B Lenarcic

Summary

Affiliation: Jozef Stefan Institute
Country: Slovenia

Publications

  1. ncbi request reprint Saxiphilin, a saxitoxin-binding protein with two thyroglobulin type 1 domains, is an inhibitor of papain-like cysteine proteinases
    B Lenarcic
    Departments of Biochemistry and Molecular Biology, J Stefan Institute, Jamova 39, 1000 Ljubljana, Slovenia
    J Biol Chem 275:15572-7. 2000
  2. ncbi request reprint Thyroglobulin type-1 domains in equistatin inhibit both papain-like cysteine proteinases and cathepsin D
    B Lenarcic
    Department of Biochemistry and Molecular Biology, J Stefan Institute, Jamova 39, 1000 Ljubljana, Slovenia
    J Biol Chem 274:563-6. 1999
  3. ncbi request reprint Equistatin, a new inhibitor of cysteine proteinases from Actinia equina, is structurally related to thyroglobulin type-1 domain
    B Lenarcic
    Department of Biochemistry and Molecular Biology, Jozef Stefan Institute, Jamova 39, 1000 Ljubljana, Slovenia
    J Biol Chem 272:13899-903. 1997
  4. ncbi request reprint Differences in specificity for the interactions of stefins A, B and D with cysteine proteinases
    B Lenarcic
    Department of Biochemistry and Molecular Biology, J Stefan Institute, Ljubljana, Slovenia
    FEBS Lett 395:113-8. 1996
  5. ncbi request reprint Molecular cloning of a putative homolog of proline/arginine-rich antibacterial peptides from porcine bone marrow
    J Pungercar
    Department of Biochemistry and Molecular Biology, Jozef Stefan Institute, Ljubljana, Slovenia
    FEBS Lett 336:284-8. 1993
  6. ncbi request reprint Acidic pH as a physiological regulator of human cathepsin L activity
    B Turk
    Department of Biochemistry and Molecular Biology, J Stefan Institute, Ljubljana, Slovenia
    Eur J Biochem 259:926-32. 1999
  7. ncbi request reprint Cathepsin D inactivates cysteine proteinase inhibitors, cystatins
    B Lenarcic
    Department of Biochemistry, J Stefan Institute, Ljubljana, Yugoslavia
    Biochem Biophys Res Commun 154:765-72. 1988
  8. ncbi request reprint Equistatin, a protease inhibitor from the sea anemone actinia equina, is composed of three structural and functional domains
    B Strukelj
    Department of Biochemistry and Molecular Biology, Jozef Stefan Institute, Jamova 39, Ljubljana, SI 1000, Slovenia
    Biochem Biophys Res Commun 269:732-6. 2000
  9. ncbi request reprint The cysteine protease activity of Colorado potato beetle (Leptinotarsa decemlineata Say) guts, which is insensitive to potato protease inhibitors, is inhibited by thyroglobulin type-1 domain inhibitors
    K Gruden
    Department of Biochemistry and Molecular Biology, Jozef Stefan Institute, Ljubljana, Slovenia
    Insect Biochem Mol Biol 28:549-60. 1998
  10. ncbi request reprint Inactivation of human cystatin C and kininogen by human cathepsin D
    B Lenarcic
    Department of Biochemistry, Jozef Stefan Institute, Slovenia, Yugoslavia
    FEBS Lett 280:211-5. 1991

