Search Results - (Author, Cooperation:R. Geurts)
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1V. S. Merckx ; K. P. Hendriks ; K. K. Beentjes ; C. B. Mennes ; L. E. Becking ; K. T. Peijnenburg ; A. Afendy ; N. Arumugam ; H. de Boer ; A. Biun ; M. M. Buang ; P. P. Chen ; A. Y. Chung ; R. Dow ; F. A. Feijen ; H. Feijen ; C. Feijen-van Soest ; J. Geml ; R. Geurts ; B. Gravendeel ; P. Hovenkamp ; P. Imbun ; I. Ipor ; S. B. Janssens ; M. Jocque ; H. Kappes ; E. Khoo ; P. Koomen ; F. Lens ; R. J. Majapun ; L. N. Morgado ; S. Neupane ; N. Nieser ; J. T. Pereira ; H. Rahman ; S. Sabran ; A. Sawang ; R. M. Schwallier ; P. S. Shim ; H. Smit ; N. Sol ; M. Spait ; M. Stech ; F. Stokvis ; J. B. Sugau ; M. Suleiman ; S. Sumail ; D. C. Thomas ; J. van Tol ; F. Y. Tuh ; B. E. Yahya ; J. Nais ; R. Repin ; M. Lakim ; M. Schilthuizen
Nature Publishing Group (NPG)
Published 2015Staff ViewPublication Date: 2015-08-13Publisher: Nature Publishing Group (NPG)Print ISSN: 0028-0836Electronic ISSN: 1476-4687Topics: BiologyChemistry and PharmacologyMedicineNatural Sciences in GeneralPhysicsKeywords: *Altitude ; Animal Migration ; Animals ; *Biota ; Climate Change ; DNA Barcoding, Taxonomic ; Extinction, Biological ; Introduced Species/*statistics & numerical data ; Malaysia ; Molecular Sequence Data ; *Phylogeny ; *Phylogeography ; Plants/classification/genetics ; Time Factors ; *Tropical ClimatePublished by: -
2R. Op den Camp ; A. Streng ; S. De Mita ; Q. Cao ; E. Polone ; W. Liu ; J. S. Ammiraju ; D. Kudrna ; R. Wing ; A. Untergasser ; T. Bisseling ; R. Geurts
American Association for the Advancement of Science (AAAS)
Published 2011Staff ViewPublication Date: 2011-01-06Publisher: American Association for the Advancement of Science (AAAS)Print ISSN: 0036-8075Electronic ISSN: 1095-9203Topics: BiologyChemistry and PharmacologyComputer ScienceMedicineNatural Sciences in GeneralPhysicsKeywords: Amino Acid Sequence ; Calcium-Calmodulin-Dependent Protein Kinases/metabolism ; Cloning, Molecular ; Evolution, Molecular ; Gene Duplication ; Genes, Plant ; Glomeromycota/physiology ; Lipopolysaccharides/*metabolism ; Molecular Sequence Data ; Mycorrhizae/*physiology ; Nitrogen Fixation ; Phylogeny ; Plant Proteins/genetics/*metabolism ; Plant Root Nodulation ; Protein Kinases/genetics/*metabolism ; RNA Interference ; Root Nodules, Plant/microbiology/physiology ; Signal Transduction ; Sinorhizobium/*physiology ; *Symbiosis ; Ulmaceae/genetics/*microbiology/*physiologyPublished by: -
3N. D. Young ; F. Debelle ; G. E. Oldroyd ; R. Geurts ; S. B. Cannon ; M. K. Udvardi ; V. A. Benedito ; K. F. Mayer ; J. Gouzy ; H. Schoof ; Y. Van de Peer ; S. Proost ; D. R. Cook ; B. C. Meyers ; M. Spannagl ; F. Cheung ; S. De Mita ; V. Krishnakumar ; H. Gundlach ; S. Zhou ; J. Mudge ; A. K. Bharti ; J. D. Murray ; M. A. Naoumkina ; B. Rosen ; K. A. Silverstein ; H. Tang ; S. Rombauts ; P. X. Zhao ; P. Zhou ; V. Barbe ; P. Bardou ; M. Bechner ; A. Bellec ; A. Berger ; H. Berges ; S. Bidwell ; T. Bisseling ; N. Choisne ; A. Couloux ; R. Denny ; S. Deshpande ; X. Dai ; J. J. Doyle ; A. M. Dudez ; A. D. Farmer ; S. Fouteau ; C. Franken ; C. Gibelin ; J. Gish ; S. Goldstein ; A. J. Gonzalez ; P. J. Green ; A. Hallab ; M. Hartog ; A. Hua ; S. J. Humphray ; D. H. Jeong ; Y. Jing ; A. Jocker ; S. M. Kenton ; D. J. Kim ; K. Klee ; H. Lai ; C. Lang ; S. Lin ; S. L. Macmil ; G. Magdelenat ; L. Matthews ; J. McCorrison ; E. L. Monaghan ; J. H. Mun ; F. Z. Najar ; C. Nicholson ; C. Noirot ; M. O'Bleness ; C. R. Paule ; J. Poulain ; F. Prion ; B. Qin ; C. Qu ; E. F. Retzel ; C. Riddle ; E. Sallet ; S. Samain ; N. Samson ; I. Sanders ; O. Saurat ; C. Scarpelli ; T. Schiex ; B. Segurens ; A. J. Severin ; D. J. Sherrier ; R. Shi ; S. Sims ; S. R. Singer ; S. Sinharoy ; L. Sterck ; A. Viollet ; B. B. Wang ; K. Wang ; M. Wang ; X. Wang ; J. Warfsmann ; J. Weissenbach ; D. D. White ; J. D. White ; G. B. Wiley ; P. Wincker ; Y. Xing ; L. Yang ; Z. Yao ; F. Ying ; J. Zhai ; L. Zhou ; A. Zuber ; J. Denarie ; R. A. Dixon ; G. D. May ; D. C. Schwartz ; J. Rogers ; F. Quetier ; C. D. Town ; B. A. Roe
Nature Publishing Group (NPG)
Published 2011Staff ViewPublication Date: 2011-11-18Publisher: Nature Publishing Group (NPG)Print ISSN: 0028-0836Electronic ISSN: 1476-4687Topics: BiologyChemistry and PharmacologyMedicineNatural Sciences in GeneralPhysicsKeywords: *Biological Evolution ; *Genome, Plant ; Medicago truncatula/*genetics/*microbiology ; Molecular Sequence Data ; Nitrogen Fixation/genetics ; Rhizobium/*physiology ; Soybeans/genetics ; *Symbiosis ; Synteny ; Vitis/geneticsPublished by: -
4Staff View
ISSN: 0021-8995Keywords: Chemistry ; Polymer and Materials ScienceSource: Wiley InterScience Backfile Collection 1832-2000Topics: Chemistry and PharmacologyMechanical Engineering, Materials Science, Production Engineering, Mining and Metallurgy, Traffic Engineering, Precision MechanicsPhysicsNotes: Graft polymerizations of methyl methacrylate onto natural, reduced, S-carboxymethylated, S-aminoethylated, sulfated, acetylated, and oxidized wools were performed at 30°C using a LiBr-K2S2O8 redox system as initiator. The extent of grafting was found to be dependent on the thiol and amino contents of wool fibers; carboxylic, sulfated groups, and oxidation intermediates had no significative influence on graft yields. The polymethacrylic chains obtained after hydrolysis of the natural part of the copolymer and analyzed by infrared and NMR spectroscopies were characterized by an atactic structure quite comparable to that found for a corresponding homopolymer. There was no stereoregulating effect on methyl methacrylate polymerization due to the crystalline components of the wool structure. A quantitative determination of the number of amino acid residues linked to the end of polymethacrylic chains after hydrolysis indicated that chain termination occurs both by disproportionation and recombination of macroradicals for natural, sulfated, S-carboxymethylated, and S-aminoethylated wools; for reduced and oxidized wools, only a recombination by disproportionation was observed in accordance with the open structure of these wool fibers. The chain lengths of the isolated poly(methyl methacrylates) were also found to be consistent with the participation of thiol and amino groups in grafting. It seems, however, that amino groups do not themselves act as initiating sites.Additional Material: 6 Ill.Type of Medium: Electronic ResourceURL: