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Molecular Aspects of Medicine|September 12, 2008
Meprins, membrane-bound and secreted astacin metalloproteinasesErwin E Sterchi, Walter Stöcker, Judith S Bond
FASEB Bioadvances|July 4, 2020
A brief history of FASEB and its programs and activitiesHoward H Garrison, Judith S Bond, Ralph A Bradshaw
The Journal of Biological Chemistry|October 26, 2002
Structure of homo- and hetero-oligomeric meprin metalloproteases. Dimers, tetramers, and high molecular mass multimersGreg P Bertenshaw, Mona T Norcum, Judith S Bond
The Journal of Biological Chemistry|July 31, 2003
Critical amino acids in the active site of meprin metalloproteinases for substrate and peptide bond specificityJames P Villa, Greg P Bertenshaw, Judith S Bond
Archives of Biochemistry and Biophysics|February 6, 2002
Chaperone interactions of the metalloproteinase meprin A in the secretory or proteasomal-degradative pathwayTakayuki Tsukuba, Tomoko Kadowaki, Jeremy A Hengst, et al.
Journal of Virology|April 17, 2020
Impact of Měnglà Virus Proteins on Human and Bat Innate Immune PathwaysCaroline G Williams, Joyce Sweeney Gibbons, Timothy R Keiffer, et al.
Proceedings of the National Academy of Sciences of the United States of America|May 19, 2016
Incoming human papillomavirus type 16 genome resides in a vesicular compartment throughout mitosisStephen DiGiuseppe, Wioleta Luszczek, Timothy R Keiffer, et al.
FEBS Letters|June 10, 2005
Meprin metalloprotease expression and regulation in kidney, intestine, urinary tract infections and cancerJudith S Bond, Gail L Matters, Sanjita Banerjee, et al.
American Journal of Physiology. Renal Physiology|July 29, 2011
Villin and actin in the mouse kidney brush-border membrane bind to and are degraded by meprins, an interaction that contributes to injury in ischemia-reperfusionElimelda Moige Ongeri, Odinaka Anyanwu, W Brian Reeves, et al.
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