In-cell NMR spectroscopy

Reckel, Sina; Hänsel, Robert; Löhr, Frank; Dötsch, Volker

doi:10.1016/j.pnmrs.2007.02.002

Cited by 49 publications

(38 citation statements)

References 70 publications

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“…Reckel et al [112] discussed the aim of in-cell NMR spectroscopy. The noninvasive character of in-cell NMR spectroscopy makes it the only biophysical method that enables the direct in-cell observation of conformational changes, post-translational modifications and binding events with high structural resolution in living cells.…”

Section: Ligand-dna Ligand-rna and Ligand Membrane Interactionsmentioning

confidence: 99%

NMR Spectroscopy for Studying Interactions of Bioactive Molecules

Novak¹,

Jednačak²

2012

Physico-Chemical Methods in Drug Discovery and Development

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Section: Ligand-dna Ligand-rna and Ligand Membrane Interactionsmentioning

confidence: 99%

NMR Spectroscopy for Studying Interactions of Bioactive Molecules

Novak¹,

Jednačak²

2012

Physico-Chemical Methods in Drug Discovery and Development

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“…I n-cell NMR represents a unique tool for characterizing physiological processes and their alteration in the 'natural' environment, that is, within a live cellular context, with an atomic-level approach [1][2][3][4][5][6][7][8][9] . This level of characterization is necessary to understand the molecular cause of cell malfunction in pathological states and to develop treatments and therapeutic protocols.…”

mentioning

confidence: 99%

In-cell NMR reveals potential precursor of toxic species from SOD1 fALS mutants

et al. 2014

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Mutations in the superoxide dismutase 1 (SOD1) gene are related to familial cases of amyotrophic lateral sclerosis (fALS). Here we exploit in-cell NMR to characterize the protein folding and maturation of a series of fALS-linked SOD1 mutants in human cells and to obtain insight into their behaviour in the cellular context, at the molecular level. The effect of various mutations on SOD1 maturation are investigated by changing the availability of metal ions in the cells, and by coexpressing the copper chaperone for SOD1, hCCS. We observe for most of the mutants the occurrence of an unstructured SOD1 species, unable to bind zinc. This species may be a common precursor of potentially toxic oligomeric species, that are associated with fALS. Coexpression of hCCS in the presence of copper restores the correct maturation of the SOD1 mutants and prevents the formation of the unstructured species, confirming that hCCS also acts as a molecular chaperone.

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“…NMR spectroscopy is well suited to study protein structure and dynamics in vivo or in "cell-like" environments, and a number of compelling examples have been reported [10][11][12][13][14][15][16]. Here, we are interested in extending such studies to folding pathways and the characterization of "invisible" protein conformers that are visited from the native state and play important roles in both folding and misfolding processes.…”

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confidence: 99%