Literature DB >> 15572255

Anionic regulation of biological systems: the special role of chloride in the coagulation cascade.

Enrico Di Stasio1.   

Abstract

The discovery that previously unidentified allosteric properties of several proteins, such as fibrinogen and myoglobin, can be triggered by anions binding, has suggested the possibility to design a new "active" role of chloride in the modulation of a broad range of biological systems. The molecular bases of the anions binding to proteins depends by their charge density in turn regulating the ability to bind water molecules and interact with basic groups on proteins. This review reports the role of the physiologically relevant chloride, and of other anions, in the regulation of several proteins, with special attention to the coagulation cascade. Moreover, possible mechanisms of modification of plasma, intra- or extracellular chloride concentration are listed.

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Year:  2004        PMID: 15572255     DOI: 10.1016/j.bpc.2004.07.026

Source DB:  PubMed          Journal:  Biophys Chem        ISSN: 0301-4622            Impact factor:   2.352


  3 in total

1.  Structural analysis of a Vibrio phospholipase reveals an unusual Ser-His-chloride catalytic triad.

Authors:  Ye Wan; Changshui Liu; Qingjun Ma
Journal:  J Biol Chem       Date:  2019-05-09       Impact factor: 5.157

2.  Structure and specificity of a binary tandem domain F-lectin from striped bass (Morone saxatilis).

Authors:  Mario A Bianchet; Eric W Odom; Gerardo R Vasta; L Mario Amzel
Journal:  J Mol Biol       Date:  2010-06-16       Impact factor: 5.469

Review 3.  Chloride channels: often enigmatic, rarely predictable.

Authors:  Charity Duran; Christopher H Thompson; Qinghuan Xiao; H Criss Hartzell
Journal:  Annu Rev Physiol       Date:  2010       Impact factor: 19.318

  3 in total

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