L Polgar

Summary

Affiliation: Hungarian Academy of Sciences
Country: Hungary

Publications

  1. ncbi The catalytic triad of serine peptidases
    L Polgar
    Institute of Enzymology, Biological Research Center, Hungarian Academy of Sciences, P O Box 7, 1518, Budapest 112, Hungary
    Cell Mol Life Sci 62:2161-72. 2005
  2. ncbi A potential processing enzyme in prokaryotes: oligopeptidase B, a new type of serine peptidase
    L Polgar
    Institute of Enzymology, Hungarian Academy of Sciences, Budapest
    Proteins 28:375-9. 1997
  3. ncbi Oligopeptidase B: cloning and probing stability under nonequilibrium conditions
    L Polgar
    Institute of Enzymology, Biological Research Center, Hungarian Academy of Sciences, Budapest
    Proteins 30:424-34. 1998
  4. ncbi Thiolate-imidazolium ion pair is not an obligatory catalytic entity of cysteine peptidases: the active site of picornain 3C
    Z Sárkány
    Institute of Enzymology, Biological Research Center, Hungarian Academy of Sciences, P O Box 7, H 1518 Budapest, Hungary
    Biochemistry 40:10601-6. 2001
  5. ncbi Oligopeptidase B: a new type of serine peptidase with a unique substrate-dependent temperature sensitivity
    L Polgar
    Institute of Enzymology, Biological Research Center, Hungarian Academy of Sciences, Budapest
    Biochemistry 38:15548-55. 1999
  6. ncbi The PREPL A protein, a new member of the prolyl oligopeptidase family, lacking catalytic activity
    Z Szeltner
    Institute of Enzymology, Biological Research Center, Hungarian Academy of Sciences, 1518, Budapest 112, P O Box 7, Hungary
    Cell Mol Life Sci 62:2376-81. 2005
  7. ncbi The prolyl oligopeptidase family
    L Polgar
    Institute of Enzymology, Hungarian Academy of Sciences, Budapest
    Cell Mol Life Sci 59:349-62. 2002

Collaborators

  • Z Szeltner
  • Z Sárkány
  • T Juhasz
  • R Parvari
  • I Alshafee

Detail Information

Publications7

  1. ncbi The catalytic triad of serine peptidases
    L Polgar
    Institute of Enzymology, Biological Research Center, Hungarian Academy of Sciences, P O Box 7, 1518, Budapest 112, Hungary
    Cell Mol Life Sci 62:2161-72. 2005
    ..The variations illustrate how different groups and different protein structures achieve the same reaction...
  2. ncbi A potential processing enzyme in prokaryotes: oligopeptidase B, a new type of serine peptidase
    L Polgar
    Institute of Enzymology, Hungarian Academy of Sciences, Budapest
    Proteins 28:375-9. 1997
    ..The present result will contribute to our understanding of the processing phenomena in prokaryotes, as well as in higher organisms...
  3. ncbi Oligopeptidase B: cloning and probing stability under nonequilibrium conditions
    L Polgar
    Institute of Enzymology, Biological Research Center, Hungarian Academy of Sciences, Budapest
    Proteins 30:424-34. 1998
    ..The results indicate that under harsher denaturing conditions there is a single rate-limiting step in unfolding, whereas under milder conditions partly unfolded intermediates are populated...
  4. ncbi Thiolate-imidazolium ion pair is not an obligatory catalytic entity of cysteine peptidases: the active site of picornain 3C
    Z Sárkány
    Institute of Enzymology, Biological Research Center, Hungarian Academy of Sciences, P O Box 7, H 1518 Budapest, Hungary
    Biochemistry 40:10601-6. 2001
    ..The inverse effects is associated with the stabilization of the protein structure in heavy water...
  5. ncbi Oligopeptidase B: a new type of serine peptidase with a unique substrate-dependent temperature sensitivity
    L Polgar
    Institute of Enzymology, Biological Research Center, Hungarian Academy of Sciences, Budapest
    Biochemistry 38:15548-55. 1999
    ..The positive entropies of activation point to substantial reorganization of water molecules upon substrate binding...
  6. ncbi The PREPL A protein, a new member of the prolyl oligopeptidase family, lacking catalytic activity
    Z Szeltner
    Institute of Enzymology, Biological Research Center, Hungarian Academy of Sciences, 1518, Budapest 112, P O Box 7, Hungary
    Cell Mol Life Sci 62:2376-81. 2005
    ..These results indicated that the catalytic serine is a reactive residue. However, the negligible hydrolytic activity suggests that the function of PREPL A is different from that of the other members of the prolyl oligopeptidase family...
  7. ncbi The prolyl oligopeptidase family
    L Polgar
    Institute of Enzymology, Hungarian Academy of Sciences, Budapest
    Cell Mol Life Sci 59:349-62. 2002
    ..The members of the family are important targets of drug design. Prolyl oligopeptidase is involved in amnesia, depression and blood pressure control, dipeptidyl peptidase IV in type 2 diabetes and oligopeptidase B in trypanosomiasis...