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1N. 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: -
2Lin, S.-Y. ; Wang, X.-M. ; Wang, Y.-P. ; Ying, F. ; Zhang, D.-L. ; Duan, H.M. ; Hermann, A.M.
Amsterdam : ElsevierStaff ViewISSN: 0921-4534Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002Topics: PhysicsType of Medium: Electronic ResourceURL: -
3Staff View
ISSN: 0038-1098Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002Topics: PhysicsType of Medium: Electronic ResourceURL: -
4Wei, L. ; Hongiuan, Y. ; Zhiyi, Y. ; Suying, Z. ; Ying, F. ; Wenlan, X. ; Xuechu, S.
Amsterdam : ElsevierStaff ViewISSN: 0038-1098Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002Topics: PhysicsType of Medium: Electronic ResourceURL: -
5Staff View
ISSN: 0040-4039Keywords: Allenyl Ether ; Furans ; Intramolecular Diels-Alder Reaction ; Methylthio Group 1,4-RearrangementSource: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002Topics: Chemistry and PharmacologyType of Medium: Electronic ResourceURL: -
6Huang, Chi-Ying F. ; Yuan, Chiun-Jye ; Livanova, Nataliya B. ; Graves, Donald J.
Springer
Published 1993Staff ViewISSN: 1573-4919Keywords: phosphorylase kinase γ subunit ; inhibitory domainSource: Springer Online Journal Archives 1860-2000Topics: BiologyChemistry and PharmacologyMedicineNotes: Abstract A catalytic fragment,γ 1-298, derived from limited chymotryptic digestion of phosphorylaseb kinase (Harris, W.R.et al., J. Biol. Chem., 265: 11740–11745, 1990), is reported to have about six-fold greater specific activity than does the γ subunit-calmodulin complex. To test whether there is an inhibitory domain located outside the catalytic core of the γ subunit, full-length wild-type and seven truncated forms of γ were expressed inE. coli. Recombinant proteins accumulate in the inclusion bodies and can be isolated, solubilized, renatured, and purified further by ammonium sulfate precipitation and Q-Sepharose column. Four out of seven truncated mutants show similar (γ 1-353 andγ 1-341) or less (γ 1-331 andγ 1-276) specific activity than does the full-length wild-type γ,γ 1-386. Three truncated forms,γ 1-316,γ 1-300, andγ 1-290 have molar specific activities approximately twice as great as those of the full-length wild-type γ and the nonactivated holoenzyme. All recombinant γs exhibit similarK m values for both substrates, i.e., about 18μM for phosphorylaseb and about 75 μM for MgATP. Three truncated γs,γ 1-316,γ 1-300, andγ 1-290, have a 1.9- to 2.5-fold greater catalytic efficiency (V max/K m) than that of the full-length wild-type γ and a 3.5- to 4.5-fold greater efficiency than that of the truncatedγ 1-331. This evidence suggests that there is at least one inhibitory domain in the C-terminal region of γ, which is located atγ 301-331·γ 1-290, but notγ 1-276, which contains the highly conserved kinase domain, is the minimum sequence required for the γ subunit to exhibit phosphotransferase activity. Bothγ 1-290 andγ 1-300 have several properties similar to full-length wild-type γ, including metal ion responses (activation by free Mg2+ and inhibition by free Mn2+) pH dependency, and substrate specificities.Type of Medium: Electronic ResourceURL: