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1,2-dimyristoyl-sn-phosphatidylinositol + H2O
?
-
poor substrate
-
-
?
6-(alpha-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol
6-(alpha-D-glucosaminyl)-1D-myo-inositol 1,2-cyclic phosphate + 1,2-diacyl-sn-glycerol
acetylcholinesterase
soluble acetylcholinesterase + 1,2-diacylglycerol
dimyristyl-P + H2O
?
-
-
-
-
?
glycosylated phosphatidylinositol + H2O
?
-
-
-
-
?
glycosylphosphatidylinositol-anchored protein
?
-
-
-
-
?
lipid A
?
-
biological precursor of variant-surface-glycoprotein glycolipid
-
-
?
membrane form variant surface glycoprotein + H2O
soluble variant surface glycoprotein + sn-1,2-dimyristoylglycerol
-
mfVSG, enzyme catalyzes the conversion of membrane form variant surface glycoproteins to soluble variant surface glycoproteins, with the release of sn-1,2-dimyristylglycerol
-
-
?
myristate-labeled variant-surface-glycoprotein
?
-
-
-
-
?
phosphatidylinositol
inositol 1,2-cyclic phosphate + inositol phosphate
pronase fragment + H2O
?
-
aspartylethanolamine-glycolipid moiety of mfVSG
-
-
?
pronase fragment of mfVSG + H2O
?
-
contains only the terminal amino acid and the glycolipid anchor
-
-
?
variant surface glycoprotein
?
variant-surface-glycoprotein
1,2-didecanoylglycerol + soluble variant-surface-glycoprotein
additional information
?
-
6-(alpha-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol
6-(alpha-D-glucosaminyl)-1D-myo-inositol 1,2-cyclic phosphate + 1,2-diacyl-sn-glycerol
-
-
-
-
?
6-(alpha-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol
6-(alpha-D-glucosaminyl)-1D-myo-inositol 1,2-cyclic phosphate + 1,2-diacyl-sn-glycerol
-
-
-
-
?
6-(alpha-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol
6-(alpha-D-glucosaminyl)-1D-myo-inositol 1,2-cyclic phosphate + 1,2-diacyl-sn-glycerol
-
the assay contains acetylcholinesterase
-
-
?
6-(alpha-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol
6-(alpha-D-glucosaminyl)-1D-myo-inositol 1,2-cyclic phosphate + 1,2-diacyl-sn-glycerol
-
-
-
-
?
acetylcholinesterase
soluble acetylcholinesterase + 1,2-diacylglycerol
-
isolated from bovine erythrocytes, does not act on membrane-bound forms but hydrolyzes the membrane-anchor from solubilized substrate
-
?
acetylcholinesterase
soluble acetylcholinesterase + 1,2-diacylglycerol
-
-
-
-
?
glycolipid A
?
-
is cleaved when Trypanosoma brucei encounters a mildly alkaline or hypotonic extracellular environment
-
-
?
glycolipid A
?
-
is cleaved when Trypanosoma brucei encounters a mildly alkaline or hypotonic extracellular environment
-
-
?
glycolipid Y
?
-
-
-
-
?
phosphatidylinositol
inositol 1,2-cyclic phosphate + inositol phosphate
-
-
-
?
phosphatidylinositol
inositol 1,2-cyclic phosphate + inositol phosphate
-
-
-
-
?
phosphatidylinositol
inositol 1,2-cyclic phosphate + inositol phosphate
-
-
-
-
?
phosphatidylinositol
inositol 1,2-cyclic phosphate + inositol phosphate
-
very poor substrate
-
-
?
phosphatidylinositol
inositol 1,2-cyclic phosphate + inositol phosphate
-
at 0.005 mM phosphatidylinositol, hydrolysis is maximal at 0.005% Triton X-100, at 1 mM phosphatidylinositol hydrolysis is maximal at 0.05% Triton X-100
-
-
?
variant surface glycoprotein
?
-
on exposure to mild alkali
-
-
?
variant surface glycoprotein
?
