Results 81 to 90 of about 4,851 (193)

Evolution of N‐terminal mechanical lability as a determinant for Type III secretion

Protein Science, Volume 35, Issue 8, August 2026.
Abstract Many Gram‐negative pathogens critically depend on the Type III secretion system (T3SS) to inject effector proteins into host cells for colonization. Because the channel of the T3SS is narrow (~2 nm), effectors must be unfolded for secretion.
Katherine E. DaPron, Alexandre M. Plastow, Morgan R. Fink, Brandon Dzuba, Marc‐Andre LeBlanc, Thomas T. Perkins, Emad Tajkhorshid, Marcelo C. Sousa   +7 more
wiley   +1 more source

Crystal structures of asymmetric ClpX hexamers reveal nucleotide-dependent motions in a AAA+ protein-unfolding machine [PDF]

, 2009
ClpX is a AAA+ machine that uses the energy of ATP binding and hydrolysis to unfold native proteins and translocate unfolded polypeptides into the ClpP peptidase.
Sauer, Robert T, Glynn, Steven E., Martin, Andreas, Nager, Andrew Ross, Baker, Tania   +4 more
core   +1 more source

Quantifying the Release of Protein Substrates from AAA+ ATPase ClpX by Single Molecule Total Internal Reflection Fluorescence Microscopy [PDF]

, 2021
The safe disposal of proteins is an essential process for maintaining proteostasis in cells. AAA+ proteases, such as proteasomes, play a major role in selective degradation of proteins. Degradation by AAA+ proteases typically requires the substrate to be
Wang, Xiao
core   +1 more source

Whole‐transcriptome sequencing analyses identified exosomal circular RNAs in the plasma of pancreatic cancer patients as novel blood‐based biomarkers of disease

VIEW, Volume 7, Issue 4, August 2026.
Pancreatic cancer (PaCa) has a poor prognosis, with low resection rates and high relapse rates, highlighting the urgent need for novel diagnostic biomarkers. Here, we performed whole‐transcriptome sequencing of plasma‐derived exosomes from PaCa patients and identified several differentially expressed circular RNAs (circRNAs).
Xiaomeng He, Yang Di, Lixiang Sun, Zhirong Wu, Mengting Luo, Xin Zhang, Huaqin Sun, Wanli Xu, Wenchuan Wu, Boheng Zhang, Jin Wang   +10 more
wiley   +1 more source

Elucidating The Specificity Determinants Responsible For ClpX-Adaptor Interaction [PDF]

Biophysical Journal, 2009
The ClpXP proteolytic machinery in bacteria consists of the AAA+ ATPase protein ClpX and the serine peptidase ClpP. ClpX recognizes, unfolds, and translocates substrates into the protease chamber where hydrolysis of the polypeptide occurs. To control substrate-specificity, the cell uses adaptor proteins, such as SspB, to modulate substrate selection ...
Chowdhury, Tahmeena, Chien, Peter, Sauer, Robert T., Baker, Tania A.   +3 more
openaire   +1 more source

Engineering an Optogenetic pH‐Modulator in Bacteria

Advanced Science, Volume 13, Issue 42, 28 July 2026.
ABSTRACT Cells in many naturally occurring organisms routinely cooperate to control their extracellular pH in a dynamic and reversible manner, but this capability has been underexplored in synthetic biology. Here, we sought to engineer a microbial system that switches between two states —high and low extracellular pH— with minimal human intervention ...
Jenevieve Kuang, Olivia J. Armendarez, Wei‐Ting Chang, Matthew M. Hausladen, Shanna Bonanno, Daniel J. Wilson, Neel S. Joshi, Leila F. Deravi   +7 more
wiley   +1 more source

Subunit asymmetry and roles of conformational switching in the hexameric AAA+ ring of ClpX [PDF]

, 2015
The hexameric AAA+ ring of Escherichia coli ClpX, an ATP-dependent machine for protein unfolding and translocation, functions with the ClpP peptidase to degrade target substrates.
Benjamin M Stinson, Baytshtok, Vladimir, Robert T Sauer, Tania A Baker, Baker, Tania, Sauer, Robert T., Karl R Schmitz, Vladimir Baytshtok, Stinson, Benjamin Michael, Schmitz, Karl Robert   +9 more
core   +1 more source

The Mycobacterium tuberculosis ClpP1P2 Protease Interacts Asymmetrically with Its ATPase Partners ClpX and ClpC1. [PDF]

PLoS ONE, 2015
Clp chaperone-proteases are cylindrical complexes built from ATP-dependent chaperonerings that stack onto a proteolytic ClpP double-ring core to carry out substrate protein degradation.Interaction of the ClpP particle with the chaperone is mediated by an
Julia Leodolter, Jannis Warweg, Eilika Weber-Ban   +2 more
doaj   +1 more source

Protein Homeostasis and Mitochondrial Quality Control in Neurodegeneration

WIREs Mechanisms of Disease, Volume 18, Issue 4, July/August 2026.
Quality control pathways form an integrated proteostasis–mitochondrial quality control axis that maintains mitochondrial and cellular homeostasis. Failure of this coordinated network drives neuronal decline and contributes to neurodegeneration. ABSTRACT Quality control (QC) processes include a network of cellular pathways that prevent the accumulation ...
Rosa Di Lorenzo, Rola S. Zeidan, Riccardo Calvani, Vito Pesce, Emanuele Marzetti, Anna Picca   +5 more
wiley   +1 more source

A proteolytic AAA+ machine poised to unfold protein substrates

Nature Communications
AAA+ proteolytic machines unfold proteins before degrading them. Here, we present cryoEM structures of ClpXP-substrate complexes that reveal a postulated but heretofore unseen intermediate in substrate unfolding/degradation. A ClpX hexamer draws natively
Alireza Ghanbarpour, Robert T. Sauer, Joseph H. Davis   +2 more
doaj   +1 more source