Zobrazeno 1 - 10
of 45
pro vyhledávání: '"Leticia Nolasco"'
Autor:
Leticia Nolasco Vicente
Publikováno v:
Biblioteca Digital de Teses e Dissertações da USP
Universidade de São Paulo (USP)
instacron:USP
Universidade de São Paulo (USP)
instacron:USP
O estudo aqui apresentado traz reflexões sobre moradia e laço social partindo de entrevistas realizadas com pessoas moradoras do bairro Jardim Ângela e de experiências profissionais anteriores. Apesar da moradia ser um dos recursos organizadores
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::edf55ec9fda170790c83ca1f7e64453d
https://doi.org/10.11606/d.47.2020.tde-02102020-155802
https://doi.org/10.11606/d.47.2020.tde-02102020-155802
Autor:
Ching-Hwa Kiang, Kevin Jiang, Joel L. Moake, Sithara S. Wijeratne, Jingqiang Li, Leticia Nolasco
Publikováno v:
The Journal of Physical Chemistry B. 122:10653-10658
Activation of proteins often involves conformational transitions, and these switches are often difficult to characterize in multidomain proteins. Full-length factor H (FH), consisting of 20 small consensus repeat domains (150 kD), is a complement con
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ebf77cf360ed5c2990b27a89d10ea314
https://doi.org/10.1021/acs.jpcb.8b06153
https://doi.org/10.1021/acs.jpcb.8b06153
Autor:
Jennifer Nolasco, Qi Da, Zaverio M. Ruggeri, Miguel A. Cruz, Leticia Nolasco, Joel L. Moake, Sonya Cirlos
Publikováno v:
TH Open, Vol 02, Iss 03, Pp e338-e345 (2018)
von Willebrand factor (VWF) is a multimeric protein composed of monomeric subunits (∼280 kD) linked by disulfide bonds. During hemostasis and thrombosis, ultralarge (UL) VWF (ULVWF) multimers initiate platelet adhesion. In vitro, human C3 binds to
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::11f33426fb099d00fa092cb36f96dee4
https://doi.org/10.1055/s-0038-1672189
https://doi.org/10.1055/s-0038-1672189
Autor:
Joel L. Moake, Jingqiang Li, Ching-Hwa Kiang, Sithara S. Wijeratne, Eric W. Frey, Jing-fei Dong, Zhou Zhou, Hui Chun Yeh, Leticia Nolasco, Angela L. Bergeron
Publikováno v:
Physical Review E. 93
Von Willebrand factor (VWF) multimers are large adhesive proteins that are essential to the initiation of hemostatic plugs at sites of vascular injury. The binding of VWF multimers to platelets, as well as VWF proteolysis, is regulated by shear stres
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::56862fabaf7decf63416d125cd19521a
https://doi.org/10.1103/physreve.93.012410
https://doi.org/10.1103/physreve.93.012410
Publikováno v:
Seminars in Thrombosis and Hemostasis. 38:38-46
Ultralarge von Willebrand factor (ULVWF) multimeric strings are rapidly secreted by, and anchored to, stimulated endothelial cells (EC), and are hyperadhesive to platelets until cleavage by ADAMTS-13 (a disintegrin and metalloproteinase with a thromb
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c1580bc73b4ff4018ed95ecbf4fc403c
https://doi.org/10.1055/s-0031-1300950
https://doi.org/10.1055/s-0031-1300950
Autor:
Subhashree Pradhan, Joel L. Moake, Tanvir Khatlani, Jing-fei Dong, K. V. Vijayan, Francisca C. Gushiken, Nancy A. Turner, Leticia Nolasco
Publikováno v:
Journal of Thrombosis and Haemostasis. 7:1009-1018
Summary. Background: Secretion of Weibel–Palade body (WPB) contents is regulated, in part, by the phosphorylation of proteins that constitute the endothelial exocytotic machinery. In comparison to protein kinases, a role for protein phosphatases in
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3ce2a1dc20f9dab57983ea8b6af71076
https://doi.org/10.1111/j.1538-7836.2009.03355.x
https://doi.org/10.1111/j.1538-7836.2009.03355.x
Autor:
K. Anthony, Jing-fei Dong, Yuandong Peng, Zhenyin Tao, Leticia Nolasco, Huiwan Choi, Lawrence Rice, Joel L. Moake
Publikováno v:
Journal of Thrombosis and Haemostasis. 4:1931-1935
Summary. Background: Thrombotic thrombocytopenic purpura (TTP) is associated with congenital and acquired deficiency of ADAMTS-13, a metalloprotease that cleaves von Willebrand factor (VWF) and reduces its adhesive activity. Mutations throughout the
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c882611e59e1e505912d69293816dade
https://doi.org/10.1111/j.1538-7836.2006.02098.x
https://doi.org/10.1111/j.1538-7836.2006.02098.x
Autor:
Renhao Li, Yuandong Peng, Zhenyin Tao, Joel L. Moake, Leticia Nolasco, José A. López, Santiago Cal, Jing-fei Dong, Carlos López-Otín
Publikováno v:
Blood. 106:4139-4145
The metalloprotease ADAMTS13 (a disintegrin and metalloprotease with thrombospondin motif) converts the hyperreactive unusually large (UL) forms of von Willebrand factor (VWF) that are newly released from endothelial cells into less active plasma for
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::46b2570a5981fd94ad0ebb289252e990
https://doi.org/10.1182/blood-2005-05-2029
https://doi.org/10.1182/blood-2005-05-2029
Autor:
Leticia Nolasco, Huiwan Choi, C. Ruan, Joel L. Moake, Jing-fei Dong, Angela L. Bergeron, Aubrey Bernardo, Li Liu
Publikováno v:
Journal of Thrombosis and Haemostasis. 3:2536-2544
Summary. The adhesion ligand von Willebrand factor (VWF) is synthesized and stored in vascular endothelial cells and megakaryocytes/platelets. As in endothelial cells, platelet VWF also contains ultra-large (UL) multimers that are hyperactive in aggr
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4fdc004f07898df94ae4dda08bbf7e2a
https://doi.org/10.1111/j.1538-7836.2005.01561.x
https://doi.org/10.1111/j.1538-7836.2005.01561.x
Publikováno v:
Journal of Thrombosis and Haemostasis. 3:562-570
Leukocyte rolling on vascular endothelium is mediated by an interaction between P-selectin expressed on endothelial cells and P-selectin glycoprotein ligand-1 on leukocytes. This interaction reduces the velocity of leukocyte movements to allow subseq
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::02b190b942f58cf1b42eaba1a9f37ba6
https://doi.org/10.1111/j.1538-7836.2005.01122.x
https://doi.org/10.1111/j.1538-7836.2005.01122.x