-
on exposure to mild alkali
-
-
?
variant-surface-glycoprotein
1,2-didecanoylglycerol + soluble variant-surface-glycoprotein
-
-
-
-
?
variant-surface-glycoprotein
1,2-didecanoylglycerol + soluble variant-surface-glycoprotein
-
peanut enzyme does not act on membrane-bound forms but hydrolyzes the membrane-anchor from solubilized substrate
-
-
?
variant-surface-glycoprotein
1,2-didecanoylglycerol + soluble variant-surface-glycoprotein
-
isolated from Trypanosoma brucei
-
-
?
variant-surface-glycoprotein
1,2-didecanoylglycerol + soluble variant-surface-glycoprotein
-
highly specific
-
-
?
variant-surface-glycoprotein
1,2-didecanoylglycerol + soluble variant-surface-glycoprotein
-
isolated from Trypanosoma equiperdum BoTat-1
-
-
?
variant-surface-glycoprotein
1,2-didecanoylglycerol + soluble variant-surface-glycoprotein
-
-
-
-
?
variant-surface-glycoprotein
1,2-didecanoylglycerol + soluble variant-surface-glycoprotein
-
-
-
-
?
variant-surface-glycoprotein
1,2-didecanoylglycerol + soluble variant-surface-glycoprotein
-
-
-
-
?
variant-surface-glycoprotein
1,2-didecanoylglycerol + soluble variant-surface-glycoprotein
-
-
i.e. 1,2-dimyristoylglycerol
?
variant-surface-glycoprotein
1,2-didecanoylglycerol + soluble variant-surface-glycoprotein
-
highly specific
i.e. 1,2-dimyristoylglycerol
?
variant-surface-glycoprotein
1,2-didecanoylglycerol + soluble variant-surface-glycoprotein
-
substrate is tethered to cell membrane by glycolipid moiety containing 1,2-dimyristoyl-sn-phosphatidylinositol
i.e. 1,2-dimyristoylglycerol
?
variant-surface-glycoprotein
1,2-didecanoylglycerol + soluble variant-surface-glycoprotein
-
enzyme activity is stimulated by acid-treatment of the cells
-
-
?
variant-surface-glycoprotein
1,2-didecanoylglycerol + soluble variant-surface-glycoprotein
-
phospholipase C-type hydrolysis
i.e. 1,2-dimyristoylglycerol
?
additional information
?
-
-
no substrates are phosphatidylcholine, phosphatidylserine, phosphatidylinositol 4-monophosphate, phosphatidylinositol 4,5-bisphosphate
-
-
?
additional information
?
-
-
glucosaminyl(alpha1-, 6)inositol is the crucial glycan moiety for substrate recognition
-
-
?
additional information
?
-
-
no substrate is 1-stearoyl-2-arachidonoyl-sn-phosphatidylinositol
-
-
?
additional information
?
-
-
does not digest glycolipid Z and glycolipid C
-
-
?
additional information
?
-
-
enzyme exhibits substantial specificity for molecules containing glycosylated phosphatidylinositol
-
-
?
additional information
?
-
-
GPI-PLC is a signalling enzyme, and DAG is a second messenger for GPI-PLC. Its enzyme activity is important for stimulating uptake of transferrin
-
-
?
additional information
?
-
-
[32P]phosphatidylinositol-4-phosphate, [32P]phosphatidylinositol 4,5-bisphosphate or [3H]phosphatidylcholine are not significantly hydrolyzed by the GPI-PLC
-
-
?
additional information
?
-
-
hippocampal detergent-resistant membranes: alpha2beta subunits of voltage-gated calcium channels, alpha2delta-1, alpha2delt-2, and alpha2delt-3, show all properties expected of GPI-anchored proteins, which are substrates for GPI-PLC
-
-
?
additional information
?
-
-
enzyme exhibits substantial specificity for molecules containing glycosylated phosphatidylinositol
-
-
?
additional information
?
-
-
[32P]phosphatidylinositol-4-phosphate, [32P]phosphatidylinositol 4,5-bisphosphate or [3H]phosphatidylcholine are not significantly hydrolyzed by the GPI-PLC
-
-
?
additional information
?
-
-
does not digest glycolipid Z and glycolipid C
-
-
?
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2-deoxy-2-fluoro-scyllo-inositol-1-O-dodecyl-phosphonic acid
cetrimide
-
i.e. alkyltrimethylammonium bromide, 0.3 mg/ml, neutral enzyme form
deoxycholate
-
neutral enzyme form, above 1 mg/ml, activation at 0.5-1 mg/ml
Glucosaminyl-alpha-1,6-2-deoxy-D-myo-inositol
-
i.e. compound VP-615L, more effective than VP-606L
Glucosaminyl-alpha-1,6-D-myo-inositol
-
i.e. compound VP-606L or 6-O-(2-amino-2-deoxy-alpha-D-glucopyranosyl)-D-myo-inositol
Glucosaminyl-alpha-1,6-D-myo-inositol 1,2-cyclic phosphate
-
i.e. compound VP-601L, product inhibition
Glucosaminyl-alpha-1,6-D-myo-inositol 1-dodecylphosphonate
-
i.e. compound VP-604L
Glucosaminyl-alpha-1,6-D-myo-inositol 1-hexylphosphonate
-
i.e. compound VFT-2
glucosaminyl-alpha-1,6-D-myo-inositol 1-phosphate
-
i.e. compound VP-600L
Hg2+
-
10 microM 100% inhibition, 1 microM 67% activity left
Inositol 1-dodecylphosphonate
-
i.e. compound VP-602L
Mannosyl-alpha-1,4-glucosaminyl-alpha-1,6-D-myo-inositol
-
i.e. O-alpha-D-mannopyranosyl-1,4-O-2-amino-2-deoxy-alpha-D-glucopyranosyl-1,6-D-myo-inositol
myo-inositol-1,2-cyclo-dodecyl-phosphonic acid
myo-inositol-1-O-dodecylphosphonic acid methylester
-
GPI-2349
N-(N,N-Dimethylcarbamyl)-glucosaminyl-alpha-1,6-D-myo-inositol
-
i.e. compound VC-109B, less effective than VP-606L
N-Acetylglucosaminyl-alpha-1,6-D-myo-inositol
-
i.e. compound VC-105B, weak
Nonidet P-40
-
above 0.1% w/v, neutral enzyme form
p-chloromercuriphenylsulfonic acid
phosphatidylcholine
-
weak
Triton X-100
-
0.05-0.5%, activation at 0.02%
2-deoxy-2-fluoro-scyllo-inositol-1-O-dodecyl-phosphonic acid
-
GPI-1793
2-deoxy-2-fluoro-scyllo-inositol-1-O-dodecyl-phosphonic acid
-
GPI-1793
Ca2+
-
activity of GPI-PLC exhibited small but significant inhibition in the presence of calcium ions, 70% activity left
EGTA
-
-
EGTA
-
Ca2+ reverses, only acidic, not neutral enzyme form
myo-inositol-1,2-cyclo-dodecyl-phosphonic acid
-
GPI-2350
myo-inositol-1,2-cyclo-dodecyl-phosphonic acid
-
GPI-2350
myo-inositol-1,2-cyclo-dodecyl-phosphonic acid
-
GPI-2350
p-chloromercuriphenylsulfonic acid
-
-
p-chloromercuriphenylsulfonic acid
-
strong, 5 mM
p-chloromercuriphenylsulfonic acid
-
-
Zn2+
-
-
Zn2+
-
100 microM 100% inhibition, 10 microM 59% activity left
additional information
-
no inhibition by 1,10-phenanthroline
-
additional information
-
no inhibition by Mn2+
-
additional information
-
low inhibition by 2-deoxy-2-fluoro-scyllo-inositol-1-O-dodecyl-phosphonic acid (GPI-1793) and very low inhibition by myo-inositol-1-O-dodecylphosphonic acid methylester (GPI-2349)
-
additional information
-
no inhibition by IAA
-
additional information
-
no inhibition by palmitate, myristate, phosphatidylethanolamine, inositol 1-phosphate, N-acetylglucosamine, ethanolamine, inositol, glucosamine, mannose, glucosaminyl-alpha-1,6-2-deoxy-D-myo-inositol 1-phosphate (i.e. VP-612L), glucosaminyl-alpha-1,6-2-deoxy-L-myo-inositol (i.e. VP-614L)
-
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C184S
