Detection of protein-ligand interactions by NMR using reductive methylation of lysine residues. (Q46345558)

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14 January 2020

title

Detection of protein-ligand interactions by NMR using reductive methylation of lysine residues (English)

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14 January 2020

3

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14 January 2020

author name string

Sherwin J Abraham

series ordinal

1

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14 January 2020

Susanne Hoheisel

series ordinal

2

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14 January 2020

publication date

26 September 2008

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Journal of Biomolecular NMR

14 January 2020

published in

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14 January 2020

volume

42

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14 January 2020

issue

2

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14 January 2020

page(s)

143-148

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https://scigraph.springernature.com/pub.10.1007/s10858-008-9274-y

14 January 2020

exact match

0 references

cites work

N epsilon,N epsilon-dimethyl-lysine cytochrome c as an NMR probe for lysine involvement in protein-protein complex formation

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An isotope labeling strategy for methyl TROSY spectroscopy

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Mass spectrometry assisted assignment of NMR resonances in reductively 13C-methylated proteins.

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Implications of protein conformational diversity for binding and development of new biological active compounds.

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Target enzyme recognition by calmodulin: 2.4 A structure of a calmodulin-peptide complex

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Protein conformational changes studied by diffusion NMR spectroscopy: application to helix-loop-helix calcium binding proteins

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The conformation of apolipoprotein A-I in discoidal and spherical recombinant high density lipoprotein particles. 13C NMR studies of lysine ionization behavior

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12 December 2020

Hydrophobic interaction of the Ca2+-calmodulin complex with calmodulin antagonists. Naphthalenesulfonamide derivatives

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12 December 2020

13C NMR of methylated lysines of fd gene 5 protein: evidence for a conformational change involving lysine 24 upon binding of a negatively charged lanthanide chelate

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12 December 2020

Reductive methylation and 13C NMR studies of the lysyl residues of fd gene 5 protein. Lysines 24, 46, and 69 may be involved in nucleic acid binding

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12 December 2020

Structure of calmodulin bound to the hydrophobic IQ domain of the cardiac Ca(v)1.2 calcium channel

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12 December 2020

Reductive alkylation of lysine residues to alter crystallization properties of proteins

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The changing landscape of protein allostery

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Ca2+-induced hydrophobic site on calmodulin: application for purification of calmodulin by phenyl-Sepharose affinity chromatography.

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Growth factor-dependent AKT activation and cell migration requires the function of c-K(B)-Ras versus other cellular ras isoforms

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12 December 2020

Structural consequences of reductive methylation of lysine residues in hen egg white lysozyme: an X-ray analysis at 1.8-A resolution

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12 December 2020

Attenuated T2 relaxation by mutual cancellation of dipole-dipole coupling and chemical shift anisotropy indicates an avenue to NMR structures of very large biological macromolecules in solution

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Protein NMR-based screening in drug discovery

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The contribution of lysine-36 to catalysis by human myo-inositol monophosphatase

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Reversible intracellular translocation of KRas but not HRas in hippocampal neurons regulated by Ca2+/calmodulin.

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Melatonin and serotonin interactions with calmodulin: NMR, spectroscopic and biochemical studies

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Solution structure of calmodulin-W-7 complex: the basis of diversity in molecular recognition

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Molecular dynamics simulations revealed Ca(2+)-dependent conformational change of Calmodulin

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12 December 2020

Intramolecular interactions of amino groups in 13C reductively methylated hen egg-white lysozyme

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12 December 2020

Determination of the side chain pKa values of the lysine residues in calmodulin

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12 December 2020

X-ray crystallographic analysis of pokeweed antiviral protein-II after reductive methylation of lysine residues

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12 December 2020

Lysine methylation as a routine rescue strategy for protein crystallization

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12 December 2020

Solution NMR spectroscopy beyond 25 kDa.

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12 December 2020

Structure of calmodulin bound to a calcineurin peptide: a new way of making an old binding mode

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Reductive alkylation of amino groups in proteins

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12 December 2020

10.1007/S10858-008-9274-Y

Identifiers

DOI

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https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:18819009%20AND%20SRC:MED&resulttype=core&format=json

release_ejfoclszfrc65b5pmv4dcxaz5e

14 January 2020

Fatcat ID

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