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R440A
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essential residue in catalysis
N345L
the mutation results in 93% reduction in LAP activity
N345Q
the mutation results in 72% reduction in LAP activity
N435E
the mutation results in complete loss of the LAP activity
N435L
the mutation results in complete loss of the LAP activity
N435Q
the mutation results in complete loss of the LAP activity
N435R
the mutation results in complete loss of the LAP activity
D375A
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leukotriene A4 hydrolase mutant
K528A
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gene A-LAP, site-directed mutagenesis, the mutant enzyme shows reduced activity
K528H
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gene A-LAP, site-directed mutagenesis, the mutant enzyme shows reduced activity
K528M
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gene A-LAP, site-directed mutagenesis, the mutant enzyme shows reduced activity
E343A
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site-directed mutagenesis, inactive, dominant-negative mutant
E365A
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site-directed mutagenesis, inactive mutant
K310V
increased specificty for Leu as Xaa, no activity with Asp-Leu in opposite to the wild-type enzyme
R402W
reduced activity with Asp-Leu compared to the wild-type enzyme
D347G
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oligonucleotide site-directed mutagenesis, formation of a stable hexamer corresponding to the wild-type enzyme, nearly catalytically inactive with dipeptide substrates
D347I
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oligonucleotide site-directed mutagenesis, no formation of stable hexamer, inactive mutant
D347S
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oligonucleotide site-directed mutagenesis, no formation of stable hexamer, inactive mutant
D347V
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oligonucleotide site-directed mutagenesis, no formation of stable hexamer, inactive mutant
D347Y
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oligonucleotide site-directed mutagenesis, formation of a more complex structure compared to the wild-type enzyme
D354E
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oligonucleotide site-directed mutagenesis, no formation of stable hexamer, inactive mutant
D354M
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oligonucleotide site-directed mutagenesis, reduced catalytic activity with dipeptide substrates compared to the wild-type
D354R
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oligonucleotide site-directed mutagenesis, no formation of stable hexamer, reduced catalytic activity with dipeptide substrates compared to the wild-type
E429A
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oligonucleotide site-directed mutagenesis, no formation of stable hexamer, inactive mutant
E429G
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oligonucleotide site-directed mutagenesis, no formation of stable hexamer, inactive mutant
E429Q
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oligonucleotide site-directed mutagenesis, no formation of stable hexamer, inactive mutant
E429R
inactive mutant with disrupted hexameric structure has increased chaperone activity
E429S
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oligonucleotide site-directed mutagenesis, formation of a stable hexamer corresponding to the wild-type enzyme
E429W
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oligonucleotide site-directed mutagenesis, formation of a stable hexamer corresponding to the wild-type enzyme, nearly catalytically inactive with dipeptide substrates
E429X
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site-directed mutagenesis, inactive mutants, overview
K354G
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oligonucleotide site-directed mutagenesis, formation of a more complex structure compared to the wild-type enzyme
K354M
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oligonucleotide site-directed mutagenesis, formation of a more complex structure compared to the wild-type enzyme
K354N
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oligonucleotide site-directed mutagenesis, formation of a more complex structure compared to the wild-type enzyme
K354T
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oligonucleotide site-directed mutagenesis, formation of a more complex structure compared to the wild-type enzyme
K354W
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oligonucleotide site-directed mutagenesis, formation of a more complex structure compared to the wild-type enzyme
K354X
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site-directed mutagenesis, inactive mutants, overview
R431G
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oligonucleotide site-directed mutagenesis, no formation of stable hexamer, inactive mutant
R431Q
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oligonucleotide site-directed mutagenesis, formation of a stable hexamer corresponding to the wild-type enzyme
R431V
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oligonucleotide site-directed mutagenesis, formation of a stable hexamer corresponding to the wild-type enzyme
