Search Results - (Author, Cooperation:R. Dijkman)
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1V. S. Raj ; H. Mou ; S. L. Smits ; D. H. Dekkers ; M. A. Muller ; R. Dijkman ; D. Muth ; J. A. Demmers ; A. Zaki ; R. A. Fouchier ; V. Thiel ; C. Drosten ; P. J. Rottier ; A. D. Osterhaus ; B. J. Bosch ; B. L. Haagmans
Nature Publishing Group (NPG)
Published 2013Staff ViewPublication Date: 2013-03-15Publisher: Nature Publishing Group (NPG)Print ISSN: 0028-0836Electronic ISSN: 1476-4687Topics: BiologyChemistry and PharmacologyMedicineNatural Sciences in GeneralPhysicsKeywords: Animals ; Bronchioles/cytology ; COS Cells ; Cercopithecus aethiops ; Chiroptera ; Coronavirus/*classification/*metabolism ; Coronavirus Infections/epidemiology/genetics/metabolism/virology ; Dipeptidyl Peptidase 4/genetics/*metabolism ; Epithelial Cells/virology ; Host Specificity ; Humans ; Molecular Sequence Data ; Receptors, Virus/genetics/*metabolismPublished by: -
2Mazel-Sanchez, B., Boal-Carvalho, I., Silva, F., Dijkman, R., Schmolke, M.
The American Society for Microbiology (ASM)
Published 2018Staff ViewPublication Date: 2018-05-15Publisher: The American Society for Microbiology (ASM)Print ISSN: 0022-538XElectronic ISSN: 1098-5514Topics: MedicinePublished by: -
3Gonzales, M.L. ; Basu, A. ; de Haas, G.H. ; Dijkman, R. ; van Oort, M.G. ; Okolo, A.A. ; Glew, R.H.
Amsterdam : ElsevierStaff ViewISSN: 0003-9861Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002Topics: BiologyChemistry and PharmacologyPhysicsType of Medium: Electronic ResourceURL: -
4Staff View
ISSN: 0005-2760Keywords: Lipolytic enzyme ; Phosphatidylcholine ; PhospholipidSource: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002Topics: BiologyChemistry and PharmacologyMedicinePhysicsType of Medium: Electronic ResourceURL: -
5de Haas, G.H. ; Dijkman, R. ; Lugtigheid, R.B. ; Dekker, N. ; Van Den Berg, L. ; Egmond, M.R. ; Verheij, H.M.
Amsterdam : ElsevierStaff ViewISSN: 0005-2760Keywords: 2-Acylamino phospholipid ; Competitive inhibition ; Lipolysis ; Pancreatic phospholipase A"2 ; Phospholipase A"2 ; Ultraviolet difference absorption spectroscopySource: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002Topics: BiologyChemistry and PharmacologyMedicinePhysicsType of Medium: Electronic ResourceURL: -
6Staff View
ISSN: 0005-2760Keywords: (Human) ; Competitive inhibition ; Pancreatic phospholipase A"2 ; Platelet phospholipase A"2Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002Topics: BiologyChemistry and PharmacologyMedicinePhysicsType of Medium: Electronic ResourceURL: -
7Deveer, A.M.T.J. ; Franken, P.A. ; Dijkman, R. ; Meeldijk, J. ; Egmond, M.R. ; Verheij, H.M. ; Verger, R. ; De Haas, G.H.
Amsterdam : ElsevierStaff ViewISSN: 0005-2760Keywords: 2-Acylamino-phospholipid ; Competitive inhibition ; Pancreatic phospholipase A"2 ; Ultraviolet difference absorption spectroscopySource: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002Topics: BiologyChemistry and PharmacologyMedicinePhysicsType of Medium: Electronic ResourceURL: -
8Jain, M.K. ; Egmond, M.R. ; Verheij, H.M. ; Apitz-Castro, R. ; Dijkman, R. ; De Haas, G.H.
Amsterdam : ElsevierStaff ViewISSN: 0005-2736Keywords: Phospholipase A"2 ; Phospholipid bilayer ; Protein-membrane interactionSource: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002Topics: BiologyChemistry and PharmacologyMedicinePhysicsType of Medium: Electronic ResourceURL: -
9Staff View
ISSN: 0005-2760Keywords: (Porcine pancreas) ; Acylamino analog ; Inhibition ; Lipolytic enzyme ; Phospholipase A"2Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002Topics: BiologyChemistry and PharmacologyMedicinePhysicsType of Medium: Electronic ResourceURL: -
10Staff View
ISSN: 0005-2760Keywords: Competitive inhibition ; Enzyme inhibition ; Phospholipase A"2 ; Substrate-derived inhibitorSource: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002Topics: BiologyChemistry and PharmacologyMedicinePhysicsType of Medium: Electronic ResourceURL: -
11Staff View
ISSN: 0005-2760Keywords: 2-Acylamino phospholipid ; Competitive inhibition ; Lipolysis ; Pancreatic phospholipase A"2Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002Topics: BiologyChemistry and PharmacologyMedicinePhysicsType of Medium: Electronic ResourceURL: -
12Staff View
ISSN: 0009-3084Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002Topics: BiologyChemistry and PharmacologyPhysicsType of Medium: Electronic ResourceURL: -
13Staff View
ISSN: 0022-2836Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002Topics: BiologyType of Medium: Electronic ResourceURL: -
14Berg, B. ; Tessari, M. ; Boelens, R. ; Dijkman, R. ; Kaptein, R. ; Haas, G. H. ; Verheij, H. M.
Springer
Published 1995Staff ViewISSN: 1573-5001Keywords: Phospholipase A2 ; Interfacial activation ; Ternary complex ; NMR structureSource: Springer Online Journal Archives 1860-2000Topics: BiologyChemistry and PharmacologyNotes: Summary The three-dimensional structure of porcine pancreatic PLA2 (PLA2), present in a 40 kDa ternary complex with micelles and a competitive inhibitor, has been determined using multidimensional heteronuclear NMR spectroscopy. The structure of the protein (124 residues) is based on 1854 constraints, comprising 1792 distance and 62 ϕ torsion angle constraints. A total of 18 structures was calculated using a combined approach of distance geometry and restrained molecular dynamics. The atomic rms distribution about the mean coordinate positions for residues 1–62 and 72–124 is 0.75±0.09 Å for the backbone atoms and 1.14±0.10 Å for all atoms. The rms difference between the averaged minimized NMR structures of the free PLA2 and PLA2 in the ternary complex is 3.5 Å for the backbone atoms and 4.0 Å for all atoms. Large differences occur for the calcium-binding loop and the surface loop from residues 62 through 72. The most important difference is found for the first three residues of the N-terminal α-helix. Whereas free in solution Ala1, Leu2 and Trp3 are disordered, with the α-amino group of Ala1 pointing out into the solvent, in the ternary complex these residues have an α-helical conformation with the α-amino group buried inside the protein. As a consequence, the important conserved hydrogen bonding network which is also seen in the crystal structures is present only in the ternary complex, but not in free PLA2. Thus, the NMR structure of the N-terminal region (as well as the calcium-binding loop and the surface loop) of PLA2 in the ternary complex resembles that of the crystal structure. Comparison of the NMR structures of the free enzyme and the enzyme in the ternary complex indicates that conformational changes play a role in the interfacial activation of PLA2.Type of Medium: Electronic ResourceURL: