Zobrazeno 1 - 7
of 7
pro vyhledávání: '"Rossella Tomazzolli"'
Publikováno v:
Archiv der Pharmazie. 348:23-33
In search for more effective drugs against HIV infection acting as non-nucleoside reverse transcriptase inhibitors (NNRTIs), a series of new molecules with hybrid structures based on the natural product (+)-calanolide A and the synthetic molecule α-
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::16fb36e2103204c7d597f45f44f189ed
https://doi.org/10.1002/ardp.201400235
https://doi.org/10.1002/ardp.201400235
Autor:
Rossella Tomazzolli, a Mauro Dalla Serra, a Giuseppe Bellisola, b Marco Colombatti, b, Graziano Guella, c
Publikováno v:
Analytical biochemistry
350 (2006): 105–112. doi:10.1016/j.ab.2005.11.037
info:cnr-pdr/source/autori:Rossella Tomazzolli;a Mauro Dalla Serra;a Giuseppe Bellisola;b Marco Colombatti;b, Graziano Guella;c,*/titolo:A fluorescence-based assay for the reductase activity of protein disulfide isomerase./doi:10.1016%2Fj.ab.2005.11.037/rivista:Analytical biochemistry (Print)/anno:2006/pagina_da:105/pagina_a:112/intervallo_pagine:105–112/volume:350
350 (2006): 105–112. doi:10.1016/j.ab.2005.11.037
info:cnr-pdr/source/autori:Rossella Tomazzolli;a Mauro Dalla Serra;a Giuseppe Bellisola;b Marco Colombatti;b, Graziano Guella;c,*/titolo:A fluorescence-based assay for the reductase activity of protein disulfide isomerase./doi:10.1016%2Fj.ab.2005.11.037/rivista:Analytical biochemistry (Print)/anno:2006/pagina_da:105/pagina_a:112/intervallo_pagine:105–112/volume:350
We report on a new spectrofluorimetric assay for the measurement of reductase activity of proteins belonging to the superfamily of thioredoxins such as protein disulfide isomerase (PDI). The assay relies on the preparation of a fluorescence-quenched
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::dd96800581614786ce87753005e2bf5d
https://doi.org/10.1016/j.ab.2005.11.037
https://doi.org/10.1016/j.ab.2005.11.037
Autor:
Francesca Bonini, Giulio Fracasso, Roberta Traini, Mauro Dalla Serra, Fabrizio Comper, Marco Colombatti, Rossella Tomazzolli
Publikováno v:
Journal of cellular biochemistry
98 (2006): 1130–1139. doi:10.1002/jcb.20845
info:cnr-pdr/source/autori:Bonini F., Traini R., Comper F., Fracasso G., Tomazzolli R., Dalla Serra M., Colombatti M./titolo:N-terminal deletion affects catalytic activity of saporin toxin./doi:10.1002%2Fjcb.20845/rivista:Journal of cellular biochemistry (Print)/anno:2006/pagina_da:1130/pagina_a:1139/intervallo_pagine:1130–1139/volume:98
98 (2006): 1130–1139. doi:10.1002/jcb.20845
info:cnr-pdr/source/autori:Bonini F., Traini R., Comper F., Fracasso G., Tomazzolli R., Dalla Serra M., Colombatti M./titolo:N-terminal deletion affects catalytic activity of saporin toxin./doi:10.1002%2Fjcb.20845/rivista:Journal of cellular biochemistry (Print)/anno:2006/pagina_da:1130/pagina_a:1139/intervallo_pagine:1130–1139/volume:98
Single-chain ribosome inactivating proteins (RIPs) are cytotoxic components of macromolecular pharmaceutics for immunotherapy of cancer and other human diseases. Saporin belongs to a family of single-chain RIPs sharing sequence and structure homology
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c2b5fa6f5c6d9168c6e858b4b2835273
https://doi.org/10.1002/jcb.20845
https://doi.org/10.1002/jcb.20845
Autor:
Katja Rebolj, a Biserka Bakrac, a Maja Garvas, b Katja Ota, a Marjeta Sentjurc, b Cristina Potrich, c,d Manuela Coraiola, c,d Rossella Tomazzolli, c,d Mauro Dalla Serra, c,d Peter Macek, a Kristina Sepcic, a,?
Publikováno v:
Biochemical journal (Lond., 1984) 1798 (2010): 891–902. doi:10.1016/j.bbamem.2010.01.016
info:cnr-pdr/source/autori:Katja Rebolj;a Biserka Bakrac;a Maja Garvas;b Katja Ota;a Marjeta Sentjurc;b Cristina Potrich;c,d Manuela Coraiola;c,d Rossella Tomazzolli;c,d Mauro Dalla Serra;c,d Peter Macek;a Kristina Sepcic;a,?/titolo:EPR and FTIR studies reveal the importance of highly ordered sterol-enriched membrane domains for ostreolysin activity./doi:10.1016%2Fj.bbamem.2010.01.016/rivista:Biochemical journal (Lond., 1984)/anno:2010/pagina_da:891/pagina_a:902/intervallo_pagine:891–902/volume:1798
info:cnr-pdr/source/autori:Katja Rebolj;a Biserka Bakrac;a Maja Garvas;b Katja Ota;a Marjeta Sentjurc;b Cristina Potrich;c,d Manuela Coraiola;c,d Rossella Tomazzolli;c,d Mauro Dalla Serra;c,d Peter Macek;a Kristina Sepcic;a,?/titolo:EPR and FTIR studies reveal the importance of highly ordered sterol-enriched membrane domains for ostreolysin activity./doi:10.1016%2Fj.bbamem.2010.01.016/rivista:Biochemical journal (Lond., 1984)/anno:2010/pagina_da:891/pagina_a:902/intervallo_pagine:891–902/volume:1798
Ostreolysin is a cytolytic protein from the edible oyster mushroom (Pleurotus ostreatus), which recognizes specifically and binds to raft-like sterol-enriched membrane domains that exist in the liquid-ordered phase. Its binding can be abolished by mi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::89da5d1434525a3ef8ef3cc61c37cc54
http://www.cnr.it/prodotto/i/9830
http://www.cnr.it/prodotto/i/9830
Autor:
Gianfranco Menestrina, Silvia Morante, Wolfram Meyer-Klaucke, Francesco Stellato, Rossella Tomazzolli, Mauro Dalla Serra, Cristina Potrich
Publikováno v:
European biophysics journal 35, 12 (2006). doi:10.1007/s00249-005-0041-7
European biophysics journal 35 (2006): 340–351. doi:10.1007/s00249-005-0041-7
info:cnr-pdr/source/autori:Stellato F., Menestrina G., Dalla Serra M., Potrich C., Tomazzolli R., Meyer-Klaucke W., Morante S./titolo:Metal binding in amyloid beta-peptides shows intra-and inter-peptide coordination modes/doi:10.1007%2Fs00249-005-0041-7/rivista:European biophysics journal/anno:2006/pagina_da:340/pagina_a:351/intervallo_pagine:340–351/volume:35
European biophysics journal 35 (2006): 340–351. doi:10.1007/s00249-005-0041-7
info:cnr-pdr/source/autori:Stellato F., Menestrina G., Dalla Serra M., Potrich C., Tomazzolli R., Meyer-Klaucke W., Morante S./titolo:Metal binding in amyloid beta-peptides shows intra-and inter-peptide coordination modes/doi:10.1007%2Fs00249-005-0041-7/rivista:European biophysics journal/anno:2006/pagina_da:340/pagina_a:351/intervallo_pagine:340–351/volume:35
X-ray absorption spectroscopy data show different metal binding site structures in beta-amyloid peptides according to whether they are complexed with Cu(2+) or Zn(2+) ions. While the geometry around copper is stably consistent with an intra-peptide b
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e4e03be362a0c676d7545b97a93696c6
https://bib-pubdb1.desy.de/record/80585
https://bib-pubdb1.desy.de/record/80585
Autor:
Rodolfo Ippoliti, Anders Rosén, Silvia Soldà, G. Menestrina, G. Bellisola, Silvia Udali, Giuseppe Tridente, Giulio Fracasso, Marco Colombatti, Rossella Tomazzolli
Publikováno v:
Biochemical pharmacology 67 (2004): 1721–1731.
info:cnr-pdr/source/autori:Bellisola G., Fracasso G., Ippoliti R., Menestrina G., Rosen A., Solda S., Udali S., Tomazzolli R., Tridente G., Colombatti M./titolo:Reductive activation of ricin and ricin A-chain immunotoxins by protein disulfide isomerase and thioredoxin reductase./doi:/rivista:Biochemical pharmacology/anno:2004/pagina_da:1721/pagina_a:1731/intervallo_pagine:1721–1731/volume:67
info:cnr-pdr/source/autori:Bellisola G., Fracasso G., Ippoliti R., Menestrina G., Rosen A., Solda S., Udali S., Tomazzolli R., Tridente G., Colombatti M./titolo:Reductive activation of ricin and ricin A-chain immunotoxins by protein disulfide isomerase and thioredoxin reductase./doi:/rivista:Biochemical pharmacology/anno:2004/pagina_da:1721/pagina_a:1731/intervallo_pagine:1721–1731/volume:67
Intracellular activation of ricin and of the ricin A-chain (RTA) immunotoxins requires reduction of their intersubunit disulfide(s). This crucial event is likely to be catalyzed by disulfide oxidoreductases and precedes dislocation of the toxic subun
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5dae2bdcdc6c69d6630cd01ee4d72a3d
http://hdl.handle.net/11697/12296
http://hdl.handle.net/11697/12296