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Improved isotopic profiling by pure shift heteronuclear 2D J-resolved NMR spectroscopy
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- Journal Article
- A1
- open access
Structure and antagonism of the receptor complex mediated by human TSLP in allergy and asthma
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- Journal Article
- A1
- open access
Tau phosphorylation regulates the interaction between BIN1's SH3 domain and Tau's proline-rich domain
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Intermolecular interaction studies using small volumes
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- Journal Article
- A1
- open access
Arabidopsis PASTICCINO2 is an antiphosphatase involved in regulation of cyclin-dependent kinase A
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Characterization of the Arabidopsis thaliana Arath;CDC25 dual-specificity tyrosine phosphatase
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A small CDC25 dual-specificity tyrosine-phosphatase isoform in Arabidopsis thaliana
(2004) PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA. 101(36). p.13380-13385 -
Solution structure of the single-domain prolyl cis/trans isomerase PIN1At from Arabidopsis thaliana
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Letter to the editor: Assignment of the 1H, 13C and 15N resonances and secondary structure of the monomeric p13suc1 protein of Saccharomyces pombe
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Solution NMR study of the monomeric form of p13suc1 protein sheds light on the hinge region determining the affinity for a phosphorylated substrate
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p13SUC1 and the WW domain of PIN1 bind to the same phosphothreonine-proline epitope
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Sequence-specific 1H, 13C and 15N chemical shift backbone NMR assignment and secondary structure of the Arabidopsis thaliana PIN1At protein
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The Arabidopsis thaliana PIN1At gene encodes a single-domain phosphorylation-dependent peptidyl prolyl cis/trans isomerase
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Recombinant production of the p10CKS1At protein from Arabidopsis thaliana and 13C and 15N double-isotopic enrichment for NMR studies
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T-1 RELAXATION-TIME OF WATER FROM A MOLECULAR-DYNAMICS SIMULATION.
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TRANSFER NUCLEAR OVERHAUSER EFFECT STUDY OF THE CONFORMATION OF OXYTOCIN BOUND TO BOVINE NEUROPHYSIN-I.
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Transfer NOE study of oxytocin bound to neurophysin
(1992) -
De CAM-methode : een analyse- en keuzemodel ter ondersteuning van investeringsbeslissingen in de landbouw