Impact of cellular health conditions on the protein folding state in mammalian cells

Inomata, Kohsuke; Kamoshida, Hajime; Ikari, Masaomi; Ito, Yutaka; Kigawa, T.

doi:10.1039/c7cc06004a

Cited by 42 publications

(45 citation statements)

References 43 publications

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“…Cells undergo changes in metabolism as they die, and the loss of cell viability results in degradation of the in-cell spectrum. [22] To ensure that NMR signals arise from proteins located inside the cell, when the experiment is complete, the cells are Nicholas Sciolino is a graduate student in the Department of Chemistry at the State University of New York at Albany. He is a US Army veteran.…”

Section: Cell Viabilitymentioning

confidence: 99%

“…[25] Bioreactors, which sustain cells in the NMR spectrometer, have also been used to extend the time for data collection. [22,25,26]…”

Section: Davidmentioning

confidence: 99%

“…The second is cell viability. Cells undergo changes in metabolism as they die, and the loss of cell viability results in degradation of the in‐cell spectrum …”

Section: Introductionmentioning

confidence: 99%

“…Stabilizing the cells can also extend the in‐cell NMR acquisition time. This is accomplished by adding cell protectants, such as glycerol or sucrose, or by encapsulating the cells in alginate or agarose . Bioreactors, which sustain cells in the NMR spectrometer, have also been used to extend the time for data collection …”

Section: Introductionmentioning

confidence: 99%

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In‐Cell NMR Spectroscopy of Intrinsically Disordered Proteins

2019

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This review summarizes the results of in‐cell Nuclear Magnetic Resonance, NMR, spectroscopic investigations of the eukaryotic and prokaryotic intrinsically disordered proteins, IDPs: α‐synuclein, prokaryotic ubiquitin‐like protein, Pup, tubulin‐related neuronal protein, Tau, phenylalanyl‐glycyl‐repeat‐rich nucleoporins, FG Nups, and the negative regulator of flagellin synthesis, FlgM. The results show that the cellular behavior of IDPs may differ significantly from that observed in the test tube.

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Section: Cell Viabilitymentioning

confidence: 99%

“…[25] Bioreactors, which sustain cells in the NMR spectrometer, have also been used to extend the time for data collection. [22,25,26]…”

Section: Davidmentioning

confidence: 99%

“…The second is cell viability. Cells undergo changes in metabolism as they die, and the loss of cell viability results in degradation of the in‐cell spectrum …”

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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In‐Cell NMR Spectroscopy of Intrinsically Disordered Proteins

2019

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“…developed an elegant bioreactor system to maintain living cells inside an NMR tube and successfully characterized the binding interface of an externally introduced protein using STD . Other strategies, involving agar or alginate gels have been used to encapsulate cells and increase their viability . However, when studying extracellular components, these highly viscous gels are not suitable because the embedded proteins no longer tumble freely in solution.…”

Section: Figurementioning

confidence: 99%

NMR Characterization of Surface Receptor Protein Interactions in Live Cells Using Methylcellulose Hydrogels

et al. 2020

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Interactions of transmembrane receptors with their extracellular ligands are essential for cellular communication and signaling and are therefore a major focus in drug discovery programs. The transition from in vitro to live cell interaction studies, however, is typically a bottleneck in many drug discovery projects due to the challenge of obtaining atomic‐resolution information under near‐physiological conditions. Although NMR spectroscopy is ideally suited to overcome this limitation, several experimental impairments are still present. Herein, we propose the use of methylcellulose hydrogels to study extracellular proteins and their interactions with plasma membrane receptors. This approach reduces cell sedimentation, prevents the internalization of membrane receptors, and increases cell survival, while retaining the free tumbling of extracellular proteins.

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Advances in the cellular structural biology of nucleic acids

et al. 2018

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Conventional biophysical and chemical biology approaches for delineating relationships between the structure and biological function of nucleic acids (NAs) abstract NAs from their native biological context. However, cumulative experimental observations have revealed that the structure, dynamics and interactions of NAs might be strongly influenced by a broad spectrum of specific and nonspecific physical-chemical environmental factors. This consideration has recently sparked interest in the development of novel tools for structural characterization of NAs in the native cellular context. Here, we review the individual methods currently being employed for structural characterization of NA structure in a native cellular environment with a focus on recent advances and developments in the emerging fields of in-cell NMR and electron paramagnetic resonance spectroscopy and in-cell single-molecule FRET of NAs.

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Impact of cellular health conditions on the protein folding state in mammalian cells

Cited by 42 publications

References 43 publications

In‐Cell NMR Spectroscopy of Intrinsically Disordered Proteins

In‐Cell NMR Spectroscopy of Intrinsically Disordered Proteins

NMR Characterization of Surface Receptor Protein Interactions in Live Cells Using Methylcellulose Hydrogels

Advances in the cellular structural biology of nucleic acids

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