Research Topics
Genomes and Genes | B LenarcicSummaryAffiliation: Jozef Stefan Institute Country: Slovenia Publications
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Publications
Saxiphilin, a saxitoxin-binding protein with two thyroglobulin type 1 domains, is an inhibitor of papain-like cysteine proteinasesB 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...- Thyroglobulin type-1 domains in equistatin inhibit both papain-like cysteine proteinases and cathepsin DB 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... - Equistatin, a new inhibitor of cysteine proteinases from Actinia equina, is structurally related to thyroglobulin type-1 domainB 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... - Differences in specificity for the interactions of stefins A, B and D with cysteine proteinasesB 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... - Molecular cloning of a putative homolog of proline/arginine-rich antibacterial peptides from porcine bone marrowJ 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... - Acidic pH as a physiological regulator of human cathepsin L activityB 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... - Cathepsin D inactivates cysteine proteinase inhibitors, cystatinsB Lenarcic
Department of Biochemistry, J Stefan Institute, Ljubljana, Yugoslavia
Biochem Biophys Res Commun 154:765-72. 1988.... - Equistatin, a protease inhibitor from the sea anemone actinia equina, is composed of three structural and functional domainsB 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... - 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 inhibitorsK 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... - Inactivation of human cystatin C and kininogen by human cathepsin DB 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... - Molecular cloning and identification of a novel porcine cathelin-like antibacterial peptide precursorB Strukelj
Department of Biochemistry and Molecular Biology, Jozef Stefan Institute, Ljubljana, Slovenia
Biol Chem Hoppe Seyler 376:507-10. 1995.... - Cloning a synthetic gene for human stefin B and its expression in E. coliR 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... - Purification and structural characterization of bovine cathelicidins, precursors of antimicrobial peptidesP 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)... - Chemical synthesis of a gene for human stefin A and its expression in E. coliM 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... 
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 interactionM 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...