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 …

Comparing protein folding in vitro and in vivo: foldability meets the fitness challenge

KS Hingorani, LM Gierasch - Current opinion in structural biology, 2014 - Elsevier
Highlights•This review discusses how folding in the test tube differs from folding in vivo.•New
research is shedding light on the complex in vivo folding landscape.•Many selective …

Repair or degrade: the thermodynamic dilemma of cellular protein quality-control

B Fauvet, ME Rebeaud, S Tiwari… - Frontiers in molecular …, 2021 - frontiersin.org
Life is a non-equilibrium phenomenon. Owing to their high free energy content, the
macromolecules of life tend to spontaneously react with ambient oxygen and water and turn …

Cellular disulfide bond formation in bioactive peptides and proteins

NA Patil, J Tailhades, RA Hughes, F Separovic… - International journal of …, 2015 - mdpi.com
Bioactive peptides play important roles in metabolic regulation and modulation and many
are used as therapeutics. These peptides often possess disulfide bonds, which are …

[HTML][HTML] Endoplasmic reticulum-unfolded protein response pathway modulates the cellular response to mitochondrial proteotoxic stress

R Sarkar, KBN Rao, MP Jha, K Mapa - Cell Stress and Chaperones, 2022 - Elsevier
Mitochondria and endoplasmic reticulum (ER) remain closely tethered by contact sites to
maintain unhindered biosynthetic, metabolic, and signalling functions. Apart from its …

Folding pathway of a discontinuous two-domain protein

G Agam, A Barth, DC Lamb - Nature Communications, 2024 - nature.com
It is estimated that two-thirds of all proteins in higher organisms are composed of multiple
domains, many of them containing discontinuous folds. However, to date, most in vitro …

Monitoring conformational heterogeneity of the lid of DnaK substrate‐binding domain during its chaperone cycle

R Banerjee, GG Jayaraj, JJ Peter, V Kumar… - The FEBS …, 2016 - Wiley Online Library
DnaK or Hsp70 of Escherichia coli is a master regulator of the bacterial proteostasis
network. Allosteric communication between the two functional domains of DnaK, the N …

Classification of chemical chaperones based on their effect on protein folding landscapes

R Dandage, A Bandyopadhyay, GG Jayaraj… - ACS Chemical …, 2015 - ACS Publications
Various small molecules present in biological systems can assist protein folding in vitro and
are known as chemical chaperones. De novo design of chemical chaperones with higher …

[HTML][HTML] Directed evolution to improve protein folding in vivo

V Sachsenhauser, JCA Bardwell - Current opinion in structural biology, 2018 - Elsevier
Highlights•Folding reporters and stability selections enable isolation of optimized folding
variants in vivo.•Host organisms can be evolved to provide a better folding environment.• …

Stress responses elicited by misfolded proteins targeted to mitochondria

KBN Rao, P Pandey, R Sarkar, A Ghosh… - Journal of Molecular …, 2022 - Elsevier
The double-membrane-bound architecture of mitochondria, essential for ATP production,
sub-divides the organelle into inter-membrane space (IMS) and matrix. IMS and matrix …