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Abz-Asp-Tyr-Val-Ala-Ser-Glu-Lys(Dnp) + H2O
?
-
-
-
?
Abz-Gly-Ile-Val-Arg-Ala-Lys(Dnp) + H2O
?
-
-
-
?
Abz-Lys-Asp-Glu-Ser-Tyr-Arg-Lys(Dnp) + H2O
?
-
-
-
?
Abz-Thr-Val-Leu-Glu-Arg-Ser-Lys(Dnp) + H2O
?
-
-
-
?
Abz-Tyr-Gly-Lys-Arg-Val-Phe-Lys(Dnp) + H2O
?
-
-
-
?
Abz-Val-Lys-Phe-Tyr-Asp-Ile-Lys(Dnp) + H2O
?
-
-
-
?
acetyl-Ala-Lys-Lys-Ala-Lys-Leu-Thr-Ala-Leu-Val-NMe + H2O
?
-
-
-
?
Actin + H2O
Fragements of actin
-
initial cleavage at Gly-Met, followed by Thr-Leu
-
?
AGLRRAALGG + H2O
AGLRRAA + LGG
-
-
-
?
alpha1-proteinase inhibitor + H2O
?
-
-
-
-
?
azocasein + H2O
?
-
-
-
?
Azocoll + H2O
Fragements of azocoll
-
-
-
?
azocollagen + H2O
?
-
-
-
?
beta-catenin + H2O
?
-
-
-
?
BODIPY FL-casein + H2O
?
-
-
-
?
collagen type IV + H2O
?
-
-
-
-
?
Fibrinogen + H2O
Fragements of fibrinogen
-
hydrolysis to a lesser degree than other substrates
-
?
Fibronectin + H2O
?
-
-
-
?
Fragilysin + H2O
Fragements of fragilysisn
-
autodigestion
-
?
Gelatin + H2O
?
-
-
-
-
?
Gelatin + H2O
Fragements of gelatin
-
-
-
?
human complement C3 + H2O
?
-
-
-
-
?
Mca-Arg-Pro-Lys-Pro-Val-Glu-Nva-Trp-Arg-Lys(Dnp)-NH2 + H2O
?
-
-
-
?
Mca-Pro-Leu-Gly-Leu-Dap(Dnp)-Ala-Arg-NH2 + H2O
?
-
-
-
?
p-phenylazobenzyl-oxycarbonyl-Pro-Leu-Gly-Pro-D-Arg + H2O
?
-
-
-
-
?
PTKIYDNIYD + H2O
PTKIY + DNIYD
-
-
-
?
SGHMAALTA + H2O
SGHMAA + LTA
-
-
-
?
SGPMSLRMTA + H2O
SGPMSLR + MTA
-
-
-
?
SGPRSLKSTA + H2O
SGPRSLK + STA
-
-
-
?
SGPVSMRYTA + H2O
SGPVSMR + YTA
-
-
-
?
tropomyosin + H2O
?
-
-
-
-
?
Tropomyosin + H2O
Fragements of tropomyosin
-
hydrolysis to a lesser degree than other substrates
-
?
VE-cadherin + H2O
?
-
-
-
-
?
additional information
?
-
actin + H2O
?
-
-
-
-
?
E-cadherin + H2O
?
-
-
-
-
?
E-cadherin + H2O
?
-
-
-
?
E-cadherin + H2O
?
-
-
-
-
?
E-cadherin + H2O
?
cleavage of the zonula adherens protein
-
?
E-cadherin + H2O
?
-
cleaves the extracellular domain
-
-
?
E-cadherin + H2O
?
-
neither human nor rat E-cadherin are the cellular receptor for BFT
-
-
?
E-cadherin + H2O
?
the enzyme hydrolyzes the extracellular domain of several protein substrate, e.g. of E-cadherin to interrupt the intercellular adhesion increasing the permeability of the epithelium, and causing intracellular redistribution of actin with morphologic changes and release of beta-catenin
-
-
?
E-cadherin + H2O
?
the enzyme hydrolyzes the extracellular domain of the substrate
-
-
?
E-cadherin + H2O
?
in vivo substrate
-
-
?
