Zobrazeno 1 - 10
of 15
pro vyhledávání: '"Scott C. Meixner"'
Publikováno v:
Scientific Reports, Vol 13, Iss 1, Pp 1-12 (2023)
Abstract Even with extensive transfusion support, trauma-induced bleeding often leads to death. Early intervention may improve outcomes, yet which blood products, factor concentrates, or other drugs constitute optimal treatment is unclear. Patients w
Externí odkaz:
https://doaj.org/article/432c6c783d1e480fba8aef1bf2870d7b
Autor:
Alan E. Mast, Scott C. Meixner, Wolfram Ruf, Piyushkumar R. Kapopara, Victor Lei, Edward M. Conway, Kevin Gonzalez, Houra Loghmani, Edward L.G. Pryzdial, Jenny Li-Ying Huang, Nooshin Safikhan
Publikováno v:
J Thromb Haemost
BACKGROUND: CD248 is a pro-inflammatory, transmembrane glycoprotein expressed by vascular smooth muscle cells (VSMC), monocytes/macrophages, and other cells of mesenchymal origin. Its distribution and properties are reminiscent of those of the initia
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::94fa97d02a80b30e2cbca9c4bd685f0d
https://europepmc.org/articles/PMC8571649/
https://europepmc.org/articles/PMC8571649/
Autor:
Jerry Leung, Hannah M. Russell, Joseph S. Palumbo, Amy W. Strilchuk, Edward L. G. Pryzdial, Jayesh A. Kulkarni, Edward M. Conway, Scott C. Meixner, Christian J. Kastrup, A. Phillip Owens, Pieter R. Cullis, Nooshin S Safikhan, Michael R. Sutherland, Roy van der Meel
Publikováno v:
Blood : the Journal of Hematology, 136(25), 2946-2954. American Society of Hematology
Blood
Blood
The activated form of coagulation factor XIII (FXIII-A2B2), FXIII-A*, is a hemostatic enzyme essential for inhibiting fibrinolysis by irreversibly crosslinking fibrin and antifibrinolytic proteins. Despite its importance, there are no modulatory ther
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::dc9f99a508f51b73c8a02a3011862607
https://pubmed.ncbi.nlm.nih.gov/32678423
https://pubmed.ncbi.nlm.nih.gov/32678423
Autor:
W. S. Hur, J. G. Van Der Gugten, Hélène C. F. Côté, Scott C. Meixner, Daniel T. Holmes, Agnes Y.Y. Lee, Christian J. Kastrup, R. L. R. Carter, Kimberley Talbot, Ed L.G. Pryzdial, Tyler Smith
Publikováno v:
Journal of Thrombosis and Haemostasis. 16:2276-2288
Essentials Activated clotting factor X (FXa) acquires fibrinolytic cofactor function after cleavage by plasmin. FXa-mediated plasma fibrinolysis is enabled by active site modification blocking a second cleavage. FXa-directed oral anticoagulants (DOAC
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c3579cb4f34c30f074d6a35a10323397
https://doi.org/10.1111/jth.14281
https://doi.org/10.1111/jth.14281
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics. 1834:989-995
Our previous work showed that purified coagulation factor Xa (FXa) acquires fibrinolysis cofactor activity after plasmin-mediated cleavage. The predominant functional species is a non-covalent heterodimer of 33 and 13 kDa, termed Xa33/13, which has p
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b9ca1950316acae09d62c93d9d12c075
https://doi.org/10.1016/j.bbapap.2013.02.007
https://doi.org/10.1016/j.bbapap.2013.02.007
Autor:
Michael R. Sutherland, Edward L.G. Pryzdial, Edwin S. Gershom, Scott C. Meixner, A. L. Vanden Hoek
Publikováno v:
Thrombosis and Haemostasis. 107:760-768
SummaryThe incorporation of virus- and host-derived procoagulant factors initiates clotting directly on the surface of herpesviruses, which is an explanation for their correlation to vascular disease. The virus exploits the resulting thrombin to enha
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::47199a1b3bcd1cd7d6da85d3ca24266b
https://doi.org/10.1160/th11-08-0601
https://doi.org/10.1160/th11-08-0601
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics. 1804:723-730
We previously showed that coagulation factor Xa (FXa) enhances activation of the fibrinolysis zymogen plasminogen to plasmin by tissue plasminogen activator (tPA). Implying that proteolytic modulation occurs in situ, intact FXa (FXaalpha) must be seq
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8e2a59912d727354495c2032c1415366
https://doi.org/10.1016/j.bbapap.2009.11.011
https://doi.org/10.1016/j.bbapap.2009.11.011
Autor:
Mark A. Hancock, Jean E. Grundy, Marlys L. Koschinsky, Scott C. Meixner, Roger C. MacKenzie, Edward L.G. Pryzdial
Publikováno v:
Thrombosis and Haemostasis. 97:38-44
SummaryPlasminogen binding to receptors involves both C-terminal lysine-dependent and -independent interactions. The latter are poorly understood. Our earlier work demonstrated a novel Ca2+-enhanced bivalent interaction between plasmin-cleaved FXa (F
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::500c02fce0eac7562f1ab4ddef1fb71d
https://doi.org/10.1160/th06-08-0476
https://doi.org/10.1160/th06-08-0476
Autor:
James R. Baylis, Louise J. Eltringham-Smith, William P. Sheffield, Edward L.G. Pryzdial, Scott C. Meixner, Kimberley Talbot, Frank M.H. Lee, Christian J. Kastrup
Publikováno v:
Journal of thrombosis and haemostasis : JTH. 14(9)
Essentials Factor Xa (FXa) acquires cleavage-mediated tissue plasminogen activator (tPA) cofactor activity. Recombinant (r) tPA is the predominant thrombolytic drug, but it may cause systemic side effects. Chemically modified, non-enzymatic FXa was p
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::bcc359322bfd012085054f2c9cf7af47
https://pubmed.ncbi.nlm.nih.gov/27359348
https://pubmed.ncbi.nlm.nih.gov/27359348
Autor:
Zhen Lu, Timothy Myles, Scott C. Meixner, Edward L.G. Pryzdial, Michael J. Krisinger, Verena Goebeler, Edward M. Conway
Publikováno v:
Blood. 120(8)
The coagulation and complement pathways simultaneously promote homeostasis in response to injury but cause tissue damage when unregulated. Mechanisms by which they cooperate are poorly understood. To delineate their interactions, we studied the effec
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::aa78a841b9b3c6754ec74d34ba92180c
https://pubmed.ncbi.nlm.nih.gov/22802338
https://pubmed.ncbi.nlm.nih.gov/22802338