Zobrazeno 1 - 10
of 83
pro vyhledávání: '"Demetrius Tsernoglou"'
Autor:
Demetrius Tsernoglou, Luca Federici, Giulia De Lorenzo, C. Caprari, Juan Fernández-Recio, Felice Cervone, Francesca Sicilia
Publikováno v:
Plant Physiology. 139:1380-1388
Botrytis cinerea is a phytopathogenic fungus that causes gray mold in >1,000 plant species. During infection, it secretes several endopolygalacturonases (PGs) to degrade cell wall pectin, and among them, BcPG1 is constitutively expressed and is an im
Autor:
Kenneth A. Johnson, Francesca M. Pisani, Beatrice Vallone, Carmelinda Savino, Luca Federici, Mosè Rossi, Demetrius Tsernoglou, Vassilios Nastopoulos
Publikováno v:
Structure. 12(11):2001-2008
To minimize the large number of mispairs during genome duplication owing to the large amount of DNA to be synthesized, many replicative polymerases have accessory domains with complementary functions. We describe the crystal structure of replicative
Publikováno v:
Nature Structural Biology. 7:38-43
Ferritin is characterized by a highly conserved architecture that comprises 24 subunits assembled into a spherical cage with 432 symmetry. The only known exception is the dodecameric ferritin from Listeria innocua. The structure of Listeria ferritin
Publikováno v:
Acta Crystallographica Section D Biological Crystallography. 54:964-974
Erabutoxin a has been crystallized in its monomeric and dimeric forms. The structures were refined at 1.50 and 1.49 A resolution, respectively, using synchrotron radiation data. The crystals belong to space group P212121, with cell dimensions a = 49.
Autor:
G van der Goot, Demetrius Tsernoglou, Michael W. Parker, J T Buckley, William J. McKinstry, Jamie Rossjohn, Susanne C. Feil
Publikováno v:
Journal of Structural Biology. 121:92-100
The determination of the crystal structure of the bacterial protein proaerolysin provided the first view of a pore-forming toxin constructed mainly from beta-sheet. The structure that was obtained and subsequent crystallographic and biochemical studi
Publikováno v:
Journal of Molecular Biology. 257:1-8
A second crystal form of the C-terminal domain of the adenovirus single-stranded DNA binding protein crystallizes in space group P2(1)2(1)2(1) with a=61.0 angstrom, b=91.2 angstrom and c=149.4 angstrom. The crystals contain two molecules per asymmetr
Autor:
Demetrius Tsernoglou, H van der Zandt, P.N. Kanellopoulos, P. C. Van Der Vliet, Paul A. Tucker
Publikováno v:
Journal of Structural Biology. 115:113-116
Crystals of the C-terminal domain of the adenovirus single-stranded DNA binding protein (DBP) in complex with the single-stranded oligonucleotide (dT)16 have been obtained by a batch method from material obtained by chymotryptic digest of full-length
Autor:
Kevin Leonard, Demetrius Tsernoglou, Franc Pattus, Alec D. Tucker, J T Buckley, J. P. M. Postma, Michael W. Parker
Publikováno v:
Nature. 367:292-295
Aerolysin is chiefly responsible for the pathogenicity of Aeromonas hydrophila, a bacterium associated with diarrhoeal diseases and deep wound infections. Like many other microbial toxins, the protein changes in a multistep process from a completely
Publikováno v:
Journal of Molecular Biology. 224:639-657
The E1 subgroup (E1, A, B, IA, IB, K and N) of anti-bacterial toxins called colicins is known to form voltage-dependent channels in lipid bilayers. The crystal structure of the pore-forming domain of colicin A from Escherichia coli has been refined t
Autor:
Demetrius Tsernoglou, Alec D. Tucker, Richard A. Pauptit, M.S. Weiss, Arg P. Rosenbusch, Johan N. Jansonius, Georg E. Schulzt, Michael W. Parker, Tilman Schirmer
Publikováno v:
Journal of Structural Biology. 107:136-145
Four new crystal packings of Escherichia coli porins are presented (phosphoporin, maltoporin, and two crystal forms of matrix porin). These were determined by molecular replacement methods using a polyalanine trial model acquired from the refined coo