-
fully active in vitro and still susceptible to p-chloromercuriphenylsulfonic acid
C24A
-
exhibits properties indistinguishable from the unmutated enzyme, in exiting glycosomes after exposure to pH 9.1 or hypotonic buffer
C24S
-
fully active in vitro and still susceptible to p-chloromercuriphenylsulfonic acid
C269-270-273S
-
33% activity of wild-type enzyme
C269C/C270S/C273S
-
exhibits activity in the range detected for the unmutated protein, localization in glycosome
C269S
-
fully active in vitro and still susceptible to p-chloromercuriphenylsulfonic acid
C269S/C270S/C273S
-
exhibits properties indistinguishable from the unmutated enzyme, in exiting glycosomes after exposure to pH 9.1 or hypotonic buffer
C270S
-
fully active in vitro and still susceptible to p-chloromercuriphenylsulfonic acid
C273S
-
fully active in vitro and still susceptible to p-chloromercuriphenylsulfonic acid
C332A
-
exhibits properties indistinguishable from the unmutated enzyme, in exiting glycosomes after exposure to pH 9.1 or hypotonic buffer
C332S
-
fully active in vitro and still susceptible to p-chloromercuriphenylsulfonic acid
C347S
-
fully active in vitro and still susceptible to p-chloromercuriphenylsulfonic acid
C80F
-
enzyme is inactive
C80S
-
fully active in vitro and still susceptible to p-chloromercuriphenylsulfonic acid
C80T
-
33% activity of wild-type enzyme, resistant to p-chloromercuriphenylsulfonic acid
H34Q
-
enzyme is totally inactive
Q81A
-
enzyme is inactive
Q81E
-
enzyme is inactive
Q81G
-
enzyme is inactive
Q81K
-
enzyme is inactive
Q81N
-
specific activity is 500fold decreased
C184A
-
exhibits properties indistinguishable from the unmutated enzyme, in exiting glycosomes after exposure to pH 9.1 or hypotonic buffer
-
C347A
-
can not exit glycosomes after treatment of cells expressing the protein with mild base or hypo-osmotic buffer
-
C80A
-
exhibits properties indistinguishable from the unmutated enzyme, in exiting glycosomes after exposure to pH 9.1 or hypotonic buffer
-
Q81L
-
fails to cleave glycosylphosphatidylinositols despite being transported from glycosomes to the endoplasmic reticulum after hypoosmotic or mild alkaline treatment of parasites, lacks enzyme activity
-
C184A
-
activity is not effected
C184A
-
exhibits activity in the range detected for the unmutated protein, deficiency of cell-associated gp63, localization in endo-lysosome
C184A
-
exhibits properties indistinguishable from the unmutated enzyme, in exiting glycosomes after exposure to pH 9.1 or hypotonic buffer
C269S/C270S
-
exhibits activity in the range detected for the unmutated protein, localization in glycosome
C269S/C270S
-
exhibits properties indistinguishable from the unmutated enzyme, in exiting glycosomes after exposure to pH 9.1 or hypotonic buffer
C269S/C273S
-
exhibits activity in the range detected for the unmutated protein, localization in glycosome
C269S/C273S
-
exhibits properties indistinguishable from the unmutated enzyme, in exiting glycosomes after exposure to pH 9.1 or hypotonic buffer
C270S/C273S
-
exhibits activity in the range detected for the unmutated protein, localization in glycosome
C270S/C273S
-
