Zobrazeno 1 - 10
of 13
pro vyhledávání: '"Jonathan Langdown"'
Autor:
David Stacey, Lingyan Chen, Paulina J. Stanczyk, Joanna M. M. Howson, Amy M. Mason, Stephen Burgess, Stephen MacDonald, Jonathan Langdown, Harriett McKinney, Kate Downes, Neda Farahi, James E. Peters, Saonli Basu, James S. Pankow, Weihong Tang, Nathan Pankratz, Maria Sabater-Lleal, Paul S. de Vries, Nicholas L. Smith, CHARGE Hemostasis Working Group, Amy D. Gelinas, Daniel J. Schneider, Nebojsa Janjic, Nilesh J. Samani, Shu Ye, Charlotte Summers, Edwin R. Chilvers, John Danesh, Dirk S. Paul
Publikováno v:
Nature Communications, Vol 13, Iss 1, Pp 1-15 (2022)
Many individual genetic risk loci associate with multiple diseases, but the molecular basis of these loci often remains unclear. Here, the authors provide a framework to reveal the genetic cross-disease associations at the PROCR vascular disease locu
Externí odkaz:
https://doaj.org/article/06e0764427f642ea9f1647a016e4fe9d
Autor:
David Stacey, Lingyan Chen, Paulina J. Stanczyk, Joanna M. M. Howson, Amy M. Mason, Stephen Burgess, Stephen MacDonald, Jonathan Langdown, Harriett McKinney, Kate Downes, Neda Farahi, James E. Peters, Saonli Basu, James S. Pankow, Weihong Tang, Nathan Pankratz, Maria Sabater-Lleal, Paul S. de Vries, Nicholas L. Smith, CHARGE Hemostasis Working Group, Amy D. Gelinas, Daniel J. Schneider, Nebojsa Janjic, Nilesh J. Samani, Shu Ye, Charlotte Summers, Edwin R. Chilvers, John Danesh, Dirk S. Paul
Publikováno v:
Nature Communications, Vol 13, Iss 1, Pp 1-2 (2022)
Externí odkaz:
https://doaj.org/article/1a0ca0f841d5435e8760059b3c401a54
Publikováno v:
Journal of Thrombosis and Haemostasis. 14:137-142
Essentials An IgA paraprotein with anti-thrombin activity was not associated with a severe bleeding phenotype. This observation challenges the paradigm that anticoagulant therapy necessarily increases bleeding risk. Characterization of the antibody s
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3ef513ef7ae3c10e1dbc45c80a3c16a5
https://doi.org/10.1111/jth.13171
https://doi.org/10.1111/jth.13171
Autor:
Melanie Proven, Catherine H-W Hsu, Chris Fisher, Roderick Lynn, Jonathan Langdown, Anna Rose, Jennifer Eglinton, Martin Besser
Publikováno v:
Hemoglobin. 42(3)
We report a novel hemoglobin (Hb) variant with a β chain amino acid substitution at codon 78 (CTG>CCG) (HBB: c.236T>C), detected through prenatal screening via capillary electrophoresis (CE) in an otherwise healthy and asymptomatic 38-year-old femal
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a05d35e253a144077f87dc8e3036075e
https://pubmed.ncbi.nlm.nih.gov/30328734
https://pubmed.ncbi.nlm.nih.gov/30328734
Publikováno v:
Proceedings of the National Academy of Sciences. 107:645-650
Factor (f) IXa is a critical enzyme for the formation of stable blood clots, and its deficiency results in hemophilia. The enzyme functions at the confluence of the intrinsic and extrinsic pathways by binding to fVIIIa and rapidly generating fXa. In
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::27082b786f70a5b2375bf864e3a101dd
https://doi.org/10.1073/pnas.0910144107
https://doi.org/10.1073/pnas.0910144107
Publikováno v:
Journal of Molecular Biology. 386:1278-1289
Summary Antithrombin (AT) is the most important inhibitor of coagulation proteases. Its activity is stimulated by glycosaminoglycans, such as heparin, through allosteric and template mechanisms. AT utilises an induced-fit mechanism to bind with high
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ea0057ecea66c338d08d19eb6cdbfa50
https://doi.org/10.1016/j.jmb.2009.01.028
https://doi.org/10.1016/j.jmb.2009.01.028
Crystal Structure of Monomeric Native Antithrombin Reveals a Novel Reactive Center Loop Conformation
Autor:
Stephan A. Luis, James A. Huntington, Daniel J. D. Johnson, Wei Li, Jonathan Langdown, Trevor Baglin
Publikováno v:
Journal of Biological Chemistry. 281:35478-35486
The poor inhibitory activity of circulating antithrombin (AT) is critical to the formation of blood clots at sites of vascular damage. AT becomes an efficient inhibitor of the coagulation proteases only after binding to a specific heparin pentasaccha
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d706fd1be345bc1002c5bb2d263d2864
https://doi.org/10.1074/jbc.m607204200
https://doi.org/10.1074/jbc.m607204200
Publikováno v:
Journal of Biological Chemistry. 279:47288-47297
Antithrombin (AT) inhibits most of the serine proteases generated in the blood coagulation cascade, but its principal targets are factors IXa, Xa, and thrombin. Heparin binding to AT, via a specific pentasaccharide sequence, alters the conformation o
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2ed933d44c792d2a46a5b3a9d4f1f47f
https://doi.org/10.1074/jbc.m408961200
https://doi.org/10.1074/jbc.m408961200
Publikováno v:
Blood. 124(12)
In this study, we describe a novel thrombomodulin (TM) mutation (c.1611C>A) that codes for a change from cysteine 537 to a premature stop codon (p.Cys537Stop). Three members of a family with a history of posttraumatic bleeding were identified to be h
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a12157b34c9fc150571c3b4986df2769
https://pubmed.ncbi.nlm.nih.gov/25606627
https://pubmed.ncbi.nlm.nih.gov/25606627
Publikováno v:
Hemoglobin. 16:11-17
Hb Turriff is a new hemoglobin variant which we have identified in a diabetic individual. During the determination of Hb A1c by high performance liquid chromatography, an inappropriately elevated result was found to be due to the abnormal hemoglobin
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::7022d5814f28b504ba048fb855dbeec9
https://doi.org/10.3109/03630269209005671
https://doi.org/10.3109/03630269209005671