Search Results - "Waldburger, Carey"

Structure of the entire cytoplasmic portion of a sensor histidine-kinase protein by Marina, Alberto, Waldburger, Carey D, Hendrickson, Wayne A

“…The large majority of histidine kinases (HKs) are multifunctional enzymes having autokinase, phosphotransfer and phosphatase activities, and most of these are…”
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Crystal Structure of a Functional Dimer of the PhoQ Sensor Domain by Cheung, Jonah, Bingman, Craig A., Reyngold, Marsha, Hendrickson, Wayne A., Waldburger, Carey D.

“…The PhoP-PhoQ two-component system is a well studied bacterial signaling system that regulates virulence and stress response. Catalytic activity of the…”
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Are buried salt bridges important for protein stability and conformational specificity? by Waldburger, Carey D, Schildbach, Joel F, Sauer, Robert T

“…The side chains of Arg 31, Glu 36 and Arg 40 in Arc repressor form a buried salt-bridge triad. The entire salt-bridge network can be replaced by hydrophobic…”
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Determination of the Physiological Dimer Interface of the PhoQ Sensor Domain by Goldberg, Shalom D., Soto, Cinque S., Waldburger, Carey D., DeGrado, William F.

“…PhoQ is the transmembrane sensor kinase of the phoPQ two-component system, which detects and responds to divalent cations and antimicrobial peptides and can…”
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Characterization of a New Member of the Fatty Acid-binding Protein Family That Binds All-trans-retinol by Vogel, Silke, Mendelsohn, Cathy L., Mertz, James R., Piantedosi, Roseann, Waldburger, Carey, Gottesman, Max E., Blaner, William S.

“…Cellular retinol-binding protein, type I (CRBP-I) and type II (CRBP-II) are the only members of the fatty acid-binding protein (FABP) family that process…”
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Repression of Escherichia coli PhoP-PhoQ Signaling by Acetate Reveals a Regulatory Role for Acetyl Coenzyme A by Lesley, Joseph A, Waldburger, Carey D

“…Article Usage Stats Services JB Citing Articles Google Scholar PubMed Related Content Social Bookmarking CiteULike Delicious Digg Facebook Google+ Mendeley…”
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Barriers to Protein Folding: Formation of Buried Polar Interactions is a Slow Step in Acquisition of Structure by Waldburger, Carey D., Jonsson, Thorlakur, Sauer, Robert T.

“…In the MYL mutant of the Arc repressor dimer, sets of partially buried salt-bridge and hydrogen-bond interactions mediated by Arg-31, Glu-36, and Arg-40 in…”
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His-Asp Signal Transduction via a Monomeric Histidine Phosphotransfer Protein by Waldburger, Carey D

“…The cocrystal structure of the yeast YPD1 histidine phosphotransfer domain in complex with its SLN1 phosphodonor by Xu and coworkers (this issue of Structure)…”
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Mutational Analysis of the Escherichia coli PhoQ Sensor Kinase: Differences with the Salmonella enterica Serovar Typhimurium PhoQ Protein and in the Mechanism of Mg2+ and Ca2+ Sensing by Regelmann, Adam G, Lesley, Joseph A, Mott, Christina, Stokes, Lissette, Waldburger, Carey D

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P22 Arc Repressor: Transition State Properties Inferred from Mutational Effects on the Rates of Protein Unfolding and Refolding by Milla, Marcos E, Brown, Bronwen M, Waldburger, Carey D, Sauer, Robert T

“…The kinetics of unfolding and refolding have been measured for a set of Arc repressor mutants bearing single amino acid substitutions at 44 of the 53 residue…”
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Domains of Mnt Repressor: Roles in Tetramer Formation, Protein Stability, and Operator DNA Binding by Waldburger, Carey D, Sauer, Robert T

“…The Mnt repressor of bacteriophage P22 is a member of the ribbon-helix-helix family of gene regulatory proteins. Proteolytic cleavage of Mnt with chymotrypsin…”
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Nonlinear Free Energy Relationships in Arc Repressor Unfolding Imply the Existence of Unstable, Native-like Folding Intermediates by Jonsson, Thorlakur, Waldburger, Carey D., Sauer, Robert T.

“…Under strongly denaturing conditions, the logarithm of the rate constant for dissociation/unfolding of the wild-type Arc dimer varies in a nonlinear fashion…”
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Comparison of the Pseudomonas aeruginosa andEscherichia coli PhoQ Sensor Domains by Lesley, Joseph A., Waldburger, Carey D.

“…The PhoP-PhoQ two-component system is present in a number of Gram-negative bacteria where it has roles in Mg 2+ homeostasis and virulence. PhoQ is a…”
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Structural and Mutational Analysis of the PhoQ Histidine Kinase Catalytic Domain by Marina, Alberto, Mott, Christina, Auyzenberg, Anna, Hendrickson, Wayne A., Waldburger, Carey D.

“…PhoQ is a transmembrane histidine kinase belonging to the family of two-component signal transducing systems common in prokaryotes and lower eukaryotes. In…”
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Signal Detection by the PhoQ Sensor-Transmitter by Waldburger, Carey D., Sauer, Robert T.

“…The PhoP-PhoQ two-component system is required for virulence and/or regulatory stress responses in enteric bacteria. The PhoQ protein responds to low…”
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Structural and mutational analysis of the PhoQ histidine kinase catalytic domain. Insight into the reaction mechanism by Marina, A, Mott, C, Auyzenberg, A, Hendrickson, W A, Waldburger, C D

“…PhoQ is a transmembrane histidine kinase belonging to the family of two-component signal transducing systems common in prokaryotes and lower eukaryotes. In…”
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Crystal Structure of a Functional Dimer of the PhoQ Sensor DomainS by Cheung, Jonah, Bingman, Craig A., Reyngold, Marsha, Hendrickson, Wayne A., Waldburger, Carey D.

“…The PhoP-PhoQ two-component system is a well studied bacterial signaling system that regulates virulence and stress response. Catalytic activity of the…”
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Comparison of the Pseudomonas aeruginosa and Escherichia coli PhoQ sensor domains: evidence for distinct mechanisms of signal detection by Lesley, J A, Waldburger, C D

“…The PhoP-PhoQ two-component system is present in a number of Gram-negative bacteria where it has roles in Mg(2+) homeostasis and virulence. PhoQ is a…”
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Signal detection by the PhoQ sensor-transmitter. Characterization of the sensor domain and a response-impaired mutant that identifies ligand-binding determinants by Waldburger, C D, Sauer, R T

“…The PhoP-PhoQ two-component system is required for virulence and/or regulatory stress responses in enteric bacteria. The PhoQ protein responds to low…”
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Mutational analysis of the Escherichia coli PhoQ sensor kinase: Differences with the Salmonella enterica serovar typhimurium PhoQ protein and in the mechanism of Mg2+ and by Regelmann, Adam G, Lesley, Joseph A, Mott, Christina, Stokes, Lissette, Waldburger, Carey D

“…The PhoP-PhoQ two-component system plays a role in Mg2+ homeostasis and/or the virulence properties of a number of bacterial species. A Salmonella enterica…”
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