• Publications
  • Influence
The Genetic Landscape of a Cell
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
  • 1,962
  • 175
  • PDF
Navigating the Chaperone Network: An Integrative Map of Physical and Genetic Interactions Mediated by the Hsp90 Chaperone
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. PhysicalExpand
  • 743
  • 31
  • PDF
Molecular chaperone Hsp90 stabilizes Pih1/Nop17 to maintain R2TP complex activity that regulates snoRNA accumulation
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 andExpand
  • 165
  • 28
  • PDF
An atlas of chaperone–protein interactions in Saccharomyces cerevisiae: implications to protein folding pathways in the cell
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 isExpand
  • 214
  • 26
  • PDF
Identification of in vivo substrates of the chaperonin GroEL
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 300Expand
  • 501
  • 24
  • PDF
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 ofExpand
  • 394
  • 19
  • PDF
In Vivo Observation of Polypeptide Flux through the Bacterial Chaperonin System
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
  • 336
  • 17
  • PDF
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 acidExpand
  • 178
  • 15
  • PDF
Linkage between the bacterial acid stress and stringent responses: the structure of the inducible lysine decarboxylase
The Escherichia coli inducible lysine decarboxylase, LdcI/CadA, together with the inner‐membrane lysine‐cadaverine antiporter, CadB, provide cells with protection against mild acidic conditionsExpand
  • 115
  • 15
  • PDF
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 proteasesExpand
  • 171
  • 13
  • PDF
...
1
2
3
4
5
...