Literature DB >> 23096346

Oligomerization of polytopic α-helical membrane proteins: causes and consequences.

Florian Cymer1, Dirk Schneider.   

Abstract

Several polytopic α-helical membrane-integrated proteins appear to be organized in higher-ordered oligomeric complexes. While many aspects are still enigmatic, in recent years, the physiological impact of membrane protein oligomerization has been analyzed to some extent. In the present article, oligomerization of structurally well-defined membrane proteins is discussed. The available experimental information indicates the causes and physiological consequences of membrane protein oligomerization, including stabilization, cooperative functions, and control of specific activities. Based on the currently available observations, we aim to derive some general principles and discuss open questions.

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Year:  2012        PMID: 23096346     DOI: 10.1515/hsz-2012-0231

Source DB:  PubMed          Journal:  Biol Chem        ISSN: 1431-6730            Impact factor:   3.915


  9 in total

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Review 4.  Life at the border: adaptation of proteins to anisotropic membrane environment.

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Journal:  Biochemistry       Date:  2014-06-03       Impact factor: 3.162

7.  Functional consequences of the oligomeric assembly of proteorhodopsin.

Authors:  Sunyia Hussain; Maia Kinnebrew; Nicole S Schonenbach; Emily Aye; Songi Han
Journal:  J Mol Biol       Date:  2015-01-15       Impact factor: 5.469

8.  Transmembrane domain quality control systems operate at the endoplasmic reticulum and Golgi apparatus.

Authors:  Kit Briant; Nicholas Johnson; Eileithyia Swanton
Journal:  PLoS One       Date:  2017-04-06       Impact factor: 3.240

9.  Accurate Determination of Conformational Transitions in Oligomeric Membrane Proteins.

Authors:  Máximo Sanz-Hernández; Vitaly V Vostrikov; Gianluigi Veglia; Alfonso De Simone
Journal:  Sci Rep       Date:  2016-03-15       Impact factor: 4.379

  9 in total

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