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Bon-Hun Koo

Showing results (11-20 of 20) with videos related to

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The FEBS Journal|September 29, 2009
Membrane type-1 matrix metalloprotease-independent activation of pro-matrix metalloprotease-2 by proprotein convertasesBon-Hun Koo, Hee-Hyun Kim, Michael Y Park, et al.
Toxicon : Official Journal of the International Society on Toxinology|June 22, 2002
Characterization and cDNA cloning of halyxin, a heterogeneous three-chain anticoagulant protein from the venom of Agkistrodon halys brevicaudusBon-Hun Koo, Young-Doug Sohn, Ki-Chul Hwang, et al.
The International Journal of Biochemistry & Cell Biology|November 11, 2008
Characterization of proADAMTS5 processing by proprotein convertasesJean-Michel Longpré, Daniel R McCulloch, Bon-Hun Koo, et al.
International Journal of Cancer|June 29, 2007
ADAMTSL3/punctin-2, a gene frequently mutated in colorectal tumors, is widely expressed in normal and malignant epithelial cells, vascular endothelial cells and other cell types, and its mRNA is reduced in colon cancerBon-Hun Koo, Tiina Hurskainen, Katrina Mielke, et al.
The Journal of Biological Chemistry|April 4, 2007
Regulation of ADAMTS9 secretion and enzymatic activity by its propeptideBon-Hun Koo, Jean-Michel Longpré, Robert P T Somerville, et al.
The Journal of Biological Chemistry|March 16, 2006
Cell-surface processing of pro-ADAMTS9 by furinBon-Hun Koo, Jean-Michel Longpré, Robert P T Somerville, et al.
Thrombosis Research|July 2, 2002
Deficiency of von Willebrand factor-cleaving protease activity in the plasma of malignant patientsBon-Hun Koo, Doyeun Oh, So Young Chung, et al.
Matrix Biology : Journal of the International Society for Matrix Biology|May 19, 2007
ADAMTS-like 2 (ADAMTSL2) is a secreted glycoprotein that is widely expressed during mouse embryogenesis and is regulated during skeletal myogenesisBon-Hun Koo, Carine Le Goff, Katherine A Jungers, et al.
Plos One|February 22, 2018
Crystal structure of a cold-active protease (Pro21717) from the psychrophilic bacterium, Pseudoalteromonas arctica PAMC 21717, at 1.4 Å resolution: Structural adaptations to cold and functional analysis of a laundry detergent enzymeHa Ju Park, Chang Woo Lee, Dockyu Kim, et al.
The American Journal of Pathology|January 23, 2010
ADAMTS9 is a cell-autonomously acting, anti-angiogenic metalloprotease expressed by microvascular endothelial cellsBon-Hun Koo, David M Coe, Laura J Dixon, et al.
Pageof 2

Showing results (11-20 of 20) with videos related to

Sort By:
Pageof 2
You have reached the last page of results.This site can display upto 20 results.
The FEBS Journal|September 29, 2009
Membrane type-1 matrix metalloprotease-independent activation of pro-matrix metalloprotease-2 by proprotein convertasesBon-Hun Koo, Hee-Hyun Kim, Michael Y Park, et al.
Toxicon : Official Journal of the International Society on Toxinology|June 22, 2002
Characterization and cDNA cloning of halyxin, a heterogeneous three-chain anticoagulant protein from the venom of Agkistrodon halys brevicaudusBon-Hun Koo, Young-Doug Sohn, Ki-Chul Hwang, et al.
The International Journal of Biochemistry & Cell Biology|November 11, 2008
Characterization of proADAMTS5 processing by proprotein convertasesJean-Michel Longpré, Daniel R McCulloch, Bon-Hun Koo, et al.
International Journal of Cancer|June 29, 2007
ADAMTSL3/punctin-2, a gene frequently mutated in colorectal tumors, is widely expressed in normal and malignant epithelial cells, vascular endothelial cells and other cell types, and its mRNA is reduced in colon cancerBon-Hun Koo, Tiina Hurskainen, Katrina Mielke, et al.
The Journal of Biological Chemistry|April 4, 2007
Regulation of ADAMTS9 secretion and enzymatic activity by its propeptideBon-Hun Koo, Jean-Michel Longpré, Robert P T Somerville, et al.
The Journal of Biological Chemistry|March 16, 2006
Cell-surface processing of pro-ADAMTS9 by furinBon-Hun Koo, Jean-Michel Longpré, Robert P T Somerville, et al.
Thrombosis Research|July 2, 2002
Deficiency of von Willebrand factor-cleaving protease activity in the plasma of malignant patientsBon-Hun Koo, Doyeun Oh, So Young Chung, et al.
Matrix Biology : Journal of the International Society for Matrix Biology|May 19, 2007
ADAMTS-like 2 (ADAMTSL2) is a secreted glycoprotein that is widely expressed during mouse embryogenesis and is regulated during skeletal myogenesisBon-Hun Koo, Carine Le Goff, Katherine A Jungers, et al.
Plos One|February 22, 2018
Crystal structure of a cold-active protease (Pro21717) from the psychrophilic bacterium, Pseudoalteromonas arctica PAMC 21717, at 1.4 Å resolution: Structural adaptations to cold and functional analysis of a laundry detergent enzymeHa Ju Park, Chang Woo Lee, Dockyu Kim, et al.
The American Journal of Pathology|January 23, 2010
ADAMTS9 is a cell-autonomously acting, anti-angiogenic metalloprotease expressed by microvascular endothelial cellsBon-Hun Koo, David M Coe, Laura J Dixon, et al.
Pageof 2