exhibits properties indistinguishable from the unmutated enzyme, in exiting glycosomes after exposure to pH 9.1 or hypotonic buffer
C347A
-
exhibits activity in the range detected for the unmutated protein, deficiency of cell-associated gp63, localization in endo-lysosome
C347A
-
can not exit glycosomes after treatment of cells expressing the protein with mild base or hypo-osmotic buffer
C80A
-
33% activity of wild-type enzyme, resistant to p-chloromercuriphenylsulfonic acid
C80A
-
exhibits activity in the range detected for the unmutated protein, localization in glycosome
C80A
-
exhibits properties indistinguishable from the unmutated enzyme, in exiting glycosomes after exposure to pH 9.1 or hypotonic buffer
Q81L
-
inactive
Q81L
-
catalytically inactive mutant
Q81L
-
enzyme is inactive
Q81L
-
fails to cleave glycosylphosphatidylinositols despite being transported from glycosomes to the endoplasmic reticulum after hypoosmotic or mild alkaline treatment of parasites, lacks enzyme activity
additional information
-
tetracyclin-inducible GPIPLC-gene, in conditional knock-out bloodstream forms and in procyclic cell line
additional information
-
PLC elimination construct, which yielded in a PLC null-mutant
additional information
-
PLC elimination construct, which yielded in a PLC null-mutant
additional information
-
generation of conditional knock-out bloodstraem forms
additional information
-
strain RUMP528, mutant GPI-PLC-/- cells, only 10% loss of alpha-toxin signal in cells exposed to hypo-osmotic buffer
additional information
-
strain RUMP528, mutant GPI-PLC-/- cells, only 10% loss of alpha-toxin signal in cells exposed to hypo-osmotic buffer
-
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Fox, J.A.; Duszenko, M.; Ferguson, M.A.J.; Low, M.G.; Cross, G.A.M.
Purification and characterization of a novel glycan-phosphatidylinositol-specific phospholipase C from Trypanosoma brucei
J. Biol. Chem.
261
15767-15771
1986
Trypanosoma brucei, Trypanosoma brucei 427
brenda
Hereld, D.; Krakow, J.L.; Bangs, J.D.; Hart, G.W.; Englund, P.T.
A phospholipase C from Trypanosoma brucei which selectively cleaves the glycolipid on the variant surface glycoprotein
J. Biol. Chem.
261
13813-13819
1986
Trypanosoma brucei
brenda
Fouchier, F.; Baltz, T.; Rougon, G.
Identification of glycosylphosphatidylinositol-specific phospholipases C in mouse brain membranes
Biochem. J.
269
321-327
1990
Mus musculus
brenda
Morris, J.C.; Ping-Sheng, L.; Shen, T.Y.; Mensa-Wilmot, K.
Glycan requirements of glycosylphosphatidylinositol phospholipase C from Trypanosoma brucei. Glucosaminylinositol derivatives inhibit phosphatidylinositol phospholipase C
J. Biol. Chem.
270
2517-2524
1995
Trypanosoma brucei
brenda
Butikofer, P.; Brodbeck, U.
Partial purification and characterization of a (glycosyl) inositol phospholipid-specific phospholipase C from peanut
J. Biol. Chem.
268
17794-17802
1993
Arachis hypogaea
brenda
Mller, G.; Grey, S.; Jung, C.; Bandlow, W.
Insulin-like signaling in yeast: modulation of protein phosphatase 2A, protein kinase A, cAMP-specific phosphodiesterase, and glycosyl-phosphatidylinositol-specific phospholipase C activities
Biochemistry
39
1475-1488
2000
Saccharomyces cerevisiae, Rattus norvegicus
brenda
Mller, G.; Deary, E.A.; Korndrfer, A.; Bandlow, W.
