Zobrazeno 1 - 4
of 4
pro vyhledávání: '"Jacob R, Mackinder"'
Autor:
Carly E, Martin, Andrew S, Murray, Jacob R, Mackinder, Kimberley E, Sala-Hamrick, Michael G, Flynn, Joseph G, Lundgren, Fausto A, Varela, Karin, List
Publikováno v:
Biological Chemistry. 403:969-982
TMPRSS13 is a member of the type II transmembrane serine protease (TTSP) family. Here we characterize a novel post-translational mechanism important for TMPRSS13 function: proteolytic cleavage within the extracellular TMPRSS13 stem region located bet
Autor:
Lauren M. Tanabe, Carly E. Martin, Karin List, Thomas E. Hyland, Jacob R. Mackinder, Fausto A. Varela, Andrew S. Murray, Kimberley E. Sala-Hamrick
Publikováno v:
Oncogene
Breast cancer progression is accompanied by increased expression of extracellular and cell-surface proteases capable of degrading the extracellular matrix as well as cleaving and activating downstream targets. The type II transmembrane serine proteas
Autor:
Kimberley E. Sala-Hamrick, Fausto A. Varela, Jacob R. Mackinder, Victoria L. Foust, Sokol V. Todi, Carly E. Martin, Karin List, Thomas E. Hyland, Andrew S. Murray
Publikováno v:
Scientific Reports, Vol 10, Iss 1, Pp 1-14 (2020)
Scientific Reports
Scientific Reports
Cancer progression is often accompanied by increased levels of extracellular proteases capable of remodeling the extracellular matrix and promoting pro-cancerous signaling pathways by activating growth factors and receptors. The type II transmembrane
Autor:
Fausto A. Varela, Kimberley E. Sala-Hamrick, Jacob R. Mackinder, Karin List, Andrew S. Murray, Carly E. Martin, Evan C. Harrison, Joseph G. Lundgren
Publikováno v:
The Journal of Biological Chemistry
TMPRSS13, a member of the type II transmembrane serine protease (TTSP) family, harbors four N-linked glycosylation sites in its extracellular domain. Two of the glycosylated residues are located in the scavenger receptor cysteine-rich (SRCR) protein