E-cadherin + H2O
?
recombinant fragilysin isoforms cause E-cadherin cleavage of intact cells and do not cleave isolated E-cadherin
-
-
?
E-cadherin + H2O
?
-
the enzyme cleaves the extracellular domain of E-cadherin. Its cleavage then releases beta-catenin associated with the cytoplasmic domain of E-cadherin
-
-
?
E-cadherin + H2O
?
-
-
-
?
E-cadherin + H2O
?
-
neither human nor rat E-cadherin are the cellular receptor for BFT
-
-
?
Fibrinogen + H2O
?
-
-
-
-
?
Fibrinogen + H2O
?
-
-
-
?
Fibrinogen + H2O
?
-
-
-
?
Proteins + H2O
?
-
the enzyme increases the paracellular permeability of the intestinal epithelium by digestion of the intestinal light junctions and cell-to-cell contacts, it does not disrupt cell membranes
-
-
?
Proteins + H2O
?
-
proteolytic action on the actin of the cytoskeleton
-
-
?
Proteins + H2O
?
-
active in lamb, rabbit, rat ileum and colon, it causes the production of fluids and hemorrhage, it increases the levels of Na+ and Cl- in intestinal loops due to tissue damage
-
-
?
additional information
?
-
-
cleaves at Cys-Leu, Ser-Leu, Thr-Leu, Gly-Leu or Leu-Gly peptide bonds in a number of proteins
-
-
?
additional information
?
-
the cytopathic effect of the enzyme is only seen in cells that can form tight junction and polarized monolayers, the enzyme affects the barrier function of the epithelium and decreases the transpithelial electrical resistance of monolayers, overview, the enzyme stimulates the recruitment of polymorphs to the lamina propria and seceretion of interleukin-8, epithelial neutrophil-activating peptide-78, and growth-related oncogene-alpha from colonocytes, overview
-
-
?
additional information
?
-
the cytopathic effect of the enzyme is only seen in cells that can form tight junction and polarized monolayers, the enzyme affects the barrier function of the epithelium and decreases the transpithelial electrical resistance of monolayers, overview, the enzyme stimulates the recruitment of polymorphs to the lamina propria and seceretion of interleukin-8, epithelial neutrophil-activating peptide-78, and growth-related oncogene-alpha from colonocytes, overview
-
-
?
additional information
?
-
the cytopathic effect of the enzyme is only seen in cells that can form tight junction and polarized monolayers, the enzyme affects the barrier function of the epithelium and decreases the transpithelial electrical resistance of monolayers, overview, the enzyme stimulates the recruitment of polymorphs to the lamina propria and seceretion of interleukin-8, epithelial neutrophil-activating peptide-78, and growth-related oncogene-alpha from colonocytes, overview
-
-
?
additional information
?
-
-
the cytopathic effect of the enzyme is only seen in cells that can form tight junction and polarized monolayers, the enzyme affects the barrier function of the epithelium and decreases the transpithelial electrical resistance of monolayers, overview, the enzyme stimulates the recruitment of polymorphs to the lamina propria and seceretion of interleukin-8, epithelial neutrophil-activating peptide-78, and growth-related oncogene-alpha from colonocytes, overview
-
-
?
additional information
?
-
the cytopathic effect of the enzyme is only seen in cells that can form tight junction and polarized monolayers, the enzyme affects the barrier function of the epithelium and decreases the transpithelial electrical resistance of monolayers, overview, the enzyme stimulates the recruitment of polymorphs to the lamina propria and secretion of interleukin-8, epithelial neutrophil-activating peptide-78, and growth-related oncogene-alpha from colonocytes, overview
-
-
?
additional information
?
-
the cytopathic effect of the enzyme is only seen in cells that can form tight junction and polarized monolayers, the enzyme affects the barrier function of the epithelium and decreases the transpithelial electrical resistance of monolayers, overview, the enzyme stimulates the recruitment of polymorphs to the lamina propria and secretion of interleukin-8, epithelial neutrophil-activating peptide-78, and growth-related oncogene-alpha from colonocytes, overview
-
-
?
additional information
?