Collaborators

Detail Information

Publications15

  1. ncbi request reprint Saxiphilin, a saxitoxin-binding protein with two thyroglobulin type 1 domains, is an inhibitor of papain-like cysteine proteinases
    B Lenarcic
    Departments of Biochemistry and Molecular Biology, J Stefan Institute, Jamova 39, 1000 Ljubljana, Slovenia
    J Biol Chem 275:15572-7. 2000
    ..These results further demonstrate that various Thyr-1 domains are selective inhibitors of cysteine proteinases with utility in the study of protein interactions and degradation...
  2. ncbi request reprint Thyroglobulin type-1 domains in equistatin inhibit both papain-like cysteine proteinases and cathepsin D
    B Lenarcic
    Department of Biochemistry and Molecular Biology, J Stefan Institute, Jamova 39, 1000 Ljubljana, Slovenia
    J Biol Chem 274:563-6. 1999
    ..Equistatin is the first inhibitor of animal origin known to inhibit cathepsin D. The obtained results demonstrate that the widely distributed thyroglobulin type-1 domains can support a variety of functions...
  3. ncbi request reprint Equistatin, a new inhibitor of cysteine proteinases from Actinia equina, is structurally related to thyroglobulin type-1 domain
    B Lenarcic
    Department of Biochemistry and Molecular Biology, Jozef Stefan Institute, Jamova 39, 1000 Ljubljana, Slovenia
    J Biol Chem 272:13899-903. 1997
    ..This superfamily currently includes equistatin, major histocompatibility complex class II- associated p41 invariant chain fragment, and chum salmon egg cysteine proteinase inhibitor...
  4. ncbi request reprint Differences in specificity for the interactions of stefins A, B and D with cysteine proteinases
    B Lenarcic
    Department of Biochemistry and Molecular Biology, J Stefan Institute, Ljubljana, Slovenia
    FEBS Lett 395:113-8. 1996
    ..The presence of a highly negatively charged N-terminus on stefin D1 constitutes a likely structural determinant of inhibitor specificity...
  5. ncbi request reprint Molecular cloning of a putative homolog of proline/arginine-rich antibacterial peptides from porcine bone marrow
    J Pungercar
    Department of Biochemistry and Molecular Biology, Jozef Stefan Institute, Ljubljana, Slovenia
    FEBS Lett 336:284-8. 1993
    ..These precursors could represent a part of the antibacterial peptide repertoire of porcine bone marrow...
  6. ncbi request reprint Acidic pH as a physiological regulator of human cathepsin L activity
    B Turk
    Department of Biochemistry and Molecular Biology, J Stefan Institute, Ljubljana, Slovenia
    Eur J Biochem 259:926-32. 1999
    ..Aspartic protease cathepsin D was shown to cleave denatured, but not active cathepsin L, suggesting a potential mechanism for in-vivo regulation and turnover of cathepsin L inside lysosomes...
  7. ncbi request reprint Cathepsin D inactivates cysteine proteinase inhibitors, cystatins
    B Lenarcic
    Department of Biochemistry, J Stefan Institute, Ljubljana, Yugoslavia
    Biochem Biophys Res Commun 154:765-72. 1988
    ....
  8. ncbi request reprint Equistatin, a protease inhibitor from the sea anemone actinia equina, is composed of three structural and functional domains
    B Strukelj
    Department of Biochemistry and Molecular Biology, Jozef Stefan Institute, Jamova 39, Ljubljana, SI 1000, Slovenia
    Biochem Biophys Res Commun 269:732-6. 2000
    ..60 nM) comparably to natural equistatin. Preliminary results on inhibition of cathepsin D, supported by structural comparison, show that the second domain is likely to be involved in activity against aspartic proteinases...
  9. ncbi request reprint The cysteine protease activity of Colorado potato beetle (Leptinotarsa decemlineata Say) guts, which is insensitive to potato protease inhibitors, is inhibited by thyroglobulin type-1 domain inhibitors
    K Gruden
    Department of Biochemistry and Molecular Biology, Jozef Stefan Institute, Ljubljana, Slovenia
    Insect Biochem Mol Biol 28:549-60. 1998
    ..This demonstrated the potential of equistatin to protect crops from insect attack...
  10. ncbi request reprint Inactivation of human cystatin C and kininogen by human cathepsin D
    B Lenarcic
    Department of Biochemistry, Jozef Stefan Institute, Slovenia, Yugoslavia
    FEBS Lett 280:211-5. 1991
    ..These results further support the proposed role of cathepsin D in the regulation of cysteine proteinase activity...
  11. ncbi request reprint Molecular cloning and identification of a novel porcine cathelin-like antibacterial peptide precursor
    B Strukelj
    Department of Biochemistry and Molecular Biology, Jozef Stefan Institute, Ljubljana, Slovenia
    Biol Chem Hoppe Seyler 376:507-10. 1995
    ....
  12. ncbi request reprint Cloning a synthetic gene for human stefin B and its expression in E. coli
    R Jerala
    Department of Biochemistry, Jozef Stefan Institute, Ljubljana, Yugoslavia
    FEBS Lett 239:41-4. 1988
    ..coli as a fusion protein with beta-galactosidase and as a native protein. The CNBr cleaved fusion protein and the native recombinant stefin B were inhibitory to papain and reacted with antibodies against human stefin B...
  13. ncbi request reprint Purification and structural characterization of bovine cathelicidins, precursors of antimicrobial peptides
    P Storici
    Dipartimento di Biochimica, Biofisica e Chimica delle Macromolecole, Universita di Trieste, Italy
    Eur J Biochem 238:769-76. 1996
    ..When assayed against cathepsin L, unlike the potent cystatin inhibitors, three of the four cathelicidins show only a poor inhibitory activity (Ki = 0.6-3 microM)...
  14. ncbi request reprint Chemical synthesis of a gene for human stefin A and its expression in E. coli
    M Strauss
    Institut fur Biochemie, Technische Hochschule Darmstadt
    Biol Chem Hoppe Seyler 369:1019-30. 1988
    ..coli alkaline phosphatase signal sequence, respectively. The secreted hybrid protein was shown to exhibit biological properties similar to the native protein isolated from human plasma...
  15. pmc The refined 2.4 A X-ray crystal structure of recombinant human stefin B in complex with the cysteine proteinase papain: a novel type of proteinase inhibitor interaction
    M T Stubbs
    Max Planck Institut fur Biochemie, Martinsried bei Munchen, FRG
    EMBO J 9:1939-47. 1990
    ..The interaction is dominated by hydrophobic contacts. Inhibition by the cysteine proteinase inhibitors is fundamentally different to that observed for the serine proteinase inhibitors...