Zobrazeno 1 - 10
of 158
pro vyhledávání: '"J. E. Sadler"'
Autor:
Timothy A. Springer, Hans Deckmyn, Joshua Muia, Louis Deforche, Elien Roose, J E Sadler, Nele Vandeputte, K. Soejima, Karen Vanhoorelbeke, Li-Zhi Mi, Aline Vandenbulcke, S. F. De Meyer, Hanspeter Rottensteiner, Hendrik B. Feys
Publikováno v:
Journal of Thrombosis and Haemostasis. 13:2063-2075
Summary Background Recently, conformational activation of ADAMTS-13 was identified. This mechanism showed the evolution from a condensed conformation, in which the proximal MDTCS and distal T2-CUB2 domains are in close contact with each other, to an
Autor:
J E Sadler, Tobias Obser, Sonja Schneppenheim, Reinhard Schneppenheim, Florian Oyen, U. Budde, M. Ledford-Kraemer, Rolf Marschalek, Cécile V. Denis, Maria A. Brehm, Robert R. Montgomery
UNLABELLED Essentials Von Willebrand disease IIC Miami features high von Willebrand factor (VWF) with reduced function. We aimed to identify and characterize the elusive underlying mutation in the original family. An inframe duplication of VWF exons
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2196a9d1a4989eea0348e64644f4e776
https://europepmc.org/articles/PMC5035592/
https://europepmc.org/articles/PMC5035592/
Publikováno v:
Journal of Thrombosis and Haemostasis. 7:2088-2095
Summary. Background: ADAMTS-13 proteolytic activity is controlled by the conformation of its substrate, von Willebrand factor (VWF), and changes in the secondary structure of VWF are essential for efficient cleavage. Substrate recognition is mediated
Autor:
J E Sadler
Publikováno v:
Journal of Thrombosis and Haemostasis. 7:24-27
During its life history, von Willebrand factor (VWF) experiences a remarkable sequence of conformational changes that are triggered by differences in pH between the endoplasmic reticulum (ER), Golgi and extracellular environments. VWF subunits dimeri
Autor:
Lars Holmberg, J E Sadler, A. Srivastava, Christine A. Lee, Ian R. Peake, M. Nishino, Emmanuel J. Favaloro, Augusto B. Federici, Dominique Meyer, U. Budde, P. M. Mannucci, F. Rodeghiero, Zaverio M. Ruggeri, Jørgen Ingerslev, Jeroen Eikenboom, Reinhard Schneppenheim, Frank Hill, Robert R. Montgomery, David Lillicrap, William L. Nichols, Claudine Mazurier
Publikováno v:
Journal of Thrombosis and Haemostasis. 4:2103-2114
von Willebrand disease (VWD) is reportedly the most common bleeding disorder and is caused by deficiencies and/or defects in the adhesive plasma protein von Willebrand factor (VWF). Functionally, normal VWF prevents bleeding by promoting both primary
Publikováno v:
Biochemistry. 41:2535-2542
Haemadin is a 57-amino acid thrombin inhibitor from the land-living leech Haemadipsa sylvestris, whose structure has recently been determined in complex with human alpha-thrombin. Here we communicate the effect of ionic strength on the kinetics of th
Publikováno v:
American Journal of Hematology. 68:122-126
INTRODUCTION (Dr. P. Ganguly)A workshop on von Willebrand factor (vWf) andThrombotic Thrombocytopenic Purpura (TTP) was orga-nized by the Division of Blood Diseases and Resourcesof the National Heart, Lung, and Blood Institute(NHLBI) and was held on
Publikováno v:
Acta Crystallographica Section D Biological Crystallography. 56:406-410
The Ser195Ala mutant of human alpha-thrombin was complexed with fibrinopeptide A(7-22) (FPA) in an effort to describe the (P1'-P6') post-cleavage binding subsites of the fibrinogen-recognition exosite and define more clearly the nature of the Michael
Autor:
U. Budde, Francesco Rodeghiero, Paolo Bucciarelli, Hiroshi Mohri, Jacob H. Rand, P. J. J. Van Genderen, Augusto B. Federici, J E Sadler, Dominique Meyer
Publikováno v:
Thrombosis and Haemostasis. 84:345-349
SummaryThe acquired von Willebrand syndrome (AvWS) is a rare bleeding disorder with laboratory findings similar to those of congenital von Willebrand disease (vWD). Despite the numerous cases reported in the literature until 1999 (n = 266), large stu
Autor:
Xinglong Zheng, Sergey Korolev, Deshun Lu, J E Sadler, Gabriel Waksman, Klaus Fütterer, Kai Tan
Publikováno v:
Journal of Molecular Biology. 292:361-373
Enteropeptidase is a membrane-bound serine protease that initiates the activation of pancreatic hydrolases by cleaving and activating trypsinogen. The enzyme is remarkably specific and cleaves after lysine residues of peptidyl substrates that resembl