Protein export through the bacterial Sec pathway

A Tsirigotaki, J De Geyter, A Economou… - Nature Reviews …, 2017 - nature.com
The general secretory (Sec) pathway comprises an essential, ubiquitous and universal
export machinery for most proteins that integrate into, or translocate through, the plasma …

Molecular chaperones in the cytosol: from nascent chain to folded protein

FU Hartl, M Hayer-Hartl - Science, 2002 - science.org
Efficient folding of many newly synthesized proteins depends on assistance from molecular
chaperones, which serve to prevent protein misfolding and aggregation in the crowded …

Recombinant protein folding and misfolding in Escherichia coli

F Baneyx, M Mujacic - Nature biotechnology, 2004 - nature.com
The past 20 years have seen enormous progress in the understanding of the mechanisms
used by the enteric bacterium Escherichia coli to promote protein folding, support protein …

Pathways of chaperone-mediated protein folding in the cytosol

JC Young, VR Agashe, K Siegers… - Nature reviews Molecular …, 2004 - nature.com
Cells are faced with the task of folding thousands of different polypeptides into a wide range
of conformations. For many proteins, the folding process requires the action of molecular …

Oxidative demethylation by Escherichia coli AlkB directly reverts DNA base damage

SC Trewick, TF Henshaw, RP Hausinger, T Lindahl… - Nature, 2002 - nature.com
Methylating agents generate cytotoxic and mutagenic DNA damage. Cells use 3-
methyladenine-DNA glycosylases to excise some methylated bases from DNA, and suicidal …

Recombinant protein secretion in Escherichia coli

FJM Mergulhão, DK Summers, GA Monteiro - Biotechnology advances, 2005 - Elsevier
The secretory production of recombinant proteins by the Gram-negative bacterium
Escherichia coli has several advantages over intracellular production as inclusion bodies. In …

The ribosome as a platform for co-translational processing, folding and targeting of newly synthesized proteins

G Kramer, D Boehringer, N Ban, B Bukau - Nature structural & …, 2009 - nature.com
The early events in the life of newly synthesized proteins in the cellular environment are
remarkably complex. Concurrently with their synthesis by the ribosome, nascent …

Structural basis for protein antiaggregation activity of the trigger factor chaperone

T Saio, X Guan, P Rossi, A Economou, CG Kalodimos - Science, 2014 - science.org
Introduction Molecular chaperones prevent aggregation and misfolding of proteins in the
cellular environment and are thus central to maintaining protein homeostasis. Molecular …

[HTML][HTML] Structure and function of the molecular chaperone Trigger Factor

A Hoffmann, B Bukau, G Kramer - … et Biophysica Acta (BBA)-Molecular Cell …, 2010 - Elsevier
Newly synthesized proteins require the assistance of molecular chaperones to efficiently fold
into functional three-dimensional structures in the crowded environment of the cell. At first …

Protein aggregation and amyloidosis: confusion of the kinds?

F Rousseau, J Schymkowitz, L Serrano - Current opinion in structural …, 2006 - Elsevier
Recent years have witnessed major advances in our understanding of the structural basis of
protein aggregation on several fronts. Firstly, high-resolution structural information that …