Stimulation of a glycosyl-phosphatidylinositol-specific phospholipase by insulin and the sulfonylurea, glimepiride, in rat adipocytes depends on increased glucose transport
J. Cell Biol.
126
1267-1276
1994
Rattus norvegicus
brenda
Mensa-Wilmot, K.; Morris, J.C.; Al-Qahtani, A.; Englund, P.T.
Purification and use of recombinant glycosylphosphatidylinositol-phospholipase C
Methods Enzymol.
250
641-655
1995
Trypanosoma brucei
brenda
Rolin, S.; Hanocq-Quertier, J.; Paturiaux-Hanocq, F.; Nolan, D.; Salmon, D.; Webb, H.; Carrington, M.; Voorheis, P.; Pays, E.
Simultaneous but independent activation of adenylate cyclase and glycosylphosphatidylinositol-phospholipase C under stress conditions in Trypanosoma brucei
J. Biol. Chem.
271
10844-10852
1996
Trypanosoma brucei
brenda
Webb, H.; Carnall, N.; Vanhamme, L.; Rolin, S.; Van Den Abbeele, J.; Welburn, S.; Pays, E.; Carrington, M.
The GPI-phospholipase C of Trypanosoma brucei is nonessential but influences parasitemia in mice
J. Cell. Biol.
139
103-114
1997
Trypanosoma brucei
brenda
Buetikofer, P.; Boschung, M.; Brodbeck, U.; Menon, A.K.
Phosphatidylinositol hydrolysis by Trypanosoma brucei glycosylphosphatidylinositol phospholipase C
J. Biol. Chem.
271
15533-15541
1996
Arachis hypogaea, Trypanosoma brucei
brenda
Carnall, N.; Webb, H.; Carrington, M.
Mutagenesis study of the glycosylphosphatidylinositol phospholipase C of Trypanosoma brucei
Mol. Biochem. Parasitol.
90
423-432
1997
Trypanosoma brucei
brenda
Carrington, M.; Carnall, N.; Crow, M.S.; Gaud, A.; Redpath, M.B.; Wasunna, C.L.; Webb, H.
The properties and function of the glycosylphosphatidylinositol-phospholipase C in Trypanosoma brucei
Mol. Biochem. Parasitol.
91
153-164
1998
Trypanosoma brucei
brenda
Rashid, M.B.; Russell, M.; Mensa-Wilmot, K.
Roles of Gln81 and Cys80 in catalysis by glycosylphosphatidylinositol-phospholipase C from Trypanosoma brucei
Eur. J. Biochem.
264
914-920
1999
Trypanosoma brucei
brenda
Armah, D.A.; Mensa-Wilmot, K.
S-myristoylation of a glycosylphosphatidylinositol-specific phospholipase C in Trypanosoma brucei
J. Biol. Chem.
274
5931-5938
1999
Trypanosoma brucei
brenda
Ochatt, C.M.; Buetikofer, P.; Navarro, M.; Wirtz, E.; Boschung, M.; Armah, D.; Cross, G.A.
Conditional expression of glycosylphosphatidylinositol phospholipase C in Trypanosoma brucei
Mol. Biochem. Parasitol.
103
35-48
1999
Trypanosoma brucei
brenda
Armah, D.A.; Mensa-Wilmot, K.
Tetramerization of glycosylphosphatidylinositol-specific phospholipase C from Trypanosoma brucei
J. Biol. Chem.
275
19334-19342
2000
Trypanosoma brucei
brenda
Paturiaux-Hanocq, F.; Hanocq-Quertier, J.; de Almeida, M.L.; Nolan, D.P.; Pays, A.; Vanhamme, L.; Van den Abbeele, J.; Wasunna, C.L.; Carrington, M.; Pays, E.
A role for the dynamic acylation of a cluster of cysteine residues in regulating the activity of the glycosylphosphatidylinositol-specific phospholipase C of Trypanosoma brucei
J. Biol. Chem.
275
12147-12155
2000
Trypanosoma brucei
brenda
Mller, G.; Schulz, A.; Wied, S.; Frick, W.
