The mechanisms of integral membrane protein biogenesis
RS Hegde, RJ Keenan - Nature Reviews Molecular Cell Biology, 2022 - nature.com
Roughly one quarter of all genes code for integral membrane proteins that are inserted into
the plasma membrane of prokaryotes or the endoplasmic reticulum membrane of …
the plasma membrane of prokaryotes or the endoplasmic reticulum membrane of …
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 …
export machinery for most proteins that integrate into, or translocate through, the plasma …
HSP40 proteins use class-specific regulation to drive HSP70 functional diversity
O Faust, M Abayev-Avraham, AS Wentink, M Maurer… - Nature, 2020 - nature.com
The ubiquitous heat shock protein 70 (HSP70) family consists of ATP-dependent molecular
chaperones, which perform numerous cellular functions that affect almost all aspects of the …
chaperones, which perform numerous cellular functions that affect almost all aspects of the …
Using chemical shift perturbation to characterise ligand binding
MP Williamson - Progress in nuclear magnetic resonance spectroscopy, 2013 - Elsevier
Chemical shift perturbation (CSP, chemical shift mapping or complexation-induced changes
in chemical shift, CIS) follows changes in the chemical shifts of a protein when a ligand is …
in chemical shift, CIS) follows changes in the chemical shifts of a protein when a ligand is …
[HTML][HTML] Methyl TROSY spectroscopy: A versatile NMR approach to study challenging biological systems
S Schütz, R Sprangers - Progress in nuclear magnetic resonance …, 2020 - Elsevier
A major goal in structural biology is to unravel how molecular machines function in detail. To
that end, solution-state NMR spectroscopy is ideally suited as it is able to study biological …
that end, solution-state NMR spectroscopy is ideally suited as it is able to study biological …
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 …
cellular environment and are thus central to maintaining protein homeostasis. Molecular …
Structure of a complex of the ATPase SecA and the protein-translocation channel
Most proteins are secreted from bacteria by the interaction of the cytoplasmic SecA ATPase
with a membrane channel, formed by the heterotrimeric SecY complex. Here we report the …
with a membrane channel, formed by the heterotrimeric SecY complex. Here we report the …
Lipid nanodiscs for high-resolution NMR studies of membrane proteins
Membrane proteins (MPs) play essential roles in numerous cellular processes. Because
around 70% of the currently marketed drugs target MPs, a detailed understanding of their …
around 70% of the currently marketed drugs target MPs, a detailed understanding of their …
Unraveling the mechanism of protein disaggregation through a ClpB-DnaK interaction
HSP-100 protein machines, such as ClpB, play an essential role in reactivating protein
aggregates that can otherwise be lethal to cells. Although the players involved are known …
aggregates that can otherwise be lethal to cells. Although the players involved are known …
[HTML][HTML] An interdomain energetic tug-of-war creates the allosterically active state in Hsp70 molecular chaperones
A Zhuravleva, EM Clerico, LM Gierasch - Cell, 2012 - cell.com
The allosteric mechanism of Hsp70 molecular chaperones enables ATP binding to the N-
terminal nucleotide-binding domain (NBD) to alter substrate affinity to the C-terminal …
terminal nucleotide-binding domain (NBD) to alter substrate affinity to the C-terminal …