Zobrazeno 1 - 6
of 6
pro vyhledávání: '"Nicholas Nobiletti"'
Autor:
Luca Goitre, Peter V. DiStefano, Andrea Moglia, Nicholas Nobiletti, Eva Baldini, Lorenza Trabalzini, Julie Keubel, Eliana Trapani, Vladimir V. Shuvaev, Vladimir R. Muzykantov, Ingrid H. Sarelius, Saverio Francesco Retta, Angela J. Glading
Publikováno v:
Scientific Reports, Vol 7, Iss 1, Pp 1-12 (2017)
Abstract The intracellular scaffold KRIT1/CCM1 is an established regulator of vascular barrier function. Loss of KRIT1 leads to decreased microvessel barrier function and to the development of the vascular disorder Cerebral Cavernous Malformation (CC
Externí odkaz:
https://doaj.org/article/6fc3adc7ae70457492848b492ff196e1
Publikováno v:
The FEBS Journal. 290:1078-1095
Loss of Krev interaction-trapped-1 (KRIT1) expression leads to the development of cerebral cavernous malformations (CCM), a disease in which abnormal blood vessel formation compromises the structure and function of the blood-brain barrier. The role o
Autor:
Nicholas, Nobiletti, Angela J, Glading
Publikováno v:
Methods in molecular biology (Clifton, N.J.). 2152
Cerebral cavernous malformation (CCM) is driven by changes in the cerebral microvascular endothelial cell population. Mouse models of CCM have successfully recapitulated the disease in vivo; however, dissection of the disease pathogenesis and molecul
Autor:
Angela Glading, Nicholas Nobiletti
Publikováno v:
Methods in Molecular Biology ISBN: 9781071606391
Cerebral cavernous malformation (CCM) is driven by changes in the cerebral microvascular endothelial cell population. Mouse models of CCM have successfully recapitulated the disease in vivo; however, dissection of the disease pathogenesis and molecul
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::1cd4a827f1ced17923fa9592794dac84
https://doi.org/10.1007/978-1-0716-0640-7_19
https://doi.org/10.1007/978-1-0716-0640-7_19
Publikováno v:
Biophysical Journal. 104:217a
Protein-protein interactions are extremely important interactions in the body responsible for many necessary functions. This study aims to specifically look at the interactions between the lectin-like domain of thrombomodulin (TM) and complement comp