Structural and dynamics analysis of intrinsically disordered proteins by high-speed atomic force microscopy-Reference-Cited by-同舟云学术

Structural and dynamics analysis of intrinsically disordered proteins by high-speed atomic force microscopy

Published:2020-11-23 Issue:2 Volume:16 Page:181-189
ISSN:1748-3387
Container-title:Nature Nanotechnology
language:en
Short-container-title:Nat. Nanotechnol.

Author:

Kodera Noriyuki,Noshiro Daisuke^ORCID,Dora Sujit K.,Mori Tetsuya,Habchi Johnny,Blocquel David,Gruet Antoine,Dosnon Marion,Salladini Edoardo^ORCID,Bignon Christophe,Fujioka Yuko,Oda Takashi,Noda Nobuo N.^ORCID,Sato Mamoru,Lotti Marina^ORCID,Mizuguchi Mineyuki,Longhi Sonia^ORCID,Ando Toshio^ORCID

Funder

MEXT | JST | Precursory Research for Embryonic Science and Technology

joint doctoral fellowship from the Direction Générale de l’Armement (DGA) and the CNRS

PhD fellowship from the French Ministry of National Education, Research and Technology

joint doctoral fellowship from the Direction Générale de l’Armement (DGA) and Aix-Marseille Université

MEXT | Japan Society for the Promotion of Science

MEXT | JST | Core Research for Evolutional Science and Technology

Agence Nationale de la Recherche

Publisher

Springer Science and Business Media LLC

Subject

Electrical and Electronic Engineering,Condensed Matter Physics,General Materials Science,Biomedical Engineering,Atomic and Molecular Physics, and Optics,Bioengineering

Link

http://www.nature.com/articles/s41565-020-00798-9.pdf

Reference59 articles.

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2. Uversky, V. N., Gillespie, J. R. & Fink, A. L. Why are ‘natively unfolded’ proteins unstructured under physiologic conditions? Proteins 41, 415–427 (2000).

3. Wright, P. E. & Dyson, H. J. Intrinsically disordered proteins in cellular signaling and regulation. Nat. Rev. Mol. Cell Biol. 16, 18–29 (2015).

4. Dyson, H. J. & Wright, P. E. Unfolded proteins and protein folding studied by NMR. Chem. Rev. 104, 3607–3622 (2004).

5. Jensen, M. R., Zweckstetter, M., Huang, J. & Blackledge, M. Exploring free-energy landscapes of intrinsically disordered proteins at atomic resolution using NMR spectroscopy. Chem. Rev. 114, 6632–6660 (2014).

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