Search Results - "Delbecq, Scott P."

A conserved histidine modulates HSPB5 structure to trigger chaperone activity in response to stress-related acidosis by Rajagopal, Ponni, Tse, Eric, Borst, Andrew J, Delbecq, Scott P, Shi, Lei, Southworth, Daniel R, Klevit, Rachel E

“…Small heat shock proteins (sHSPs) are essential 'holdase' chaperones that form large assemblies and respond dynamically to pH and temperature stresses to…”
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Binding determinants of the small heat shock protein, αB-crystallin: recognition of the 'IxI' motif by Delbecq, Scott P, Jehle, Stefan, Klevit, Rachel

“…Small heat shock proteins (sHSPs) play a central role in protein homeostasis under conditions of stress by binding partly unfolded, aggregate‐prone proteins…”
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Acidic pH and divalent cation sensing by PhoQ are dispensable for systemic salmonellae virulence by Hicks, Kevin G, Delbecq, Scott P, Sancho-Vaello, Enea, Blanc, Marie-Pierre, Dove, Katja K, Prost, Lynne R, Daley, Margaret E, Zeth, Kornelius, Klevit, Rachel E, Miller, Samuel I

“…Salmonella PhoQ is a histidine kinase with a periplasmic sensor domain (PD) that promotes virulence by detecting the macrophage phagosome. PhoQ activity is…”
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One size does not fit all: The oligomeric states of αB crystallin by Delbecq, Scott P., Klevit, Rachel E.

“…Small Heat Shock Proteins (sHSPs) are a diverse family of molecular chaperones that delay protein aggregation through interactions with non-native and…”
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HSPB5 engages multiple states of a destabilized client to enhance chaperone activity in a stress-dependent manner by Delbecq, Scott P., Klevit, Rachel E.

“…Small heat shock proteins (sHSPs) delay protein aggregation in an ATP-independent manner by interacting with client proteins that are in states susceptible to…”
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A Mechanism of Subunit Recruitment in Human Small Heat Shock Protein Oligomers by Delbecq, Scott P, Rosenbaum, Joel C, Klevit, Rachel E

“…Small heat shock proteins (sHSPs) make up a class of molecular chaperones broadly observed across organisms. Many sHSPs form large oligomers that undergo…”
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The ubiquitin ligase SspH1 from Salmonella uses a modular and dynamic E3 domain to catalyze substrate ubiquitylation by Cook, Matt, Delbecq, Scott P., Schweppe, Thomas P., Guttman, Miklos, Klevit, Rachel E., Brzovic, Peter S.

“…SspH/IpaH bacterial effector E3 ubiquitin (Ub) ligases, unrelated in sequence or structure to eukaryotic E3s, are utilized by a wide variety of Gram-negative…”
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One size doesn't fit all: the oligomeric states of αB crystallin by Delbecq, Scott P., Klevit, Rachel E.

“…Small Heat Shock Proteins (sHSPs) are a diverse family of molecular chaperones that delay protein aggregation through interactions with nonnative and…”
Get full text

Binding determinants of the small heat shock protein, [alpha]B-crystallin: recognition of the 'IxI' motif by Delbecq, Scott P, Jehle, Stefan, Klevit, Rachel

“…Small heat shock proteins (sHSPs) play a central role in protein homeostasis under conditions of stress by binding partly unfolded, aggregate-prone proteins…”
Get full text

Defining Protein Interactions With Small Heat Shock Proteins by Delbecq, Scott P

“…Small heat shock proteins (sHSPs) are a class of molecular chaperones broadly observed across organisms where they play a central role in maintaining protein…”
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