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of 10
pro vyhledávání: '"Sara, Zanardelli"'
Autor:
Ioanna, Antoniades, Anna, Charalambous, Neophytos, Christodoulou, Sara, Zanardelli, Paris A, Skourides
Publikováno v:
Methods in molecular biology (Clifton, N.J.). 1915
Calpains are a family of calcium-dependent intracellular cysteine proteases that regulate important physiological processes by substrate cleavage. Despite the fact that the role of calpains in cell migration and other processes has been extensively s
Autor:
Anna, Charalambous, Ioanna, Antoniades, Neophytos, Christodoulou, Sara, Zanardelli, Paris A, Skourides
Publikováno v:
Methods in molecular biology (Clifton, N.J.). 1915
Calpains are a family of calcium-dependent intracellular cysteine proteases that regulate important physiological processes by substrate cleavage. Despite the fact that Calpains have been identified in the Xenopus genome, their expression patterns an
Autor:
Neophytos Christodoulou, Sara Zanardelli, Ioanna Antoniades, Anna Charalambous, Paris A. Skourides
Publikováno v:
Methods in Molecular Biology ISBN: 9781493989874
Calpains are a family of calcium-dependent intracellular cysteine proteases that regulate important physiological processes by substrate cleavage. Despite the fact that Calpains have been identified in the Xenopus genome, their expression patterns an
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::b74039136622d82b532a7dfdfef25a59
https://doi.org/10.1007/978-1-4939-8988-1_6
https://doi.org/10.1007/978-1-4939-8988-1_6
Autor:
Anna Charalambous, Sara Zanardelli, Neophytos Christodoulou, Paris A. Skourides, Ioanna Antoniades
Publikováno v:
Methods in Molecular Biology ISBN: 9781493989874
Calpains are a family of calcium-dependent intracellular cysteine proteases that regulate important physiological processes by substrate cleavage. Despite the fact that the role of calpains in cell migration and other processes has been extensively s
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::d61019458e6adf26dc7278dbe7cb6b32
https://doi.org/10.1007/978-1-4939-8988-1_19
https://doi.org/10.1007/978-1-4939-8988-1_19
Autor:
Michael Laffan, Alain Chion, Sara Zanardelli, Thomas A. J. McKinnon, Michelle Tseng, Evelyn Groot, Peter J. Lenting, David A. Lane
Publikováno v:
Blood. 114:2819-2828
ADAMTS13 metalloprotease regulates the multimeric size of von Willebrand factor (VWF) by cleaving the Tyr1605-Met1606 bond in the VWF A2 domain. The mechanisms of VWF recognition by ADAMTS13 have yet to be fully resolved. Most studies have focused on
Autor:
Chan K N Chan Kwo Chion, James T. B. Crawley, David A. Lane, Sara Zanardelli, Roger J. S. Preston, Jonathan Lam
Publikováno v:
Journal of Biological Chemistry. 281:1555-1563
ADAMTS13 controls the multimeric size of circulating von Willebrand factor (VWF) by cleaving the Tyr1605-Met1606 bond in theA2 domain. To examine substrate recognition, we expressed in bacteria and purified three A2 (VWF76-(1593-1668), VWF115-(1554-1
Publikováno v:
Journal of thrombosis and haemostasis : JTH. 5
Following vascular injury, blood loss is controlled by the mechanisms of hemostasis. During this process, the serine proteinase, thrombin, is generated both locally and rapidly at sites of vessel damage. It plays a pivotal role in clot promotion and
Publikováno v:
Journal of Thrombosis and Haemostasis
Summary. Background: The multimeric size and platelettethering function of von Willebrand factor (VWF) are modulated by the plasma metalloprotease, a disintegrin and metalloproteinase with a thrombospondin type 1 motif, member 13 (ADAMTS-13). In vitr
Autor:
Francesca Marino, Pasqualina D'Ursi, Ermanna Rovida, Sara Zanardelli, Elena M. Faioni, Gessica Fontana, Giancarlo Castaman, Giuliana Merati
Publikováno v:
Human mutation 28 (2007): 345–355. doi:10.1002/humu.20445
info:cnr-pdr/source/autori:Ermanna Rovida 1, Giuliana Merati 2, Pasqualina D'Ursi 3, Sara Zanardelli 2, Francesca Marino 1, Gessica Fontana 4, GiancarloCastaman 5, Elena M. Faioni 4/titolo:Identification and computionally-based structural interpretation of naturally occuring variants of human protein C/doi:10.1002%2Fhumu.20445/rivista:Human mutation/anno:2007/pagina_da:345/pagina_a:355/intervallo_pagine:345–355/volume:28
info:cnr-pdr/source/autori:Rovida E; Merati G; D'Ursi P; Zanardelli S; Marino F; Fontana G; Castaman G; Faioni EM/titolo:Identification and computationally-based structural interpretation of naturally occurring variants of human protein C./doi:10.1002%2Fhumu.20445/rivista:Human mutation/anno:2007/pagina_da:345/pagina_a:355/intervallo_pagine:345–355/volume:28
info:cnr-pdr/source/autori:Ermanna Rovida 1, Giuliana Merati 2, Pasqualina D'Ursi 3, Sara Zanardelli 2, Francesca Marino 1, Gessica Fontana 4, GiancarloCastaman 5, Elena M. Faioni 4/titolo:Identification and computionally-based structural interpretation of naturally occuring variants of human protein C/doi:10.1002%2Fhumu.20445/rivista:Human mutation/anno:2007/pagina_da:345/pagina_a:355/intervallo_pagine:345–355/volume:28
info:cnr-pdr/source/autori:Rovida E; Merati G; D'Ursi P; Zanardelli S; Marino F; Fontana G; Castaman G; Faioni EM/titolo:Identification and computationally-based structural interpretation of naturally occurring variants of human protein C./doi:10.1002%2Fhumu.20445/rivista:Human mutation/anno:2007/pagina_da:345/pagina_a:355/intervallo_pagine:345–355/volume:28
Protein C (PC) is a key regulator of blood clotting and inflammation. Its inherited deficiency is associated with venous thromboembolism, and recombinant activated PC is currently used to increase survival in severe sepsis. The molecular basis of inh
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::77b27476a8e8451d128fb7236a52649f
https://publications.cnr.it/doc/323974
https://publications.cnr.it/doc/323974
Autor:
Michael Laffan, Peter J. Lenting, Sara Zanardelli, Evelyn Groot, Chan K N Chan Kwo Chion, David A. Lane
Publikováno v:
ResearcherID
ADAMTS13 plasma metalloprotease regulates the multimeric size of von Willebrand factor (VWF) by cleaving the Y1605-M1606 bond in the A2 domain. Several studies have characterised high affinity binding sites in the A2 domain, probably interacting with
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::affe90438f741d75ce22ecb4325a119e
http://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcAuth=ORCID&SrcApp=OrcidOrg&DestLinkType=FullRecord&DestApp=WOS_CPL&KeyUT=WOS:000262104704530&KeyUID=WOS:000262104704530
http://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcAuth=ORCID&SrcApp=OrcidOrg&DestLinkType=FullRecord&DestApp=WOS_CPL&KeyUT=WOS:000262104704530&KeyUID=WOS:000262104704530