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The Journal of Biological Chemistry
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February 18, 2017
A model for the conformational activation of the structurally quiescent metalloprotease ADAMTS13 by von Willebrand factor
Kieron South, Marta O Freitas, David A Lane
Blood
|
July 5, 2005
Directing thrombin
David A Lane, Helen Philippou, James A Huntington
Blood
|
February 22, 2014
Control of VWF A2 domain stability and ADAMTS13 access to the scissile bond of full-length VWF
Christopher J Lynch, David A Lane, Brenda M Luken
Blood
|
July 22, 2010
The ADAMTS13 metalloprotease domain: roles of subsites in enzyme activity and specificity
Rens de Groot, David A Lane, James T B Crawley
Blood
|
January 8, 2015
The role of the ADAMTS13 cysteine-rich domain in VWF binding and proteolysis
Rens de Groot, David A Lane, James T B Crawley
Journal of Thrombosis and Haemostasis : JTH
|
August 30, 2019
Partial rescue of naturally occurring active site factor X variants through decreased inhibition by tissue factor pathway inhibitor and antithrombin
Josefin Ahnström, Magdalena Gierula, Joseph Temenu, et al.
Peptides
|
June 14, 2005
Efficient isolation of peptide ligands for the endothelial cell protein C receptor (EPCR) using candidate receptor phage display biopanning
Stephen J White, Rachel E Simmonds, David A Lane, et al.
Proceedings of the National Academy of Sciences of the United States of America
|
June 28, 2011
Mechanism of von Willebrand factor scissile bond cleavage by a disintegrin and metalloproteinase with a thrombospondin type 1 motif, member 13 (ADAMTS13)
Yaozu Xiang, Rens de Groot, James T B Crawley, et al.
Plos One
|
November 30, 2017
A common mechanism by which type 2A von Willebrand disease mutations enhance ADAMTS13 proteolysis revealed with a von Willebrand factor A2 domain FRET construct
Christopher J Lynch, Adam D Cawte, Carolyn M Millar, et al.
Blood
|
February 24, 2009
Essential role of the disintegrin-like domain in ADAMTS13 function
Rens de Groot, Ajoy Bardhan, Nalisha Ramroop, et al.
Page
of 7
Search research articles
Search
Showing results (11-20 of 61) with videos related to
Sort By:
Page
of 7
The Journal of Biological Chemistry
|
February 18, 2017
A model for the conformational activation of the structurally quiescent metalloprotease ADAMTS13 by von Willebrand factor
Kieron South, Marta O Freitas, David A Lane
Blood
|
July 5, 2005
Directing thrombin
David A Lane, Helen Philippou, James A Huntington
Blood
|
February 22, 2014
Control of VWF A2 domain stability and ADAMTS13 access to the scissile bond of full-length VWF
Christopher J Lynch, David A Lane, Brenda M Luken
Blood
|
July 22, 2010
The ADAMTS13 metalloprotease domain: roles of subsites in enzyme activity and specificity
Rens de Groot, David A Lane, James T B Crawley
Blood
|
January 8, 2015
The role of the ADAMTS13 cysteine-rich domain in VWF binding and proteolysis
Rens de Groot, David A Lane, James T B Crawley
Journal of Thrombosis and Haemostasis : JTH
|
August 30, 2019
Partial rescue of naturally occurring active site factor X variants through decreased inhibition by tissue factor pathway inhibitor and antithrombin
Josefin Ahnström, Magdalena Gierula, Joseph Temenu, et al.
Peptides
|
June 14, 2005
Efficient isolation of peptide ligands for the endothelial cell protein C receptor (EPCR) using candidate receptor phage display biopanning
Stephen J White, Rachel E Simmonds, David A Lane, et al.
Proceedings of the National Academy of Sciences of the United States of America
|
June 28, 2011
Mechanism of von Willebrand factor scissile bond cleavage by a disintegrin and metalloproteinase with a thrombospondin type 1 motif, member 13 (ADAMTS13)
Yaozu Xiang, Rens de Groot, James T B Crawley, et al.
Plos One
|
November 30, 2017
A common mechanism by which type 2A von Willebrand disease mutations enhance ADAMTS13 proteolysis revealed with a von Willebrand factor A2 domain FRET construct
Christopher J Lynch, Adam D Cawte, Carolyn M Millar, et al.
Blood
|
February 24, 2009
Essential role of the disintegrin-like domain in ADAMTS13 function
Rens de Groot, Ajoy Bardhan, Nalisha Ramroop, et al.
Page
of 7