Výsledky vyhledávání - "G. T. Robillard"

The thermal stability and domain interactions of the mannitol permease of Escherichia coli. A differential scanning calorimetry study

Autor: W, Meijberg, G K, Schuurman-Wolters, H, Boer, R M, Scheek, G T, Robillard

Publikováno v: The Journal of biological chemistry. 273(33)

The thermal stability and domain interactions in the mannitol transporter from Escherichia coli, enzyme IImtl, have been studied by differential scanning calorimetry. To this end, the wild type enzyme, IICBAmtl, as well as IICBmtl and IICmtl, were re

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::d52e27f6cbedf0e30f071e91ebc691ea
https://pubmed.ncbi.nlm.nih.gov/9694823

Zobrazit plný text záznamu

Structure characterization of the central repetitive domain of high molecular weight gluten proteins. I. Model studies using cyclic and linear peptides

Autor: A A, Van Dijk, L L, Van Wijk, A, Van Vliet, P, Haris, E, Van Swieten, G I, Tesser, G T, Robillard

Publikováno v: Protein science : a publication of the Protein Society. 6(3)

The high molecular weight (HMW) proteins from wheat contain a repetitive domain that forms 60-80% of their sequence. The consensus peptides PGQGQQ and GYYPTSPQQ form more than 90% of the domain; both are predicted to adopt beta-turn structure. This p

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::e6545c6df8b022b9fd1794459f927449
https://pubmed.ncbi.nlm.nih.gov/9070446

Zobrazit plný text záznamu

Phosphorylation-induced torsion-angle strain in the active center of HPr, detected by NMR and restrained molecular dynamics refinement

Autor: N A, Van Nuland, J A, Wiersma, D, Van Der Spoel, B L, De Groot, R M, Scheek, G T, Robillard

Publikováno v: Protein science : a publication of the Protein Society. 5(3)

The structure of the phosphorylated form of the histidine-containing phosphocarrier protein HPr from Escherichia coli has been solved by NMR and compared with that of unphosphorylated HPr. The structural changes that occur upon phosphorylation of His

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::ebe5bba81478b798b47168301a4dd4d9
https://pubmed.ncbi.nlm.nih.gov/8868480

Zobrazit plný text záznamu

Expression, purification, and kinetic characterization of the mannitol transport domain of the phosphoenolpyruvate-dependent mannitol phosphotransferase system of Escherichia coli. Kinetic evidence that the E. coli mannitol transport protein is a functional dimer

Autor: H, Boer, R H, ten Hoeve-Duurkens, G K, Schuurman-Wolters, A, Dijkstra, G T, Robillard

Publikováno v: The Journal of biological chemistry. 269(27)

The overexpression of the membrane-bound C domain of the mannitol transport protein EIIMtl of Escherichia coli has been achieved. This protein, IICMtl, consisting of the first 346 amino acids, was purified from membrane vesicles and still bound manni

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::cc4a5e84c2afe9a9167da87e4dc2e136
https://pubmed.ncbi.nlm.nih.gov/8027040

Zobrazit plný text záznamu

Steady state kinetics of mannitol phosphorylation catalyzed by enzyme IImtl of the Escherichia coli phosphoenolpyruvate-dependent phosphotransferase system

Autor: J S, Lolkema, R H, ten Hoeve-Duurkens, G T, Robillard

Publikováno v: The Journal of biological chemistry. 268(24)

The kinetics of mannitol phosphorylation catalyzed by enzyme IImtl of the bacterial P-enolpyruvate-dependent phosphotransferase system are described for three different physical conditions of the enzyme, (i) embedded in the membrane of inside-out (IS

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::bfb4cec85934880366bad4af83ec8406
https://pubmed.ncbi.nlm.nih.gov/8349668

Zobrazit plný text záznamu

31phospho-NMR demonstration of phosphocysteine as a catalytic intermediate on the Escherichia coli phosphotransferase system EIIMtl

Autor: H H, Pas, G H, Meyer, W H, Kruizinga, K S, Tamminga, R P, van Weeghel, G T, Robillard

Publikováno v: The Journal of biological chemistry. 266(11)

The mannitol-specific phosphotransferase system transport protein, Enzyme IIMtl, contains two catalytically important phosphorylated amino acid residues, both present on the cytoplasmic part of the enzyme. Recently, this portion has been subcloned, p

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::dbdc7623218eccb02a323e342b924f5c
https://pubmed.ncbi.nlm.nih.gov/2016284

Zobrazit plný text záznamu

NMR spectroscopy analysis of phosphorus metabolites and the effect of adriamycin on these metabolite levels in an adriamycin-sensitive and -resistant human small cell lung carcinoma cell line

Autor: G T Robillard, Nanno Mulder, de Elisabeth G. E. Vries, de Steven Jong

Publikováno v: British Journal of Cancer

31P nuclear magnetic resonance (NMR) spectra of cells and of cell extract revealed high levels of phosphorylcholine (PC) and phosphocreatine (PCr) in an adriamycin-resistant human small cell lung carcinoma cell line (GLC4/ADR) and the adriamycin-sens

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c2caa0397b821112eea8c4bccf13cf1a
https://pubmed.ncbi.nlm.nih.gov/1847646

Zobrazit plný text záznamu

Partial purification of the 5-hydroxytryptamine-reuptake system from human blood platelets using a citalopram-derived affinity resin [corrected]

Autor: E A, Biessen, A S, Horn, G T, Robillard

Publikováno v: Biochemistry. 29(13)

This paper describes a procedure for the synthesis and application of a citalopram-derived affinity resin in purifying the 5HT-reuptake system from human blood platelets. A two-step scheme has been developed for partial purification, based on wheat g

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::2d7e7ff50b85b2065479061799ddc138
https://pubmed.ncbi.nlm.nih.gov/2334696

Zobrazit plný text záznamu

Vyhledávací nástroje:

Upřesnit hledání