Regulation of lipid raft proteins by glimepiride- and insulin-induced glycosylphosphatidylinositol-specific phospholipase C in rat adipocytes
Biochem. Pharmacol.
69
761-780
2005
Bacillus cereus, Rattus norvegicus, Trypanosoma brucei
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Zheng, Z.; Butler, K.D.; Tweten, R.K.; Mensa-Wilmot, K.
Endosomes, glycosomes, and glycosylphosphatidylinositol catabolism in Leishmania major
J. Biol. Chem.
279
42106-42113
2004
Trypanosoma brucei
brenda
Gruszynski, A.E.; van Deursen, F.J.; Albareda, M.C.; Best, A.; Chaudhary, K.; Cliffe, L.J.; Del Rio, L.; Dunn, J.D.; Ellis, L.; Evans, K.J.; Figueiredo, J.M.; Malmquist, N.A.; Omosun, Y.; Palenchar, J.B.; Prickett, S.; Punkosdy, G.A.; van Dooren, G.; Wang, Q.; Menon, A.K.; Matthews, K.R.; Bangs, J.D.
Regulation of surface coat exchange by differentiating African trypanosomes
Mol. Biochem. Parasitol.
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2006
Trypanosoma brucei
brenda
Subramanya, S.; Mensa-Wilmot, K.
Regulated cleavage of intracellular glycosylphosphatidylinositol in a trypanosome. Peroxisome-to-endoplasmic reticulum translocation of a phospholipase C
FEBS J.
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2006
Trypanosoma brucei, Trypanosoma brucei 427
brenda
Subramanya, S.; Hardin, C.F.; Steverding, D.; Mensa-Wilmot, K.
Glycosylphosphatidylinositol-specific phospholipase C regulates transferrin endocytosis in the African trypanosome
Biochem. J.
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685-694
2009
Trypanosoma brucei
brenda
Mueller, G.; Wied, S.; Jung, C.; Over, S.
Hydrogen peroxide-induced translocation of glycolipid-anchored (c)AMP-hydrolases to lipid droplets mediates inhibition of lipolysis in rat adipocytes
Br. J. Pharmacol.
154
901-913
2008
Rattus norvegicus
brenda
Subramanya, S.; Armah, D.A.; Mensa-Wilmot, K.
Trypanosoma brucei: reduction of GPI-phospholipase C protein during differentiation is dependent on replication of newly transformed cells
Exp. Parasitol.
125
222-229
2010
Trypanosoma brucei
brenda
Davies, A.; Kadurin, I.; Alvarez-Laviada, A.; Douglas, L.; Nieto-Rostro, M.; Bauer, C.S.; Pratt, W.S.; Dolphin, A.C.
The alpha2delta subunits of voltage-gated calcium channels form GPI-anchored proteins, a posttranslational modification essential for function
Proc. Natl. Acad. Sci. USA
107
1654-1659
2010
Trypanosoma brucei
brenda
Xing, Y.; Gu, Y.; Xu, L.C.; Siedlecki, C.A.; Donahue, H.J.; You, J.
Effects of membrane cholesterol depletion and GPI-anchored protein reduction on osteoblastic mechanotransduction
J. Cell. Physiol.
226
2350,235-9
2010
Mus musculus
brenda
Sunter, J.; Webb, H.; Carrington, M.
Determinants of GPI-PLC localisation to the flagellum and access to GPI-anchored substrates in trypanosomes
PLoS Pathog.
9
e1003566
2013
Trypanosoma brucei, Trypanosoma brucei 427, Trypanosoma congolense
brenda
Van Veen, M.; Matas-Rico, E.; van de Wetering, K.; Leyton-Puig, D.; Kedziora, K.; de Lorenzi, V.; Stijf-Bultsma, Y.; van den Broek, B.; Jalink, K.; Sidenius, N.; Perrakis, A.; Moolenaar, W.
Negative regulation of urokinase receptor activity by a GPI-specific phospholipase C in breast cancer cells
eLife
6
e23649
2017
Homo sapiens (Q9HCC8)
brenda