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The ensemble nature of allostery

Author

Listed:
  • Hesam N. Motlagh

    (Johns Hopkins University)

  • James O. Wrabl

    (Johns Hopkins University)

  • Jing Li

    (Johns Hopkins University)

  • Vincent J. Hilser

    (Johns Hopkins University)

Abstract

Allostery is the process by which biological macromolecules transmit the effect of binding at one site to another, often distal, functional site, allowing for the regulation of activity; here facilitation of allostery through dynamic and intrinsically disordered proteins is discussed, and a framework to unify the description of allosteric mechanisms for different systems is proposed.

Suggested Citation

  • Hesam N. Motlagh & James O. Wrabl & Jing Li & Vincent J. Hilser, 2014. "The ensemble nature of allostery," Nature, Nature, vol. 508(7496), pages 331-339, April.
    • Handle: RePEc:nat:nature:v:508:y:2014:i:7496:d:10.1038_nature13001
    DOI: 10.1038/nature13001
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    Citations

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    Cited by:

    1. Marko Novinec, 2017. "Computational investigation of conformational variability and allostery in cathepsin K and other related peptidases," PLOS ONE, Public Library of Science, vol. 12(8), pages 1-22, August.
    2. Federica Maschietto & Uriel N. Morzan & Florentina Tofoleanu & Aria Gheeraert & Apala Chaudhuri & Gregory W. Kyro & Peter Nekrasov & Bernard Brooks & J. Patrick Loria & Ivan Rivalta & Victor S. Batist, 2023. "Turning up the heat mimics allosteric signaling in imidazole-glycerol phosphate synthase," Nature Communications, Nature, vol. 14(1), pages 1-13, December.
    3. Yuya Nishida & Sachiko Yanagisawa & Rikuri Morita & Hideki Shigematsu & Kyoko Shinzawa-Itoh & Hitomi Yuki & Satoshi Ogasawara & Ken Shimuta & Takashi Iwamoto & Chisa Nakabayashi & Waka Matsumura & His, 2022. "Identifying antibiotics based on structural differences in the conserved allostery from mitochondrial heme-copper oxidases," Nature Communications, Nature, vol. 13(1), pages 1-14, December.
    4. Jonathan Schubert & Andrea Schulze & Chrisostomos Prodromou & Hannes Neuweiler, 2021. "Two-colour single-molecule photoinduced electron transfer fluorescence imaging microscopy of chaperone dynamics," Nature Communications, Nature, vol. 12(1), pages 1-12, December.
    5. Zhong Guo & Rinky D. Parakra & Ying Xiong & Wayne A. Johnston & Patricia Walden & Selvakumar Edwardraja & Shayli Varasteh Moradi & Jacobus P. J. Ungerer & Hui-wang Ai & Jonathan J. Phillips & Kirill A, 2022. "Engineering and exploiting synthetic allostery of NanoLuc luciferase," Nature Communications, Nature, vol. 13(1), pages 1-12, December.
    6. Zhihong Xiao & Jinyin Zha & Xu Yang & Tingting Huang & Shuxin Huang & Qi Liu & Xiaozheng Wang & Jie Zhong & Jianting Zheng & Rubing Liang & Zixin Deng & Jian Zhang & Shuangjun Lin & Shaobo Dai, 2024. "A three-level regulatory mechanism of the aldo-keto reductase subfamily AKR12D," Nature Communications, Nature, vol. 15(1), pages 1-15, December.
    7. Leonila Lagunes & Lee Bardwell & German A Enciso, 2020. "Effect of magnitude and variability of energy of activation in multisite ultrasensitive biochemical processes," PLOS Computational Biology, Public Library of Science, vol. 16(8), pages 1-26, August.
    8. Luhao Zhang & Maodong Li & Zhirong Liu, 2018. "A comprehensive ensemble model for comparing the allosteric effect of ordered and disordered proteins," PLOS Computational Biology, Public Library of Science, vol. 14(12), pages 1-22, December.
    9. Zhong Guo & Oleh Smutok & Wayne A. Johnston & Patricia Walden & Jacobus P. J. Ungerer & Thomas S. Peat & Janet Newman & Jake Parker & Tom Nebl & Caryn Hepburn & Artem Melman & Richard J. Suderman & Ev, 2021. "Design of a methotrexate-controlled chemical dimerization system and its use in bio-electronic devices," Nature Communications, Nature, vol. 12(1), pages 1-13, December.
    10. Yichen Yu & Robert T. O’Neill & Roman Boulatov & Ross A. Widenhoefer & Stephen L. Craig, 2023. "Allosteric control of olefin isomerization kinetics via remote metal binding and its mechanochemical analysis," Nature Communications, Nature, vol. 14(1), pages 1-10, December.
    11. Robert Kalescky & Hongyu Zhou & Jin Liu & Peng Tao, 2016. "Rigid Residue Scan Simulations Systematically Reveal Residue Entropic Roles in Protein Allostery," PLOS Computational Biology, Public Library of Science, vol. 12(4), pages 1-21, April.
    12. Manuel Weh & Kazutaka Shoyama & Frank Würthner, 2023. "Preferential molecular recognition of heterochiral guests within a cyclophane receptor," Nature Communications, Nature, vol. 14(1), pages 1-10, December.
    13. David P. Tilly & Jean-Paul Heeb & Simon J. Webb & Jonathan Clayden, 2023. "Switching imidazole reactivity by dynamic control of tautomer state in an allosteric foldamer," Nature Communications, Nature, vol. 14(1), pages 1-7, December.

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