-
the cytopathic effect of the enzyme is only seen in cells that can form tight junction and polarized monolayers, the enzyme affects the barrier function of the epithelium and decreases the transpithelial electrical resistance of monolayers, overview, the enzyme stimulates the recruitment of polymorphs to the lamina propria and secretion of interleukin-8, epithelial neutrophil-activating peptide-78, and growth-related oncogene-alpha from colonocytes, overview
-
-
?
additional information
?
-
-
the cytopathic effect of the enzyme is only seen in cells that can form tight junction and polarized monolayers, the enzyme affects the barrier function of the epithelium and decreases the transpithelial electrical resistance of monolayers, overview, the enzyme stimulates the recruitment of polymorphs to the lamina propria and secretion of interleukin-8, epithelial neutrophil-activating peptide-78, and growth-related oncogene-alpha from colonocytes, overview
-
-
?
additional information
?
-
-
the enterotoxin has cytotoxic activity, however strains isolated from stool samples of calves with diarrhea contain the gene bft, but do not show cytotoxic activity against HT29 cells, overview
-
-
?
additional information
?
-
fragilysin is a zinc metalloprotease toxin with a C-terminal zinc-binding protease domain
-
-
?
additional information
?
-
fragilysin is a zinc metalloprotease toxin with a C-terminal zinc-binding protease domain
-
-
?
additional information
?
-
fragilysin is a zinc metalloprotease toxin with a C-terminal zinc-binding protease domain
-
-
?
additional information
?
-
-
fragilysin is a zinc metalloprotease toxin with a C-terminal zinc-binding protease domain
-
-
?
additional information
?
-
isozyme fargilysin-3 does not cleave azoalbumin
-
-
?
additional information
?
-
-
isozyme fargilysin-3 does not cleave azoalbumin
-
-
?
additional information
?
-
-
azocoll, azocasein and gelatin are not proteolytically cleaved by mature fragilysin-2
-
-
?
additional information
?
-
does not cleave GHSRRSRRSG
-
-
?
additional information
?
-
-
does not cleave GHSRRSRRSG
-
-
?
additional information
?
-
the recombinant enzyme does not cleave thioredoxin, gelatin, azocoll or azocasein both with and without Zn2+ ions
-
-
?
additional information
?
-
-
the recombinant enzyme does not cleave thioredoxin, gelatin, azocoll or azocasein both with and without Zn2+ ions
-
-
?
additional information
?
-
-
the enzyme does not demonstrate hemagglutination activity
-
-
?
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Fibrinogen + H2O
?
-
-
-
?
VE-cadherin + H2O
?
-
-
-
-
?
additional information
?
-
E-cadherin + H2O
?
-
-
-
-
?
E-cadherin + H2O
?
-
-
-
?
E-cadherin + H2O
?
cleavage of the zonula adherens protein
-
?
E-cadherin + H2O
?
the enzyme hydrolyzes the extracellular domain of several protein substrate, e.g. of E-cadherin to interrupt the intercellular adhesion increasing the permeability of the epithelium, and causing intracellular redistribution of actin with morphologic changes and release of beta-catenin
-
-
?
E-cadherin + H2O
?
in vivo substrate
-
-
?
E-cadherin + H2O
?
-
the enzyme cleaves the extracellular domain of E-cadherin. Its cleavage then releases beta-catenin associated with the cytoplasmic domain of E-cadherin
-
-
?
Proteins + H2O
?
-
the enzyme increases the paracellular permeability of the intestinal epithelium by digestion of the intestinal light junctions and cell-to-cell contacts, it does not disrupt cell membranes
-
-
?
Proteins + H2O
?
-
proteolytic action on the actin of the cytoskeleton
-
-
?
Proteins + H2O
?
-
active in lamb, rabbit, rat ileum and colon, it causes the production of fluids and hemorrhage, it increases the levels of Na+ and Cl- in intestinal loops due to tissue damage
-
-
?
additional information
?
-
the cytopathic effect of the enzyme is only seen in cells that can form tight junction and polarized monolayers, the enzyme affects the barrier function of the epithelium and decreases the transpithelial electrical resistance of monolayers, overview, the enzyme stimulates the recruitment of polymorphs to the lamina propria and seceretion of interleukin-8, epithelial neutrophil-activating peptide-78, and growth-related oncogene-alpha from colonocytes, overview
-
-
?
additional information
?
-
the cytopathic effect of the enzyme is only seen in cells that can form tight junction and polarized monolayers, the enzyme affects the barrier function of the epithelium and decreases the transpithelial electrical resistance of monolayers, overview, the enzyme stimulates the recruitment of polymorphs to the lamina propria and seceretion of interleukin-8, epithelial neutrophil-activating peptide-78, and growth-related oncogene-alpha from colonocytes, overview
-
-
?
additional information
?
-
the cytopathic effect of the enzyme is only seen in cells that can form tight junction and polarized monolayers, the enzyme affects the barrier function of the epithelium and decreases the transpithelial electrical resistance of monolayers, overview, the enzyme stimulates the recruitment of polymorphs to the lamina propria and seceretion of interleukin-8, epithelial neutrophil-activating peptide-78, and growth-related oncogene-alpha from colonocytes, overview
-
-
?
additional information
?
-
-
the cytopathic effect of the enzyme is only seen in cells that can form tight junction and polarized monolayers, the enzyme affects the barrier function of the epithelium and decreases the transpithelial electrical resistance of monolayers, overview, the enzyme stimulates the recruitment of polymorphs to the lamina propria and seceretion of interleukin-8, epithelial neutrophil-activating peptide-78, and growth-related oncogene-alpha from colonocytes, overview
-
-
?
additional information
?
-
the cytopathic effect of the enzyme is only seen in cells that can form tight junction and polarized monolayers, the enzyme affects the barrier function of the epithelium and decreases the transpithelial electrical resistance of monolayers, overview, the enzyme stimulates the recruitment of polymorphs to the lamina propria and secretion of interleukin-8, epithelial neutrophil-activating peptide-78, and growth-related oncogene-alpha from colonocytes, overview
-
-
?
additional information
?
-
the cytopathic effect of the enzyme is only seen in cells that can form tight junction and polarized monolayers, the enzyme affects the barrier function of the epithelium and decreases the transpithelial electrical resistance of monolayers, overview, the enzyme stimulates the recruitment of polymorphs to the lamina propria and secretion of interleukin-8, epithelial neutrophil-activating peptide-78, and growth-related oncogene-alpha from colonocytes, overview
-
-
?
additional information
?
-
the cytopathic effect of the enzyme is only seen in cells that can form tight junction and polarized monolayers, the enzyme affects the barrier function of the epithelium and decreases the transpithelial electrical resistance of monolayers, overview, the enzyme stimulates the recruitment of polymorphs to the lamina propria and secretion of interleukin-8, epithelial neutrophil-activating peptide-78, and growth-related oncogene-alpha from colonocytes, overview
-
-
?
additional information
?
-
-
the cytopathic effect of the enzyme is only seen in cells that can form tight junction and polarized monolayers, the enzyme affects the barrier function of the epithelium and decreases the transpithelial electrical resistance of monolayers, overview, the enzyme stimulates the recruitment of polymorphs to the lamina propria and secretion of interleukin-8, epithelial neutrophil-activating peptide-78, and growth-related oncogene-alpha from colonocytes, overview
-
-
?
additional information
?
-
-
the enterotoxin has cytotoxic activity, however strains isolated from stool samples of calves with diarrhea contain the gene bft, but do not show cytotoxic activity against HT29 cells, overview
-
-
?
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Kling, J.J.; Wright, R.L.; Moncrief, J.S.; Wilkins, T.D.
Cloning and characterization of the gene for the metalloprotease enterotoxin of Bacteroides fragilis
FEMS Microbiol. Lett.
146
279-284
1997
Bacteroides fragilis
brenda
Moncrief, J.S.; Obisco, R.; Barroso, L.A.; Kling, J.J.; Wright, R.L.; van Tassell, R.L.; Lyerly, D.M.; Wilkins, T.D.
The enterotoxin of Bacteroides fragilis is a metalloprotease
Infect. Immun.
63
175-181
1995
Bacteroides fragilis
brenda
Obisco, R.J.; Lyerly, D.M.; van Tassell, R.L.; Wilkins, R.D.
Proteolytic activity of Bacteroides fragilis enterotoxin causes fluid secretion and intestinal damage in vivo
Infect. Immun.
63
3820-3826
1995
Bacteroides fragilis
brenda
Obisco, R.J.; Bevan, D.R.; Wilkins, T.D.
Molecular modeling and analysis of fragilysin, the Bacteroides fragilis toxin
Clin. Infect. Dis.
25
S153-155
1997
Bacteroides fragilis
brenda
Mundy, L.M.; Sears, C.L.
Detection of toxin production by Bacteroides fragilis: assay development and screening of extraintestinal clinical isolates
Clin. Infect. Dis.
23
269-276
1996
Bacteroides fragilis
brenda
Moncrief, J.S.; Duncan, A.J.; Wright, R.L.; Barroso, L.A.; Wilkins, T.D.
Molecular characterization of the fragilysin pathogenicity islet of enterotoxigenic Bacteroides fragilis
Infect. Immun.
66
1735-1739
1998
Bacteroides fragilis
brenda
Obisco, R.J.; Azghani, A.O.; Wilkins, T.D.
The Bacteroides fragilis toxin fragilysin disrupts the paracellular barrier of epitheliar cells
Infect. Immun.
65
1431-1439
1997
Bacteroides fragilis
brenda
Van Tassell, R.L.; Lyerly, D.M.; Wilkins, T.D.
Purification and characterization of an enterotoxin from Bacteroides fragilis
Infect. Immun.
60
1343-1350
1992
Bacteroides fragilis
brenda
Donelli, G.; Fabbri, A.; Florentini, C.
Bacteroides fragilis enterotoxin induces cytoskeletal changes and surface blebbing in HT-29 cells
Infect. Immun.
64
113-119
1996
Bacteroides fragilis
brenda
Kato, N.; Liu, C.X.; Kato, H.; Watanabe, K.; Tanaka, Y.; Yamamoto, T.; Suzuki, K.; Ueno, K.
A new subtype of the metalloprotease toxin gene and the incidence of the three bft subtypes among Bacteroides fragilis isolates in Japan
FEMS Microbiol. Lett.
182
171-176
2000
Bacteroides fragilis
brenda
Chung, G.T.; Franco, A.A.; Wu, S.; Rhie, G.E.; Cheng, R.; Oh, H.B.; Sears, C.L.
Identification of a third metalloprotease toxin gene in extraintestinal isolates of Bacteroides fragilis
Infect. Immun.
67
4945-4949
1999
Bacteroides fragilis (O86049), Bacteroides fragilis
brenda
Wu, S.; Dreyfus, L.A.; Tzianabos, A.O.; Hayashi, C.; Sears, C.L.
Diversity of the metalloprotease toxin produced by enterotoxigenic Bacteroides fragilis
Infect. Immun.
70
2463-2471
2002
Bacteroides fragilis
brenda
Ulger Toprak, N.; Rajendram, D.; Yagci, A.; Gharbia, S.; Shah, H.N.; Gulluoglu, B.M.; Akin, L.M.; Demirkalem, P.; Celenk, T.; Soyletir, G.
The distribution of the bft alleles among enterotoxigenic Bacteroides fragilis strains from stool specimens and extraintestinal sites
Anaerobe
12
71-74
2006
Bacteroides fragilis, Bacteroides fragilis NCTC 11295
brenda
Vines, R.R.; Wilkins, T.D.
Fragilysin
Handbook Of Proteolytic Enzymes(Barrett,A. J. ,Rawlings,N. D. ,Woessner,J. F. ,Eds. )Academic Press
1
588-591
2004
Bacteroides fragilis
-
brenda
Wu, S.; Powell, J.; Mathioudakis, N.; Kane, S.; Fernandez, E.; Sears, C.L.
