Zobrazeno 1 - 10
of 42
pro vyhledávání: '"Patricia J Anderson"'
Publikováno v:
PLoS Pathogens, Vol 1, Iss 4, p e35 (2005)
The Streptococcus pyogenes NAD-glycohydrolase (SPN) is a toxic enzyme that is introduced into infected host cells by the cytolysin-mediated translocation pathway. However, how S. pyogenes protects itself from the self-toxicity of SPN had been unknown
Externí odkaz:
https://doaj.org/article/bb3f96ab6b7d4d36b36220ada6f5721f
Autor:
Patricia J. Anderson
The population of Ooolandia is hypnotized by the culture of MORE. Citizens of all kinds and colors go about their lives unaware that a great calamity is approaching. Banshooo, an amazingly mindful monkey, works for the Ooolandian Department of Nature
Autor:
Jian Zhu, Weiqiang Gao, Elodee A. Tuley, Lisa A. Westfield, J. Evan Sadler, Patricia J. Anderson
Publikováno v:
Journal of Biological Chemistry. 287:26944-26952
ADAMTS proteases typically employ some combination of ancillary C-terminal disintegrin-like, thrombospondin-1, cysteine-rich, and spacer domains to bind substrates and facilitate proteolysis by an N-terminal metalloprotease domain. We constructed chi
Publikováno v:
Journal of Biological Chemistry. 285:5683-5694
The Gram-positive pathogen Streptococcus pyogenes injects a β-NAD+ glycohydrolase (SPN) into the cytosol of an infected host cell using the cytolysin-mediated translocation pathway. In this compartment, SPN accelerates the death of the host cell by
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
Publikováno v:
Blood. 112:1713-1719
The metalloprotease ADAMTS13 efficiently cleaves only the Tyr1605-Met1606 bond in the central A2 domain of multimeric von Willebrand factor (VWF), even though VWF constitutes only 0.02% of plasma proteins. This remarkable specificity depends in part
Publikováno v:
Proceedings of the National Academy of Sciences. 103:19099-19104
Von Willebrand factor (VWF) is a multimeric protein that mediates platelet adhesion at sites of vascular injury, and ADAMTS13 (a disintegrin and metalloprotease with thrombospondin)is a multidomain metalloprotease that limits platelet adhesion by a f
Publikováno v:
Journal of Biological Chemistry. 280:21773-21778
ADAMTS13, a metalloprotease, cleaves von Willebrand factor (VWF) in plasma to generate smaller, less thrombogenic fragments. The interaction of von Willebrand factor with specific ADAMTS13 domains was characterized with a binding assay employing von
Publikováno v:
Proceedings of the National Academy of Sciences. 101:10578-10583
von Willebrand factor (vWF) is a multimeric plasma glycoprotein with three tandem A domains. Domains A1 and A3 bind to platelet glycoprotein Ibalpha (GPIbalpha) and collagen, respectively. Domain A2 contains the Tyr-1605-Met-1606 bond that is cleaved
Autor:
Patricia J. Anderson, Ann A. Bullock
Publikováno v:
Action in Teacher Education. 26:33-36
No Child Left Behind (NCLB) regulations mandate that alternative route teachers have a minimum of ten days of exposure to schools, students, and the educational system prior to their entry into schools. This regulation, along with increasing concerns