Zobrazeno 1 - 10
of 13
pro vyhledávání: '"Kristina Gegenbauer"'
Autor:
Niamh O'Regan, Kristina Gegenbauer, Eimear M. Gleeson, Kenji Fukudome, Jamie M. O'Sullivan, Clive Drakeford, Niall Dalton, Alain Chion, Teresa M. Brophy, Owen P. Smith, Roger J.S. Preston, James S. O'Donnell
Publikováno v:
Haematologica, Vol 107, Iss 8 (2022)
Externí odkaz:
https://doaj.org/article/915af75fe6c7477c8bc22b31031e043d
Publikováno v:
PLoS ONE, Vol 8, Iss 11, p e80251 (2013)
Regulator of G-protein signaling 18 (RGS18) is a GTPase-activating protein that turns off Gq signaling in platelets. RGS18 is regulated by binding to the adaptor protein 14-3-3 via phosphorylated serine residues S49 and S218 on RGS18. In this study w
Externí odkaz:
https://doaj.org/article/acd9242442494ee2b89a8b6f3631abe1
Autor:
Niamh O'Regan, Kristina Gegenbauer, Eimear M. Gleeson, Kenji Fukudome, Jamie M. O'Sullivan, Clive Drakeford, Niall Dalton, Alain Chion, Teresa M. Brophy, Owen P. Smith, Roger J.S. Preston, James S. O'Donnell
Publikováno v:
Haematologica. 107(8)
Autor:
Barry J. Byrne, Richard O’Kennedy, Teresa M. Brophy, Jamie M. O’Sullivan, Michelle Lavin, Orla Rawley, P. Vince Jenkins, Alain Chion, Kristina Gegenbauer, Roger J. S. Preston, James S. O’Donnell
Publikováno v:
Arteriosclerosis, Thrombosis, and Vascular Biology. 36:855-863
Objective— Recent studies have demonstrated that galectin-1 (Gal-1) and galectin-3 (Gal-3) can bind von Willebrand factor and directly modulate von Willebrand factor–dependent early thrombus formation in vivo. Because the glycans expressed on hum
Autor:
Tatjana Pabst, Werner Müller-Esterl, Kristina Wagner, Sabine Meurer, Johannes-Peter Stasch, Peter Schmidt, Sandra Geschka, Harald H.H.W. Schmidt, Kristina Gegenbauer, Michael Karas, Simone Matt, Sylke Pioch, Tobias Beckhaus, Nils Opitz
Publikováno v:
Circulation Research. 105:33-41
Nitric oxide (NO) is an essential vasodilator. In vascular diseases, oxidative stress attenuates NO signaling by both chemical scavenging of free NO and oxidation and downregulation of its major intracellular receptor, the αβ heterodimeric heme-con
Autor:
Niamh, O'Regan, Chris, Moxon, Kristina, Gegenbauer, Jamie M, O'Sullivan, Alain, Chion, Owen P, Smith, Roger J S, Preston, Teresa M, Brophy, Alister G, Craig, James S, O'Donnell
Publikováno v:
Thrombosis and Haemostasis
Summary Adherence of infected erythrocytes to vascular endothelium causes acute endothelial cell (EC) activation during Plasmodium falciparum infection. Consequently, proteins stored in Weibel-Palade (WP) bodies within EC are secreted into the plasma
Autor:
Jamie M. O’Sullivan, Alister Craig, Owen P. Smith, Padraic G. Fallon, Niall Dalton, James S. O’Donnell, Teresa M. Brophy, Alain Chion, Kristina Gegenbauer, Georges E. Grau, Ulrich Budde, Roger J. S. Preston, Niamh O’Regan, Sanaz Maleki
Publikováno v:
Blood. 127(9)
Plasmodium falciparum malaria infection is associated with an early marked increase in plasma von Willebrand factor (VWF) levels, together with a pathological accumulation of hyperreactive ultra-large VWF (UL-VWF) multimers. Given the established cri
Autor:
Eva Nievergall, Martin Lackmann, Carmen Llerena, Maxime Hallé, Lakmali Atapattu, Mariam Mansour, Peter W. Janes, Kristina Gegenbauer, Michel L. Tremblay
Publikováno v:
Journal of cell science. 129(2)
Eph receptors and their corresponding membrane-bound ephrin ligands regulate cell positioning and establish tissue patterns during embryonic and oncogenic development. Emerging evidence suggests that assembly of polymeric Eph signalling clusters reli
Publikováno v:
PLoS ONE, Vol 8, Iss 11, p e80251 (2013)
PLoS ONE
PLoS ONE
Regulator of G-protein signaling 18 (RGS18) is a GTPase-activating protein that turns off Gq signaling in platelets. RGS18 is regulated by binding to the adaptor protein 14-3-3 via phosphorylated serine residues S49 and S218 on RGS18. In this study w
Autor:
Carola Prelle, Meike Hoffmeister, Kristina Gegenbauer, Albert Smolenski, Jan Babica, Olga Neumüller
Publikováno v:
Blood. 114(7)
The small guanine-nucleotide–binding protein Rap1 plays a key role in platelet aggregation and hemostasis, and we recently identified Rap1GAP2 as the only GTPase-activating protein of Rap1 in platelets. In search of Rap1GAP2-associated proteins, we