R431W
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oligonucleotide site-directed mutagenesis, formation of a stable hexamer corresponding to the wild-type enzyme
K528R
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A-LAP polymorphism, leads to hypertension
K528R
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gene A-LAP, natural polymorphism and site-directed mutagenesis, hypertension-associated mutant, the mutant enzyme shows reduced activity
D347E
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oligonucleotide site-directed mutagenesis, formation of a more complex structure compared to the wild-type enzyme, nearly catalytically inactive with dipeptide substrates
D347E
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site-directed mutagenesis, inactive mutant
D347N
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oligonucleotide site-directed mutagenesis, no formation of stable hexamer, inactive mutant
D347N
mutation leads to inactivation of peptidase activity but does not have an impact on chaperone activity
D347R
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site-directed mutagenesis, reduced activity
D347R
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oligonucleotide site-directed mutagenesis, formation of a stable hexamer corresponding to the wild-type enzyme, reduced catalytic activity with dipeptide substrates compared to the wild-type
D347R
inactive mutant with disrupted hexameric structure has increased chaperone activity
E429D
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oligonucleotide site-directed mutagenesis, formation of a stable hexamer corresponding to the wild-type enzyme, activity with dipeptide substrates is similar or slightly reduced compared to the wild-type enzyme
E429D
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site-directed mutagenesis, 95% activity compared to wild-type enzyme
E429V
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oligonucleotide site-directed mutagenesis, formation of a stable hexamer corresponding to the wild-type enzyme, reduced catalytic activity with dipeptide substrates compared to the wild-type
E429V
mutation leads to inactivation of peptidase activity but does not have an impact on chaperone activity
K354E
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oligonucleotide site-directed mutagenesis, formation of a more complex structure compared to the wild-type enzyme
K354E
inactive mutant with disrupted hexameric structure has increased chaperone activity
K354R
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oligonucleotide site-directed mutagenesis, formation of a stable hexamer corresponding to the wild-type enzyme
K354R
mutation leads to inactivation of peptidase activity but does not have an impact on chaperone activity
R431A
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oligonucleotide site-directed mutagenesis, formation of a stable hexamer corresponding to the wild-type enzyme, nearly catalytically inactive with dipeptide substrates
R431A
mutation leads to inactivation of peptidase activity but does not have an impact on chaperone activity
R431K
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oligonucleotide site-directed mutagenesis, reduced catalytic activity with dipeptide substrates compared to the wild-type
R431K
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site-directed mutagenesis, 4fold reduced activity
additional information
AcLAP knockout using siRNA, AcLAP knockdown affects encystation of Acanthamoeba castellanii
additional information
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AcLAP knockout using siRNA, AcLAP knockdown affects encystation of Acanthamoeba castellanii
additional information
construction of mutants of lap genes S-Lap1 to S-Lap8, comparisons of the phenotypes of the mutant alleles of S-Lap genes, mutant Mi(ET)S-Lap3MB01319, overview
additional information
construction of mutants of lap genes S-Lap1 to S-Lap8, comparisons of the phenotypes of the mutant alleles of S-Lap genes, mutant Mi(ET)S-Lap3MB01319, overview
additional information
construction of mutants of lap genes S-Lap1 to S-Lap8, comparisons of the phenotypes of the mutant alleles of S-Lap genes, mutant Mi(ET)S-Lap3MB01319, overview
additional information
construction of mutants of lap genes S-Lap1 to S-Lap8, comparisons of the phenotypes of the mutant alleles of S-Lap genes, mutant Mi(ET)S-Lap3MB01319, overview
additional information
construction of mutants of lap genes S-Lap1 to S-Lap8, comparisons of the phenotypes of the mutant alleles of S-Lap genes, mutant Mi(ET)S-Lap3MB01319, overview
additional information
construction of mutants of lap genes S-Lap1 to S-Lap8, comparisons of the phenotypes of the mutant alleles of S-Lap genes, mutant Mi(ET)S-Lap3MB01319, overview
additional information
construction of mutants of lap genes S-Lap1 to S-Lap8, comparisons of the phenotypes of the mutant alleles of S-Lap genes, mutant Mi(ET)S-Lap3MB01319, overview
additional information
construction of mutants of lap genes S-Lap1 to S-Lap8, comparisons of the phenotypes of the mutant alleles of S-Lap genes, mutant Mi(ET)S-Lap3MB01319, overview
additional information
