Search Results - "Bardwell, James C. A"

Trigger factor both holds and folds its client proteins by Wu, Kevin, Minshull, Thomas C., Radford, Sheena E., Calabrese, Antonio N., Bardwell, James C. A.

“…ATP-independent chaperones like trigger factor are generally assumed to play passive roles in protein folding by acting as holding chaperones. Here we show…”
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Mechanism of the small ATP-independent chaperone Spy is substrate specific by Mitra, Rishav, Gadkari, Varun V., Meinen, Ben A., van Mierlo, Carlo P. M., Ruotolo, Brandon T., Bardwell, James C. A.

“…ATP-independent chaperones are usually considered to be holdases that rapidly bind to non-native states of substrate proteins and prevent their aggregation…”
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Flexible, symmetry-directed approach to assembling protein cages by Sciore, Aaron, Su, Min, Koldewey, Philipp, Eschweiler, Joseph D., Diffley, Kelsey A., Linhares, Brian M., Ruotolo, Brandon T., Bardwell, James C. A., Skiniotis, Georgios, Marsh, E. Neil G.

“…The assembly of individual protein subunits into large-scale symmetrical structures is widespread in nature and confers new biological properties. Engineered…”
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Chaperone activation by unfolding by Foit, Linda, George, Jenny S., Zhang, Bin W., Brooks, Charles L., Bardwell, James C. A.

“…Conditionally disordered proteins can alternate between highly ordered and less ordered configurations under physiological conditions. Whereas protein function…”
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Snapshots of DsbA in Action: Detection of Proteins in the Process of Oxidative Folding by Kadokura, Hiroshi, Tian, Hongping, Zander, Thomas, James C. A. Bardwell, Beckwith, Jon

“…DsbA, a thioredoxin superfamily member, introduces disulfide bonds into newly translocated proteins. This process is thought to occur via formation of mixed…”
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Cytosolic Selection Systems To Study Protein Stability by Malik, Ajamaluddin, Mueller-Schickert, Antje, Bardwell, James C. A

“…Here we describe biosensors that provide readouts for protein stability in the cytosolic compartment of prokaryotes. These biosensors consist of tripartite…”
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Protein folding while chaperone bound is dependent on weak interactions by Wu, Kevin, Stull, Frederick, Lee, Changhan, Bardwell, James C. A.

“…It is generally assumed that protein clients fold following their release from chaperones instead of folding while remaining chaperone-bound, in part because…”
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A cytochrome c is the natural electron acceptor for nicotine oxidoreductase by Dulchavsky, Mark, Clark, Christopher T., Bardwell, James C. A., Stull, Frederick

“…Nicotine oxidoreductase (NicA2), a member of the flavin-containing amine oxidase family, is of medical relevance as it shows potential as a therapeutic to aid…”
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Protein G-quadruplex interactions and their effects on phase transitions and protein aggregation by Sahoo, Bikash R, Kocman, Vojč, Clark, Nathan, Myers, Nikhil, Deng, Xiexiong, Wong, Ee L, Yang, Harry J, Kotar, Anita, Guzman, Bryan B, Dominguez, Daniel, Plavec, Janez, Bardwell, James C A

“…The SERF family of proteins were originally discovered for their ability to accelerate amyloid formation. Znf706 is an uncharacterized protein whose N-terminus…”
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Author Correction: A cytochrome c is the natural electron acceptor for nicotine oxidoreductase by Dulchavsky, Mark, Clark, Christopher T., Bardwell, James C. A., Stull, Frederick

“…A Correction to this paper has been published: https://doi.org/10.1038/s41589-021-00756-z…”
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Folding against the wind by Stull, Frederick, Bardwell, James C. A.

“…Many thermodynamically unfavorable processes in biology are powered by ATP, the energy currency of the cell. New evidence suggests that chaperone-mediated…”
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Directed evolution unlocks oxygen reactivity for a nicotine-degrading flavoenzyme by Dulchavsky, Mark, Mitra, Rishav, Wu, Kevin, Li, Joshua, Boer, Karli, Liu, Xiaomeng, Zhang, Zhiyao, Vasquez, Cristian, Clark, Christopher T., Funckes, Kaitrin, Shankar, Kokila, Bonnet-Zahedi, Selene, Siddiq, Mohammad, Sepulveda, Yadira, Suhandynata, Raymond T., Momper, Jeremiah D., Calabrese, Antonio N., George, Olivier, Stull, Frederick, Bardwell, James C. A.

“…The flavoenzyme nicotine oxidoreductase (NicA2) is a promising injectable treatment to aid in the cessation of smoking, a behavior responsible for one in ten…”
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Do nucleic acids moonlight as molecular chaperones? by Docter, Brianne E, Horowitz, Scott, Gray, Michael J, Jakob, Ursula, Bardwell, James C A

“…Organisms use molecular chaperones to combat the unfolding and aggregation of proteins. While protein chaperones have been widely studied, here we demonstrate…”
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Capturing a Dynamic Chaperone–Substrate Interaction Using NMR-Informed Molecular Modeling by Salmon, Loïc, Ahlstrom, Logan S, Horowitz, Scott, Dickson, Alex, Brooks, Charles L, Bardwell, James C. A

“…Chaperones maintain a healthy proteome by preventing aggregation and by aiding in protein folding. Precisely how chaperones influence the conformational…”
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Symmetry‐Directed Self‐Assembly of a Tetrahedral Protein Cage Mediated by de Novo‐Designed Coiled Coils by Badieyan, Somayesadat, Sciore, Aaron, Eschweiler, Joseph D., Koldewey, Philipp, Cristie‐David, Ajitha S., Ruotolo, Brandon T., Bardwell, James C. A., Su, Min, Marsh, E. Neil G.

“…The organization of proteins into new hierarchical forms is an important challenge in synthetic biology. However, engineering new interactions between protein…”
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Protein unfolding as a switch from self-recognition to high-affinity client binding by Groitl, Bastian, Horowitz, Scott, Makepeace, Karl A. T., Petrotchenko, Evgeniy V., Borchers, Christoph H., Reichmann, Dana, Bardwell, James C. A., Jakob, Ursula

“…Stress-specific activation of the chaperone Hsp33 requires the unfolding of a central linker region. This activation mechanism suggests an intriguing…”
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Directed evolution to improve protein folding in vivo by Sachsenhauser, Veronika, Bardwell, James CA

“…[Display omitted] •Folding reporters and stability selections enable isolation of optimized folding variants in vivo.•Host organisms can be evolved to provide…”
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The CXXC Motif Is More than a Redox Rheostat by Quan, Shu, Schneider, Irmhild, Pan, Jonathan, Von Hacht, Annekathrin, Bardwell, James C.A.

“…The CXXC active-site motif of thiol-disulfide oxidoreductases is thought to act as a redox rheostat, the sequence of which determines its reduction potential…”
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Backbone 1H, 13C, and 15N chemical shift assignments for human SERF2 by Sahoo, Bikash R., Subramanian, Vivekanandan, Bardwell, James C.A.

“…Human small EDRK-rich factor protein SERF2 is a cellular driver of protein amyloid formation, a process that has been linked to neurodegenerative diseases…”
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An Engineered Pathway for the Formation of Protein Disulfide Bonds by Masip, Lluis, Pan, Jonathan L., Haldar, Suranjana, Penner-Hahn, James E., DeLisa, Matthew P., Georgiou, George, James C. A. Bardwell, Collet, Jean-François

“…We have engineered a pathway for the formation of disulfide bonds. By imposing evolutionary pressure, we isolated mutations that changed thioredoxin, which is…”
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