Zobrazeno 1 - 10
of 34
pro vyhledávání: '"L. Kroon-Zitko"'
Publikováno v:
Proteins: Structure, Function, and Genetics. 36:205-216
Trifluoroethanol (TFE) has been used to probe differences in the stability of the native state and in the folding pathways of the homologous cysteine protein inhibitors, human stefin A and B. After complete unfolding in 4.5 mol/L GuHCl, stefin A refo
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::a2744aabaae59fa074dbe1cb3d354c04
https://doi.org/10.1002/(sici)1097-0134(19990801)36:2<205::aid-prot6>3.0.co
https://doi.org/10.1002/(sici)1097-0134(19990801)36:2<205::aid-prot6>3.0.co
Autor:
J.R. Martin, Vito Turk, Roman Jerala, Jonathan P. Waltho, L. Kroon-Zitko, Eva Zerovnik, C. J. Craven
Publikováno v:
Journal of Molecular Biology. 246:331-343
The three-dimensional solution structure of recombinant human stefin A has been determined by a simulated annealing protocol using a total of 1113 distance and angle constraints obtained from 1H and 15N HMR spectroscopy. The solution structure is rep
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::fe252685b10daab501197ca3ea04ca4f
https://doi.org/10.1006/jmbi.1994.0088
https://doi.org/10.1006/jmbi.1994.0088
Publikováno v:
European Journal of Biochemistry. 225:1181-1194
Stefin A is a member of the cystatin superfamily of proteins which are tight and reversibly binding inhibitors of the papain-like cysteine proteinases. The 'H-NMR and "N-NMR resonances of human stefin A have been sequentially assigned using two-dimen
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5c382cf3f630714818e62d29b961d198
https://doi.org/10.1111/j.1432-1033.1994.1181b.x
https://doi.org/10.1111/j.1432-1033.1994.1181b.x
Publikováno v:
Scopus-Elsevier
Guanidinium HCl (GdmHCl), pH, and heat denaturation of the recombinant human stefin B, a low molecular weight protein inhibitor of cysteine proteinases, has been followed by circular dichroism. From the noncoincidence of the transitions in the near a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b7dbc7d5c6f5b59b98f8f3632e2d6e75
https://doi.org/10.1016/s0021-9258(19)50385-4
https://doi.org/10.1016/s0021-9258(19)50385-4
Publikováno v:
Scopus-Elsevier
GuHCl, pH and thermal denaturation of the recombinant stefin B was followed by circular dichroism (CD) and size-exclusion chromatography (SEC). CD at 277 nm was taken as an indicator of integral tertiary structure and CD at 222 nm as an indicator of
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::aee599537615efa1f86171a8f0310d31
https://doi.org/10.1515/bchm3.1992.373.2.453
https://doi.org/10.1515/bchm3.1992.373.2.453
Autor:
Magda Tus̆ek, Eva Zerovnik, Maruša Pompe-Novak, L. Kroon-Zitko, Manca Kenig, Aida Krijes̆torac, Selma Berbić
We describe expression, purification, and characterization of three site-specific mutants of recombinant human stefin B: H75W, P36G, and P79S. The far- and near-UV CD spectra have shown that they have similar secondary and tertiary structures to the
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c07090330595f968f6ee93192f3ebe02
https://europepmc.org/articles/PMC2286520/
https://europepmc.org/articles/PMC2286520/
Publikováno v:
Proteins. 36(2)
Trifluoroethanol (TFE) has been used to probe differences in the stability of the native state and in the folding pathways of the homologous cysteine protein inhibitors, human stefin A and B. After complete unfolding in 4.5 mol/L GuHCl, stefin A refo
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::3a75cddaa41d9df5a4c539924846f81e
https://pubmed.ncbi.nlm.nih.gov/10398367
https://pubmed.ncbi.nlm.nih.gov/10398367
Publikováno v:
Protein expression and purification. 5(1)
Synthetic gene coding for human cysteine proteinase inhibitor stefin B was expressed in Escherichia coli by the use of pKP1500 plasmid-containing tac promotor and temperature-sensitive origin of replication, ensuring high plasmid copy number. Several
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a099c09cbdab78e37b1275617bd2e05c
https://pubmed.ncbi.nlm.nih.gov/8167475
https://pubmed.ncbi.nlm.nih.gov/8167475
Publikováno v:
The Journal of biological chemistry. 267(13)
Guanidinium HCl (GdmHCl), pH, and heat denaturation of the recombinant human stefin B, a low molecular weight protein inhibitor of cysteine proteinases, has been followed by circular dichroism. From the noncoincidence of the transitions in the near a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::2a5bb5dfdab358d1db0657d92a8f7044
https://pubmed.ncbi.nlm.nih.gov/1577741
https://pubmed.ncbi.nlm.nih.gov/1577741
Deletion of the carboxy terminal part of stefin B does not have a major effect for binding to papain
Publikováno v:
Biomedica biochimica acta. 50(4-6)
Determination of crystal structures of chicken cystatin and human stefin B complexed with papain revealed a novel model of protease inhibition and also structural differences between two cysteine proteinase inhibitor (CPI) families. According to the
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::91572ff29811e509e54faab6c8556fdd
https://pubmed.ncbi.nlm.nih.gov/1801733
https://pubmed.ncbi.nlm.nih.gov/1801733