Author pages are created from data sourced from our academic publisher partnerships and public sources.
- Publications
- Influence
The Genetic Landscape of a Cell
- M. Costanzo, A. Baryshnikova, +50 authors Charles Boone
- Biology, Medicine
- Science
- 22 January 2010
Making Connections Genetic interaction profiles highlight cross-connections between bioprocesses, providing a global view of cellular pleiotropy, and enable the prediction of genetic network hubs.… Expand
Navigating the Chaperone Network: An Integrative Map of Physical and Genetic Interactions Mediated by the Hsp90 Chaperone
- R. Zhao, Michael Davey, +10 authors W. Houry
- Biology, Medicine
- Cell
- 11 March 2005
Physical, genetic, and chemical-genetic interactions centered on the conserved chaperone Hsp90 were mapped at high resolution in yeast using systematic proteomic and genomic methods. Physical… Expand
Molecular chaperone Hsp90 stabilizes Pih1/Nop17 to maintain R2TP complex activity that regulates snoRNA accumulation
- R. Zhao, Y. Kakihara, +9 authors W. Houry
- Biology, Medicine
- The Journal of cell biology
- 11 February 2008
Hsp90 is a highly conserved molecular chaperone that is involved in modulating a multitude of cellular processes. In this study, we identify a function for the chaperone in RNA processing and… Expand
An atlas of chaperone–protein interactions in Saccharomyces cerevisiae: implications to protein folding pathways in the cell
- Y. Gong, Y. Kakihara, +4 authors W. Houry
- Biology, Medicine
- Molecular systems biology
- 16 June 2009
Molecular chaperones are known to be involved in many cellular functions, however, a detailed and comprehensive overview of the interactions between chaperones and their cofactors and substrates is… Expand
Identification of in vivo substrates of the chaperonin GroEL
- W. Houry, D. Frishman, C. Eckerskorn, F. Lottspeich, F. Hartl
- Biology, Medicine
- Nature
- 11 November 1999
The chaperonin GroEL has an essential role in mediating protein folding in the cytosol of Escherichia coli. Here we show that GroEL interacts strongly with a well-defined set of approximately 300… Expand
Polypeptide Flux through Bacterial Hsp70 DnaK Cooperates with Trigger Factor in Chaperoning Nascent Chains
A role for DnaK, the major E. coli Hsp70, in chaperoning de novo protein folding has remained elusive. Here we show that under nonstress conditions DnaK transiently associates with a wide variety of… Expand
In Vivo Observation of Polypeptide Flux through the Bacterial Chaperonin System
- K. Ewalt, J. Hendrick, W. Houry, F. Hartl
- Biology, Medicine
- Cell
- 8 August 1997
The quantitative contribution of chaperonin GroEL to protein folding in E. coli was analyzed. A diverse set of newly synthesized polypeptides, predominantly between 10-55 kDa, interacts with GroEL,… Expand
Mechanisms of acid resistance in Escherichia coli.
Adaptation to acid stress is an important factor in the transmission of intestinal microbes. The enterobacterium Escherichia coli uses a range of physiological, metabolic, and proton-consuming acid… Expand
Linkage between the bacterial acid stress and stringent responses: the structure of the inducible lysine decarboxylase
- Usheer Kanjee, I. Gutsche, +8 authors W. Houry
- Biology, Medicine
- The EMBO journal
- 2 March 2011
The Escherichia coli inducible lysine decarboxylase, LdcI/CadA, together with the inner‐membrane lysine‐cadaverine antiporter, CadB, provide cells with protection against mild acidic conditions… Expand
ClpP: A distinctive family of cylindrical energy‐dependent serine proteases
Processes maintaining protein homeostasis in the cell are governed by the activities of molecular chaperones that mainly assist in the folding of polypeptide chains and by a large class of proteases… Expand
...
1
2
3
4
5
...