Bacteroides fragilis enterotoxin induces intestinal epithelial cell secretion of interleukin-8 through mitogen-activated protein kinases and a tyrosine kinase-regulated nuclear factor-kappaB pathway
Infect. Immun.
72
5832-5839
2004
Bacteroides fragilis, Bacteroides fragilis 086-5443-2-2
brenda
Franco, A.A.; Buckwold, S.L.; Shin, J.W.; Ascon, M.; Sears, C.L.
Mutation of the zinc-binding metalloprotease motif affects Bacteroides fragilis toxin activity but does not affect propeptide processing
Infect. Immun.
73
5273-5277
2005
Bacteroides fragilis
brenda
Wu, S.; Shin, J.; Zhang, G.; Cohen, M.; Franco, A.; Sears, C.L.
The Bacteroides fragilis toxin binds to a specific intestinal epithelial cell receptor
Infect. Immun.
74
5382-5390
2006
Bacteroides fragilis, Bacteroides fragilis I-1345
brenda
Sears, C.L.; Buckwold, S.L.; Shin, J.W.; Franco, A.A.
The C-terminal region of Bacteroides fragilis toxin is essential to its biological activity
Infect. Immun.
74
5595-5601
2006
Bacteroides fragilis
brenda
Holton, J.
Enterotoxigenic Bacteroides fragilis
Curr. Infect. Dis. Rep.
10
99-104
2008
Bacteroides fragilis (O05091), Bacteroides fragilis (O86049), Bacteroides fragilis (Q9S5W0), Bacteroides fragilis
brenda
Almeida, F.S.; Nakano, V.; Avila-Campos, M.J.
Occurrence of enterotoxigenic and nonenterotoxigenic Bacteroides fragilis in calves and evaluation of their antimicrobial susceptibility
FEMS Microbiol. Lett.
272
15-21
2007
Bacteroides fragilis
brenda
Kim, J.M.; Lee, D.H.; Kim, J.S.; Lee, J.Y.; Park, H.G.; Kim, Y.J.; Oh, Y.K.; Jung, H.C.; Kim, S.I.
5,7-dihydroxy-3,4,6-trimethoxyflavone inhibits the inflammatory effects induced by Bacteroides fragilis enterotoxin via dissociating the complex of heat shock protein 90 and I kappaB alpha and I kappaB kinase-gamma in intestinal epithelial cell culture
Clin. Exp. Immunol.
155
541-551
2009
Bacteroides fragilis
brenda
Kim, J.M.; Lee, J.Y.; Kim, Y.J.
Inhibition of apoptosis in Bacteroides fragilis enterotoxin-stimulated intestinal epithelial cells through the induction of c-IAP-2
Eur. J. Immunol.
38
2190-2199
2008
Bacteroides fragilis
brenda
Rhee, K.J.; Wu, S.; Wu, X.; Huso, D.L.; Karim, B.; Franco, A.A.; Rabizadeh, S.; Golub, J.E.; Mathews, L.E.; Shin, J.; Sartor, R.B.; Golenbock, D.; Hamad, A.R.; Gan, C.M.; Housseau, F.; Sears, C.L.
Induction of persistent colitis by a human commensal, enterotoxigenic Bacteroides fragilis, in wild-type C57BL/6 mice
Infect. Immun.
77
1708-1718
2009
Bacteroides fragilis
brenda
Yoon, Y.M.; Lee, J.Y.; Yoo, D.; Sim, Y.S.; Kim, Y.J.; Oh, Y.K.; Kang, J.S.; Kim, S.; Kim, J.S.; Kim, J.M.
Bacteroides fragilis enterotoxin induces human beta-defensin-2 expression in intestinal epithelial cells via a mitogen-activated protein kinase/I kappaB kinase/NF-kappaB-dependent pathway
Infect. Immun.
78
2024-2033
2010
Bacteroides fragilis
brenda
Roh, H.C.; Yoo, d.o..Y.; Ko, S.H.; Kim, Y.J.; Kim, J.M.
