Walid A. Houry

Phylogenetic web profiler.

The N-terminal zinc binding domain of ClpX is a dimerization domain that modulates the chaperone function.

Solution structure of the dimeric zinc binding domain of the chaperone ClpX.

Chaperone networks in bacteria: analysis of protein homeostasis in minimal cells.

The ClpP double ring tetradecameric protease exhibits plastic ring-ring interactions, and the N termini of its subunits form flexible loops that are essential for ClpXP and ClpAP complex formation.

Navigating the chaperone network: an integrative map of physical and genetic interactions mediated by the hsp90 chaperone.

Quantitative NMR spectroscopy of supramolecular complexes: dynamic side pores in ClpP are important for product release.

Formation of a distinctive complex between the inducible bacterial lysine decarboxylase and a novel AAA+ ATPase.

Hsp90: a chaperone for protein folding and gene regulation.

MoxR AAA+ ATPases: a novel family of molecular chaperones?

Large nucleotide-dependent movement of the N-terminal domain of the ClpX chaperone.

Hsp90 at the crossroads of genetics and epigenetics.

Specificity in substrate and cofactor recognition by the N-terminal domain of the chaperone ClpX.

Molecular interaction network of the Hsp90 chaperone system.

ClpP: a distinctive family of cylindrical energy-dependent serine proteases.

AAA+ proteins: diversity in function, similarity in structure.

Yeast Rvb1 and Rvb2 are ATP-dependent DNA helicases that form a heterohexameric complex.

Molecular chaperone Hsp90 stabilizes Pih1/Nop17 to maintain R2TP complex activity that regulates snoRNA accumulation.

The AAA+ superfamily of functionally diverse proteins.

An atlas of chaperone-protein interactions in Saccharomyces cerevisiae: implications to protein folding pathways in the cell.

The genetic landscape of a cell.

Rvb1-Rvb2: essential ATP-dependent helicases for critical complexes.

Comparison of the multiple oligomeric structures observed for the Rvb1 and Rvb2 proteins.

AAA proteins: movers and shakers.

Tamoxifen enhances the Hsp90 molecular chaperone ATPase activity.

Acid stress response in enteropathogenic gammaproteobacteria: an aptitude for survival.

Structural and theoretical studies indicate that the cylindrical protease ClpP samples extended and compact conformations.

The Clp chaperones and proteases of the human malaria parasite Plasmodium falciparum.

Alternative oligomeric states of the yeast Rvb1/Rvb2 complex induced by histidine tags.

Structure of RavA MoxR AAA+ protein reveals the design principles of a molecular cage modulating the inducible lysine decarboxylase activity.

Linkage between the bacterial acid stress and stringent responses: the structure of the inducible lysine decarboxylase.

Bioinformatic approach to identify chaperone pathway relationship from large-scale interaction networks.

The R2TP complex: Discovery and functions.

Activators of cylindrical proteases as antimicrobials: identification and development of small molecule activators of ClpP protease.

The role of Hsp90 in protein complex assembly.

The enzymatic activities of the Escherichia coli basic aliphatic amino acid decarboxylases exhibit a pH zone of inhibition.

The structure of the minimal tetratricopeptide repeat domain protein Tah1 reveals the mechanism of its interaction with Pih1 and Hsp90.