[HTML][HTML] Probiotic gastrointestinal transit and colonization after oral administration: A long journey

S Han, Y Lu, J Xie, Y Fei, G Zheng, Z Wang… - Frontiers in cellular …, 2021 - frontiersin.org
Orally administered probiotics encounter various challenges on their journey through the
mouth, stomach, intestine and colon. The health benefits of probiotics are diminished mainly …

In vivo aspects of protein folding and quality control

D Balchin, M Hayer-Hartl, FU Hartl - Science, 2016 - science.org
BACKGROUND Proteins are synthesized on ribosomes as linear chains of amino acids and
must fold into unique three-dimensional structures to fulfill their biological functions. Protein …

Unravelling biological macromolecules with cryo-electron microscopy

R Fernandez-Leiro, SHW Scheres - Nature, 2016 - nature.com
Abstract Knowledge of the three-dimensional structures of proteins and other biological
macromolecules often aids understanding of how they perform complicated tasks in the cell …

Chaperone machines for protein folding, unfolding and disaggregation

H Saibil - Nature reviews Molecular cell biology, 2013 - nature.com
Molecular chaperones are diverse families of multidomain proteins that have evolved to
assist nascent proteins to reach their native fold, protect subunits from heat shock during the …

The GroEL–GroES chaperonin machine: a nano-cage for protein folding

M Hayer-Hartl, A Bracher, FU Hartl - Trends in biochemical sciences, 2016 - cell.com
The bacterial chaperonin GroEL and its cofactor GroES constitute the paradigmatic
molecular machine of protein folding. GroEL is a large double-ring cylinder with ATPase …

Cryo-EM: a unique tool for the visualization of macromolecular complexity

E Nogales, SHW Scheres - Molecular cell, 2015 - cell.com
3D cryo-electron microscopy (cryo-EM) is an expanding structural biology technique that has
recently undergone a quantum leap progression in its achievable resolution and its …

Molecular chaperone functions in protein folding and proteostasis

YE Kim, MS Hipp, A Bracher… - Annual review of …, 2013 - annualreviews.org
The biological functions of proteins are governed by their three-dimensional fold. Protein
folding, maintenance of proteome integrity, and protein homeostasis (proteostasis) critically …

Time-resolved cryo-EM using a combination of droplet microfluidics with on-demand jetting

S Torino, M Dhurandhar, A Stroobants, R Claessens… - Nature …, 2023 - nature.com
Single-particle cryogenic electron microscopy (cryo-EM) allows reconstruction of high-
resolution structures of proteins in different conformations. Protein function often involves …

Structural probing of a protein phosphatase 2A network by chemical cross-linking and mass spectrometry

F Herzog, A Kahraman, D Boehringer, R Mak… - Science, 2012 - science.org
The identification of proximate amino acids by chemical cross-linking and mass
spectrometry (XL-MS) facilitates the structural analysis of homogeneous protein complexes …

Structure and allostery of the chaperonin GroEL

HR Saibil, WA Fenton, DK Clare, AL Horwich - Journal of molecular biology, 2013 - Elsevier
Chaperonins are intricate allosteric machines formed of two back-to-back, stacked rings of
subunits presenting end cavities lined with hydrophobic binding sites for nonnative …