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Jessica L Tacchi

Showing results (1-10 of 16) with videos related to

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Proteomics|December 11, 2014
Non-proteolytic functions of microbial proteases increase pathological complexityVeronica M Jarocki, Jessica L Tacchi, Steven P Djordjevic
International Journal of Medical Microbiology : IJMM|May 26, 2019
Formylated N-terminal methionine is absent from the Mycoplasma hyopneumoniae proteome: Implications for translation initiationVeronica M Jarocki, Joel R Steele, Michael Widjaja, et al.
Journal of Extracellular Vesicles|September 11, 2014
Proteome analysis of multidrug-resistant, breast cancer-derived microparticlesDeep Pokharel, Matthew P Padula, Jamie F Lu, et al.
Journal of Proteome Research|November 8, 2013
P159 from Mycoplasma hyopneumoniae binds porcine cilia and heparin and is cleaved in a manner akin to ectodomain sheddingBenjamin B A Raymond, Jessica L Tacchi, Veronica M Jarocki, et al.
Journal of Proteome Research|May 9, 2014
Cilium adhesin P216 (MHJ_0493) is a target of ectodomain shedding and aminopeptidase activity on the surface of Mycoplasma hyopneumoniaeJessica L Tacchi, Benjamin B A Raymond, Veronica M Jarocki, et al.
BMC Genomics|July 10, 2014
Proteogenomic mapping of Mycoplasma hyopneumoniae virulent strain 232Ken Pendarvis, Matthew P Padula, Jessica L Tacchi, et al.
Scientific Reports|September 13, 2017
N-terminomics identifies widespread endoproteolysis and novel methionine excision in a genome-reduced bacterial pathogenIain J Berry, Veronica M Jarocki, Jessica L Tacchi, et al.
Open Biology|January 16, 2015
MHJ_0461 is a multifunctional leucine aminopeptidase on the surface of Mycoplasma hyopneumoniaeVeronica M Jarocki, Jerran Santos, Jessica L Tacchi, et al.
Journal of Proteome Research|January 11, 2012
Mycoplasma hyopneumoniae Surface proteins Mhp385 and Mhp384 bind host cilia and glycosaminoglycans and are endoproteolytically processed by proteases that recognize different cleavage motifsAnia T Deutscher, Jessica L Tacchi, F Chris Minion, et al.
The Journal of Biological Chemistry|October 5, 2011
Sequence TTKF ↓ QE defines the site of proteolytic cleavage in Mhp683 protein, a novel glycosaminoglycan and cilium adhesin of Mycoplasma hyopneumoniaeDaniel R Bogema, Nichollas E Scott, Matthew P Padula, et al.
Pageof 2

Showing results (1-10 of 16) with videos related to

Sort By:
Pageof 2
Proteomics|December 11, 2014
Non-proteolytic functions of microbial proteases increase pathological complexityVeronica M Jarocki, Jessica L Tacchi, Steven P Djordjevic
International Journal of Medical Microbiology : IJMM|May 26, 2019
Formylated N-terminal methionine is absent from the Mycoplasma hyopneumoniae proteome: Implications for translation initiationVeronica M Jarocki, Joel R Steele, Michael Widjaja, et al.
Journal of Extracellular Vesicles|September 11, 2014
Proteome analysis of multidrug-resistant, breast cancer-derived microparticlesDeep Pokharel, Matthew P Padula, Jamie F Lu, et al.
Journal of Proteome Research|November 8, 2013
P159 from Mycoplasma hyopneumoniae binds porcine cilia and heparin and is cleaved in a manner akin to ectodomain sheddingBenjamin B A Raymond, Jessica L Tacchi, Veronica M Jarocki, et al.
Journal of Proteome Research|May 9, 2014
Cilium adhesin P216 (MHJ_0493) is a target of ectodomain shedding and aminopeptidase activity on the surface of Mycoplasma hyopneumoniaeJessica L Tacchi, Benjamin B A Raymond, Veronica M Jarocki, et al.
BMC Genomics|July 10, 2014
Proteogenomic mapping of Mycoplasma hyopneumoniae virulent strain 232Ken Pendarvis, Matthew P Padula, Jessica L Tacchi, et al.
Scientific Reports|September 13, 2017
N-terminomics identifies widespread endoproteolysis and novel methionine excision in a genome-reduced bacterial pathogenIain J Berry, Veronica M Jarocki, Jessica L Tacchi, et al.
Open Biology|January 16, 2015
MHJ_0461 is a multifunctional leucine aminopeptidase on the surface of Mycoplasma hyopneumoniaeVeronica M Jarocki, Jerran Santos, Jessica L Tacchi, et al.
Journal of Proteome Research|January 11, 2012
Mycoplasma hyopneumoniae Surface proteins Mhp385 and Mhp384 bind host cilia and glycosaminoglycans and are endoproteolytically processed by proteases that recognize different cleavage motifsAnia T Deutscher, Jessica L Tacchi, F Chris Minion, et al.
The Journal of Biological Chemistry|October 5, 2011
Sequence TTKF ↓ QE defines the site of proteolytic cleavage in Mhp683 protein, a novel glycosaminoglycan and cilium adhesin of Mycoplasma hyopneumoniaeDaniel R Bogema, Nichollas E Scott, Matthew P Padula, et al.
Pageof 2