(Q33756699)

29 July 2017

title

Solution NMR-derived global fold of a monomeric 82-kDa enzyme (English)

1 reference

29 July 2017

4

Lewis E Kay

1 reference

29 July 2017

Vitali Tugarinov

1

1 reference

29 July 2017

Wing-Yiu Choy

series ordinal

2

1 reference

29 July 2017

Vladislav Yu Orekhov

series ordinal

3

1 reference

29 July 2017

language of work or name

English

0 references

publication date

6 January 2005

1 reference

Proceedings of the National Academy of Sciences of the United States of America

29 July 2017

published in

1 reference

29 July 2017

volume

102

1 reference

29 July 2017

issue

3

1 reference

29 July 2017

page(s)

622-627

1 reference

NMR View: A computer program for the visualization and analysis of NMR data

29 July 2017

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Molecular basis for synergistic transcriptional activation by Oct1 and Sox2 revealed from the solution structure of the 42-kDa Oct1.Sox2.Hoxb1-DNA ternary transcription factor complex

21 June 2018

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Structure of theEscherichia colimalate synthase G:pyruvate:acetyl-coenzyme A abortive ternary complex at 1.95 Å resolution

21 June 2018

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21 June 2018

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Transverse relaxation-optimized NMR spectroscopy with the outer membrane protein OmpX in dihexanoyl phosphatidylcholine micelles

21 June 2018

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Global folds of proteins with low densities of NOEs using residual dipolar couplings: application to the 370-residue maltodextrin-binding protein

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21 June 2018

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21 June 2018

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21 June 2018

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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

21 June 2018

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21 June 2018

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Solution structure of an rRNA methyltransferase (ErmAM) that confers macrolide-lincosamide-streptogramin antibiotic resistance

21 June 2018

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21 June 2018

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21 June 2018

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21 June 2018

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21 June 2018

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21 June 2018

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21 June 2018

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21 June 2018

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Post-irradiation inactivation, protection, and repair of the sulfhydryl enzyme malate synthase. Effects of formate, superoxide dismutase, catalase, and dithiothreitol.

21 June 2018

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21 June 2018

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Stereospecific nuclear magnetic resonance assignments of the methyl groups of valine and leucine in the DNA-binding domain of the 434 repressor by biosynthetically directed fractional 13C labeling

21 June 2018

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21 June 2018

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Four-dimensional NMR spectroscopy of a 723-residue protein: chemical shift assignments and secondary structure of malate synthase g.

21 January 2018

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Ile, Leu, and Val Methyl Assignments of the 723-Residue Malate Synthase G Using a New Labeling Strategy and Novel NMR Methods

21 January 2018

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Quantitative NMR studies of high molecular weight proteins: application to domain orientation and ligand binding in the 723 residue enzyme malate synthase G.

21 January 2018

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Stereospecific NMR assignments of prochiral methyls, rotameric states and dynamics of valine residues in malate synthase G.

21 January 2018

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An isotope labeling strategy for methyl TROSY spectroscopy

21 January 2018

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21 January 2018

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A robust and cost-effective method for the production of Val, Leu, Ile (delta 1) methyl-protonated 15N-, 13C-, 2H-labeled proteins

21 January 2018

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Relaxation-optimized NMR spectroscopy of methylene groups in proteins and nucleic acids

21 January 2018

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PubMed

https://pubmed.ncbi.nlm.nih.gov/15637152

inferred from PubMed ID database lookup

12 December 2020

based on heuristic

Identifiers

DOI

10.1073/PNAS.0407792102

1 reference

29 July 2017

0 references

1 reference

29 July 2017

1 reference