Bacteroides fragilis enterotoxin upregulates intercellular adhesion molecule-1 in endothelial cells via an aldose reductase-, MAPK-, and NF-kappaB-dependent pathway, leading to monocyte adhesion to endothelial cells
J. Immunol.
187
1931-1941
2011
Bacteroides fragilis
brenda
Goodwin, A.C.; Destefano Shields, C.E.; Wu, S.; Huso, D.L.; Wu, X.; Murray-Stewart, T.R.; Hacker-Prietz, A.; Rabizadeh, S.; Woster, P.M.; Sears, C.L.; Casero, R.A.
Polyamine catabolism contributes to enterotoxigenic Bacteroides fragilis-induced colon tumorigenesis
Proc. Natl. Acad. Sci. USA
108
15354-15359
2011
Bacteroides fragilis, Bacteroides fragilis 86-5443-2-2
brenda
Goulas, T.; Arolas, J.L.; Gomis-Rueth, F.X.
Structure, function and latency regulation of a bacterial enterotoxin potentially derived from a mammalian adamalysin/ADAM xenolog
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Kharlampieva, D.; Manuvera, V.; Podgorny, O.; Kovalchuk, S.; Pobeguts, O.; Altukhov, I.; Alexeev, D.; Lazarev, V.; Govorun, V.
Purification and characterisation of recombinant Bacteroides fragilis toxin-2
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Bacteroides fragilis
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Shiryaev, S.; Aleshin, A.; Muranaka, N.; Kukreja, M.; Routenberg, D.; Remacle, A.; Liddington, R.; Cieplak, P.; Kozlov, I.; Strongin, A.
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Bacteroides fragilis (O86049), Bacteroides fragilis
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Shiryaev, S.; Remacle, A.; Chernov, A.; Golubkov, V.; Motamedchaboki, K.; Muranaka, N.; Dambacher, C.; Capek, P.; Kukreja, M.; Kozlov, I.; Perucho, M.; Cieplak, P.; Strongin, A.
Substrate cleavage profiling suggests a distinct function of Bacteroides fragilis metalloproteinases (fragilysin and metalloproteinase II) at the microbiome-inflammation-cancer interface
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Bacteroides fragilis (O86049), Bacteroides fragilis
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Bacteroides fragilis (O86049), Bacteroides fragilis
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Kharlampieva, D.; Manuvera, V.; Podgorny, O.; Grafskaia, E.; Kovalchuk, S.; Pobeguts, O.; Altukhov, I.; Govorun, V.; Lazarev, V.
Recombinant fragilysin isoforms cause E-cadherin cleavage of intact cells and do not cleave isolated E-cadherin
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Bacteroides fragilis (O86049), Bacteroides fragilis
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Herrou, J.; Choi, V.M.; Bubeck Wardenburg, J.; Crosson, S.
Activation Mechanism of the Bacteroides fragilis cysteine peptidase, fragipain
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Bacteroides fragilis
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Zakharzhevskaya, N.B.; Tsvetkov, V.B.; Vanyushkina, A.A.; Varizhuk, A.M.; Rakitina, D.V.; Podgorsky, V.V.; Vishnyakov, I.E.; Kharlampieva, D.D.; Manuvera, V.A.; Lisitsyn, F.V.; Gushina, E.A.; Lazarev, V.N.; Govorun, V.M.
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Bacteroides fragilis
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Jeon, J.I.; Ko, S.H.; Kim, J.M.
Intestinal epithelial cells exposed to Bacteroides fragilis enterotoxin regulates NF-kappaB activation and inflammatory responses through beta-catenin expression
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Bacteroides fragilis
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Choi, V.M.; Herrou, J.; Hecht, A.L.; Teoh, W.P.; Turner, J.R.; Crosson, S.; Bubeck Wardenburg, J.
Activation of Bacteroides fragilis toxin by a novel bacterial protease contributes to anaerobic sepsis in mice
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Bacteroides fragilis ATCC 43858 (A0A164V5U8)
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Lv, Y.; Ye, T.; Wang, H.P.; Zhao, J.Y.; Chen, W.J.; Wang, X.; Shen, C.X.; Wu, Y.B.; Cai, Y.K.
Suppression of colorectal tumorigenesis by recombinant Bacteroides fragilis enterotoxin-2 in vivo
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Bacteroides fragilis
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