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Recent publications

Articles

1.   Menyhárd DK, Kiss-Szemán A, Tichy-Rács E, Hornung B, Rádi K, Szeltner Z, Domokos K, Szamosi I, Náray-Szabó G, Polgár L and Harmat V (2013) [23632025]
  A self-compartmentalizing hexamer serine protease from Pyrococcus horikoshii - substrate selection achieved through multimerization.
  J Biol Chem notSet,
2.   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
3.   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
4.   Harmat V, Domokos K, Menyhárd DK, Palló A, Szeltner Z, Szamosi I, Beke-Somfai T, Náray-Szabó G and Polgár L (2011) [21084296]
  Structure and Catalysis of Acylaminoacyl Peptidase: CLOSED AND OPEN SUBUNITS OF A DIMER OLIGOPEPTIDASE.
  J Biol Chem 286, 1987-98
5.   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
6.   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
7.   Szeltner Z, Kiss AL, Domokos K, Harmat V, Náray-Szabó G and Polgár L (2009) [19303951]
  Characterization of a novel acylaminoacyl peptidase with hexameric structure and endopeptidase activity.
  Bba-proteins Proteom 1794, 1204-10
8.   Szeltner Z and Polgár L (2008) [18336325]
  Structure, function and biological relevance of prolyl oligopeptidase.
  Curr Protein Pept Sc 9, 96-107
9.   Gorrão SS, Hemerly JP, Lima AR, Melo RL, Szeltner Z, Polgár L, Juliano MA and Juliano L (2007) [17904692]
  Fluorescence resonance energy transfer (FRET) peptides and cycloretro-inverso peptides derived from bradykinin as substrates and inhibitors of prolyl oligopeptidase.
  Peptides 28, 2146-54
10.   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
11.   Juhász T, Szeltner Z and Polgár L (2007) [17623862]
  Truncated prolyl oligopeptidase from Pyrococcus furiosus.
  Proteins 69, 633-43
12.   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
13.   Juhász T, Szeltner Z and Polgár L (2006) [16714022]
  Properties of the prolyl oligopeptidase homologue from Pyrococcus furiosus.
  FEBS Lett 580, 3493-7
14.   Wright H, Kiss AL, Szeltner Z, Polgár L and Fülöp V (2005) [-10008742]
  Crystallization and preliminary crystallographic analysis of porcine acylaminoacyl peptidase
  Acta Crystallogr F 61, 942-4
15.   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
16.   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
17.   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
18.   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
19.   Kiss AL, Szeltner Z, Fülöp V and Polgár L (2004) [15280010]
  His507 of acylaminoacyl peptidase stabilizes the active site conformation, not the catalytic intermediate.
  FEBS Lett 571, 17-20
20.   Szeltner Z, Rea D, Renner V, Juliano L, Fülop V and Polgár L (2003) [14514675]
  Electrostatic environment at the active site of prolyl oligopeptidase is highly influential during substrate binding.
  J Biol Chem 278, 48786-93
21.   Szeltner Z, Rea D, Renner V, Fülöp V and Polgár L (2002) [12202494]
  Electrostatic effects and binding determinants in the catalysis of prolyl oligopeptidase. Site specific mutagenesis at the oxyanion binding site.
  J Biol Chem 277, 42613-22
22.   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
23.   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
24.   Fülöp V, Szeltner Z, Renner V and Polgár L (2001) [11031266]
  Structures of prolyl oligopeptidase substrate/inhibitor complexes. Use of inhibitor binding for titration of the catalytic histidine residue.
  J Biol Chem 276, 1262-6
25.   Sárkány Z, Szeltner Z and Polgár L (2001) [11524003]
  Thiolate-imidazolium ion pair is not an obligatory catalytic entity of cysteine peptidases: the active site of picornain 3C.
  Biochemistry-us 40, 10601-6
26.   Fidy J, Laberge M, Ullrich B, Polgár L, Szeltner Z, Gallay J and Vincent M (2001) [-100002668]
  Tryptophan rotamers that report the conformational dynamics of proteins.
  Pure Appl Chem 73, 415-9
27.   Fülöp V, Szeltner Z and Polgár L (2000) [11256612]
  Catalysis of serine oligopeptidases is controlled by a gating filter mechanism.
  EMBO Rep 1, 277-81
28.   Szeltner Z, Renner V and Polgár L (2000) [10716187]
  Substrate- and pH-dependent contribution of oxyanion binding site to the catalysis of prolyl oligopeptidase, a paradigm of the serine oligopeptidase family.
  Protein Sci 9, 353-60
29.   Szeltner Z, Renner V and Polgár L (2000) [10747969]
  The noncatalytic beta-propeller domain of prolyl oligopeptidase enhances the catalytic capability of the peptidase domain.
  J Biol Chem 275, 15000-5
30.   Ullrich B, Laberge M, Tölgyesi F, Szeltner Z, Polgár L and Fidy J (2000) [11152134]
  Trp42 rotamers report reduced flexibility when the inhibitor acetyl-pepstatin is bound to HIV-1 protease.
  Protein Sci 9, 2232-45
31.   Szeltner Z and Polgár L (1996) [8621402]
  Conformational stability and catalytic activity of HIV-1 protease are both enhanced at high salt concentration.
  J Biol Chem 271, 5458-63
32.   Szeltner Z and Polgár L (1996) [8943273]
  Rate-determining steps in HIV-1 protease catalysis. The hydrolysis of the most specific substrate.
  J Biol Chem 271, 32180-4
33.   Polgár L, Szeltner Z and Boros I (1994) [8049236]
  Substrate-dependent mechanisms in the catalysis of human immunodeficiency virus protease.
  Biochemistry-us 33, 9351-7