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Protein Quality Control at Membranes

New Content ItemGuest Editors: Anne Bertolotti, Ramanujan Hegde, Peter Walter, Jonathan Weissman

Cells employ stringent quality control processes to ensure appropriate folding of proteins, which – if misfolded – could disrupt cell functions and lead to disease. Many of these strategies take place at cellular membranes, whose hydrophobic environment provides an additional challenge.

For this series we have invited Reviews and Q&As on how protein quality control is ensured at membranes, as well as why protein quality control is needed in the first place.

The series is open for submission of research articles that bring fresh insights into the causes and consequences of protein misfolding at membranes, as well as papers that report new methods or techniques of broad interest. 

To submit your paper please visit our website at:

“Image created by Bob Schiffrin (Astbury Centre for Structural Molecular Biology, University of Leeds); adapted from Bob Schiffrin, David Brockwell, and Sheena Radford’s review in this series: Outer membrane protein folding from an energy landscape perspective, BMC Biology, 2017” 

  1. Content type: Question and Answer

    Caenorhabditis elegans neurons have recently been found to throw out cellular debris for remote degradation and/or storage, adding an “extracellular garbage elimination” option to known intracellular protein and ...

    Authors: Meghan Lee Arnold, Ilija Melentijevic, Anna Joelle Smart and Monica Driscoll

    Citation: BMC Biology 2018 16:17

    Published on:

  2. Content type: Review

    Efficient movement of proteins across membranes is required for cell health. The translocation process is particularly challenging when the channel in the membrane through which proteins must pass is narrow—su...

    Authors: Elizabeth A. Craig

    Citation: BMC Biology 2018 16:11

    Published on:

  3. Content type: Review

    The efficient production, folding, and secretion of proteins is critical for cancer cell survival. However, cancer cells thrive under stress conditions that damage proteins, so many cancer cells overexpress mo...

    Authors: Sara Sannino and Jeffrey L. Brodsky

    Citation: BMC Biology 2017 15:109

    Published on:

  4. Content type: Research article

    Many proteins of the mitochondrial intermembrane space (IMS) contain structural disulfide bonds formed by the mitochondrial disulfide relay. In fungi and animals, the sulfhydryl oxidase Erv1 ‘generates’ disulf...

    Authors: Valentina Peleh, Flavien Zannini, Sandra Backes, Nicolas Rouhier and Johannes M. Herrmann

    Citation: BMC Biology 2017 15:106

    Published on: