Zobrazeno 1 - 10
of 15
pro vyhledávání: '"Vincenzo Lanzara"'
Autor:
Carlo Mischiati, Carlo Ferrari, Francesco Spinozzi, Katy Montin, Vincenzo Lanzara, Carlo M. Bergamini, Carlo Cervellati, Heinz Amenitsch, Monica Squerzanti, Paolo Mariani
Publikováno v:
Amino Acids. 42:2233-2242
Tissue transglutaminase undergoes thermal inactivation with first-order kinetics at moderate temperatures, in a process which is affected in opposite way by the regulatory ligands calcium and GTP, which stabilize different conformations. We have expl
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5fb494026c134a840d5716a63a8b3408
https://doi.org/10.1007/s00726-011-0963-6
https://doi.org/10.1007/s00726-011-0963-6
Autor:
Monica Squerzanti, Alberto Spisni, Carlo M. Bergamini, Carlo Cervellati, Vincenzo Lanzara, Lorella Franzoni, Francesco Spinozzi, Paolo Mariani
Publikováno v:
Amino Acids. 36:633-641
Activation of tissue transglutaminase by calcium involves a conformational change which allows exposition of the active site to the substrate via movements of domains 3 and 4 that lead to an increase of the inter-domain distance. The inhibitor GTP co
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a650e3169eec7d5841cb0e0234bf397f
https://doi.org/10.1007/s00726-008-0161-3
https://doi.org/10.1007/s00726-008-0161-3
Autor:
Patrizia Fortini, Rea Legnaro, G. L. Scapoli, Donato Gemmati, Marcello Izzo, Silvia Tognazzo, Vincenzo Lanzara, Annunziata Palazzo, Paolo Zamboni
Publikováno v:
Dermatologic Surgery. 31:644-649
BACKGROUND. Severe chronic venous disease (CVD) is characterized by both dermal hemosiderin accumulation and matrix metalloproteinase (MMP) hyperactivation. The iron-driven pathway is one of the recognized mechanisms of MMP hyperactivation. OBJECTIVE
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3dcc9a6cfa7b35f889dcb09eb04cc10a
https://doi.org/10.1111/j.1524-4725.2005.31611
https://doi.org/10.1111/j.1524-4725.2005.31611
Publikováno v:
Journal of Vascular Surgery. 37:132-136
Objective: Impaired venous drainage in severe chronic venous insufficiency (CVI) leads to microcirculatory overload, characterized by erythrocyte diapedesis and subsequent extravascular hemolysis, resulting in typical dermal hemosiderin deposition. W
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::69978bcf525c2668d17fc86b50f94f85
https://doi.org/10.1067/mva.2003.64
https://doi.org/10.1067/mva.2003.64
Autor:
Mattia Portinari, Vincenzo Lanzara, Patrizia Polverino de Laureto, Erica Frare, Carlo Mischiati, Carlo M. Bergamini, Carlo Cervellati, Giordana Feriotto, S. Lanzara, Paolo Carcoforo, Blendi Ura, Monica Squerzanti, Roberta Calza, Enzo Agostinelli
The aim of the present study was to analyze the protein composition of ductal breast carcinoma and the surrounding normal tissue in individual patients using comparative 2D proteomics and mass spectrometry to detect candidate disease biomarkers for d
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::63738f9049f0ef800299161d5b2f93f9
http://hdl.handle.net/11392/1811701
http://hdl.handle.net/11392/1811701
Autor:
Marco Signorini, Melandri P, Luigi Caselli, Carlo M. Bergamini, Carlo Ferrari, Vincenzo Lanzara
Publikováno v:
Scopus-Elsevier
Homogenates of Yoshida hepatoma cells, cultured as ascite suspension in vivo, display significant transglutaminase activity in both the cytosolic and the particulate fraction. The enzyme, however, is predominantly membrane-bound. Transglutaminase was
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::88fc4fdd52d8635c9d97e6be12257a03
https://doi.org/10.1515/bchm3.1996.377.3.167
https://doi.org/10.1515/bchm3.1996.377.3.167
Autor:
Carlo Mischiati, Vincenzo Lanzara, Carlo M. Bergamini, Katy Montin, Carlo Cervellati, Rita Casadio, Martin Griffin, Russell Collighan, Monica Squerzanti, Alessia Dondi, Gianluca Tasco
The transamidating activity of tissue transglutaminase is regulated by the ligands calcium and GTP, via conformational changes which facilitate or interfere with interaction with the peptidyl-glutamine substrate. We have analysed binding of these lig
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::dc36c3cc21a6873e18987f55939bf9a1
http://hdl.handle.net/11392/1391076
http://hdl.handle.net/11392/1391076
Autor:
Vincenzo Lanzara, Carlo M. Bergamini, Carlo Cervellati, Elena Casanova, Patrizia Polverino de Laureto, Alessandro Medici, Mariangela Dean, Monica Squerzanti
Publikováno v:
Applied and environmental microbiology. 68(6)
Purified bile salt hydrolase from bile-adapted Xanthomonas maltophilia displays Michaelis-Menten kinetics on cholylglycine and cholyltaurine and hydrolyzes bile salts also in crude bovine bile. The protein is a dimer and is resistant to proteinases a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f26293502709ccabfe00f7d31a92c2dd
https://pubmed.ncbi.nlm.nih.gov/12039776
https://pubmed.ncbi.nlm.nih.gov/12039776
Publikováno v:
Biochemical and Biophysical Research Communications. 110:578-583
At −11°C, −13°C only two of the four dihydroxyacetone phosphate binding sites of aldolase are catalytically active. The substrate is very tightly bound to the two sites since it does not exchange with the free substrate of the medium.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::fce302780256b6b1831ea4f12f4712dc
https://doi.org/10.1016/0006-291x(83)91189-0
https://doi.org/10.1016/0006-291x(83)91189-0
Autor:
Vincenzo Lanzara, Enrico Grazi
Publikováno v:
FEBS Letters. 221:387-390
In the presence of Mg2+, the formation of actin filaments is hindered by glyceraldehyde-3-phosphate dehydrogenase. This effect, which increases with the square of Mg2+ concentration, is counteracted by 0.15 M KCl. Thus KCl, at concentrations found in
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7d269ee50c60c2456b1f6a790a964027
https://doi.org/10.1016/0014-5793(87)80961-4
https://doi.org/10.1016/0014-5793(87)80961-4