Literature DB >> 20005798

During transitions proteins make fleeting bonds.

David D Boehr1.   

Abstract

How do proteins efficiently and precisely shift from one conformation to another? Gardino et al. (2009) show that transient hydrogen bonds are critical to the conformational transition of the nitrogen regulatory protein NtrC between its native state and its active state.

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Year:  2009        PMID: 20005798     DOI: 10.1016/j.cell.2009.11.031

Source DB:  PubMed          Journal:  Cell        ISSN: 0092-8674            Impact factor:   41.582


  5 in total

1.  A combined molecular dynamics and rapid kinetics approach to identify conserved three-dimensional communication networks in elongation factor Tu.

Authors:  Hans-Joachim Wieden; Evan Mercier; John Gray; Brett Steed; Davis Yawney
Journal:  Biophys J       Date:  2010-12-01       Impact factor: 4.033

2.  XerR, a negative regulator of XccR in Xanthomonas campestris pv. campestris, relieves its repressor function in planta.

Authors:  Li Wang; Lili Zhang; Yunfeng Geng; Wei Xi; Rongxiang Fang; Yantao Jia
Journal:  Cell Res       Date:  2011-04-12       Impact factor: 25.617

3.  The free energy landscape in translational science: how can somatic mutations result in constitutive oncogenic activation?

Authors:  Chung-Jung Tsai; Ruth Nussinov
Journal:  Phys Chem Chem Phys       Date:  2014-01-21       Impact factor: 3.676

Review 4.  Tuning the "violin" of protein kinases: The role of dynamics-based allostery.

Authors:  Lalima G Ahuja; Susan S Taylor; Alexandr P Kornev
Journal:  IUBMB Life       Date:  2019-05-07       Impact factor: 3.885

Review 5.  Principles of allosteric interactions in cell signaling.

Authors:  Ruth Nussinov; Chung-Jung Tsai; Jin Liu
Journal:  J Am Chem Soc       Date:  2014-12-15       Impact factor: 15.419

  5 in total

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