communications, Nature, vol. 13(1), pages 1-14, December.
- Rebecca San Gil & Dana Pascovici & Juliana Venturato & Heledd Brown-Wright & Prachi Mehta & Lidia Madrid San Martin & Jemma Wu & Wei Luan & Yi Kit Chui & Adekunle T. Bademosi & Shilpa Swaminathan & Se, 2024. "A transient protein folding response targets aggregation in the early phase of TDP-43-mediated neurodegeneration," Nature Communications, Nature, vol. 15(1), pages 1-23, December.
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