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Recent publications

Articles

1.   Szeltner Z, Juhász T, Szamosi I, Rea D, Fülöp V, Módos K, Juliano L and Polgár L (2013) [22940581]
  The loops facing the active site of prolyl oligopeptidase are crucial components in substrate gating and specificity.
  Biochim Biophys Acta 1834, 98-111
2.   Kaszuba K, Róg T, Danne R, Canning P, Fülöp V, Juhász T, Szeltner Z, St Pierre JF, García-Horsman A, Männistö PT, Karttunen M, Hokkanen J and Bunker A (2012) [22484394]
  Molecular dynamics, crystallography and mutagenesis studies on the substrate gating mechanism of prolyl oligopeptidase.
  Biochimie 94, 1398-411
3.   Szeltner Z, Morawski M, Juhász T, Szamosi I, Liliom K, Csizmók V, Tölgyesi F and Polgár L (2010) [20869470]
  GAP43 shows partial co-localisation but no strong physical interaction with prolyl oligopeptidase.
  Bba-proteins Proteom 1804, 2162-76
4.   Okamoto DN, Oliveira LC, Kondo MY, Cezari MH, Szeltner Z, Juhász T, Juliano MA, Polgár L, Juliano L and Gouvea IE (2010) [21087086]
  Increase of SARS-CoV 3CL peptidase activity due to macromolecular crowding effects in the milieu composition.
  Biol Chem 391, 1461-8
5.   Kiss AL, Hornung B, Rádi K, Gengeliczki Z, Sztáray B, Juhász T, Szeltner Z, Harmat V and Polgár L (2007) [17350041]
  The acylaminoacyl peptidase from Aeropyrum pernix K1 thought to be an exopeptidase displays endopeptidase activity.
  J Mol Biol 368, 509-20
6.   Juhász T, Szeltner Z and Polgár L (2007) [17623862]
  Truncated prolyl oligopeptidase from Pyrococcus furiosus.
  Proteins 69, 633-43
7.   Gouvea IE, Judice WA, Cezari MH, Juliano MA, Juhász T, Szeltner Z, Polgár L and Juliano L (2006) [17002308]
  Kosmotropic salt activation and substrate specificity of poliovirus protease 3C.
  Biochemistry-us 45, 12083-9
8.   Juhász T, Szeltner Z and Polgár L (2006) [16714022]
  Properties of the prolyl oligopeptidase homologue from Pyrococcus furiosus.
  FEBS Lett 580, 3493-7
9.   Fuxreiter M, Magyar C, Juhász T, Szeltner Z, Polgár L and Simon I (2005) [15971204]
  Flexibility of prolyl oligopeptidase: molecular dynamics and molecular framework analysis of the potential substrate pathways.
  Proteins 60, 504-12
10.   Szeltner Z, Alshafee I, Juhász T, Parvari R and Polgár L (2005) [16143824]
  The PREPL A protein, a new member of the prolyl oligopeptidase family, lacking catalytic activity.
  Cell Mol Life Sci 62, 2376-81
11.   Juhász T, Szeltner Z, Fülöp V and Polgár L (2005) [15713471]
  Unclosed beta-propellers display stable structures: implications for substrate access to the active site of prolyl oligopeptidase.
  J Mol Biol 346, 907-17
12.   Szeltner Z, Rea D, Juhász T, Renner V, Fülöp V and Polgár L (2004) [15210359]
  Concerted structural changes in the peptidase and the propeller domains of prolyl oligopeptidase are required for substrate binding.
  J Mol Biol 340, 627-37
13.   Juhász T, Szeltner Z, Renner V and Polgár L (2002) [11900553]
  Role of the oxyanion binding site and subsites S1 and S2 in the catalysis of oligopeptidase B, a novel target for antimicrobial chemotherapy.
  Biochemistry-us 41, 4096-106
14.   Szeltner Z, Rea D, Juhász T, Renner V, Mucsi Z, Orosz G, Fülöp V and Polgár L (2002) [12228249]
  Substrate-dependent competency of the catalytic triad of prolyl oligopeptidase.
  J Biol Chem 277, 44597-605