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construction of mutants of lap genes S-Lap1 to S-Lap8, comparisons of the phenotypes of the mutant alleles of S-Lap genes, mutant Mi(ET)S-Lap3MB01319, overview
additional information
construction of mutants of lap genes S-Lap1 to S-Lap8, comparisons of the phenotypes of the mutant alleles of S-Lap genes, mutant Mi(ET1)S-Lap4MB11296, overview
additional information
construction of mutants of lap genes S-Lap1 to S-Lap8, comparisons of the phenotypes of the mutant alleles of S-Lap genes, mutant Mi(ET1)S-Lap4MB11296, overview
additional information
construction of mutants of lap genes S-Lap1 to S-Lap8, comparisons of the phenotypes of the mutant alleles of S-Lap genes, mutant Mi(ET1)S-Lap4MB11296, overview
additional information
construction of mutants of lap genes S-Lap1 to S-Lap8, comparisons of the phenotypes of the mutant alleles of S-Lap genes, mutant Mi(ET1)S-Lap4MB11296, overview
additional information
construction of mutants of lap genes S-Lap1 to S-Lap8, comparisons of the phenotypes of the mutant alleles of S-Lap genes, mutant Mi(ET1)S-Lap4MB11296, overview
additional information
construction of mutants of lap genes S-Lap1 to S-Lap8, comparisons of the phenotypes of the mutant alleles of S-Lap genes, mutant Mi(ET1)S-Lap4MB11296, overview
additional information
construction of mutants of lap genes S-Lap1 to S-Lap8, comparisons of the phenotypes of the mutant alleles of S-Lap genes, mutant Mi(ET1)S-Lap4MB11296, overview
additional information
construction of mutants of lap genes S-Lap1 to S-Lap8, comparisons of the phenotypes of the mutant alleles of S-Lap genes, mutant Mi(ET1)S-Lap4MB11296, overview
additional information
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construction of mutants of lap genes S-Lap1 to S-Lap8, comparisons of the phenotypes of the mutant alleles of S-Lap genes, mutant Mi(ET1)S-Lap4MB11296, overview
additional information
construction of mutants of lap genes S-Lap1 to S-Lap8, comparisons of the phenotypes of the mutant alleles of S-Lap genes, mutant Mi(MIC)S-Lap2MI14597, overview
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construction of mutants of lap genes S-Lap1 to S-Lap8, comparisons of the phenotypes of the mutant alleles of S-Lap genes, mutant Mi(MIC)S-Lap2MI14597, overview
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construction of mutants of lap genes S-Lap1 to S-Lap8, comparisons of the phenotypes of the mutant alleles of S-Lap genes, mutant Mi(MIC)S-Lap2MI14597, overview
additional information
construction of mutants of lap genes S-Lap1 to S-Lap8, comparisons of the phenotypes of the mutant alleles of S-Lap genes, mutant Mi(MIC)S-Lap2MI14597, overview
additional information
construction of mutants of lap genes S-Lap1 to S-Lap8, comparisons of the phenotypes of the mutant alleles of S-Lap genes, mutant Mi(MIC)S-Lap2MI14597, overview
additional information
construction of mutants of lap genes S-Lap1 to S-Lap8, comparisons of the phenotypes of the mutant alleles of S-Lap genes, mutant Mi(MIC)S-Lap2MI14597, overview
additional information
construction of mutants of lap genes S-Lap1 to S-Lap8, comparisons of the phenotypes of the mutant alleles of S-Lap genes, mutant Mi(MIC)S-Lap2MI14597, overview
additional information
construction of mutants of lap genes S-Lap1 to S-Lap8, comparisons of the phenotypes of the mutant alleles of S-Lap genes, mutant Mi(MIC)S-Lap2MI14597, overview
additional information
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construction of mutants of lap genes S-Lap1 to S-Lap8, comparisons of the phenotypes of the mutant alleles of S-Lap genes, mutant Mi(MIC)S-Lap2MI14597, overview
additional information
construction of mutants of lap genes S-Lap1 to S-Lap8, comparisons of the phenotypes of the mutant alleles of S-Lap genes, mutant S-Lap8KK106866, overview
additional information
construction of mutants of lap genes S-Lap1 to S-Lap8, comparisons of the phenotypes of the mutant alleles of S-Lap genes, mutant S-Lap8KK106866, overview
additional information
construction of mutants of lap genes S-Lap1 to S-Lap8, comparisons of the phenotypes of the mutant alleles of S-Lap genes, mutant S-Lap8KK106866, overview
additional information
construction of mutants of lap genes S-Lap1 to S-Lap8, comparisons of the phenotypes of the mutant alleles of S-Lap genes, mutant S-Lap8KK106866, overview
additional information
construction of mutants of lap genes S-Lap1 to S-Lap8, comparisons of the phenotypes of the mutant alleles of S-Lap genes, mutant S-Lap8KK106866, overview
additional information
construction of mutants of lap genes S-Lap1 to S-Lap8, comparisons of the phenotypes of the mutant alleles of S-Lap genes, mutant S-Lap8KK106866, overview
additional information
construction of mutants of lap genes S-Lap1 to S-Lap8, comparisons of the phenotypes of the mutant alleles of S-Lap genes, mutant S-Lap8KK106866, overview
additional information
construction of mutants of lap genes S-Lap1 to S-Lap8, comparisons of the phenotypes of the mutant alleles of S-Lap genes, mutant S-Lap8KK106866, overview
additional information
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construction of mutants of lap genes S-Lap1 to S-Lap8, comparisons of the phenotypes of the mutant alleles of S-Lap genes, mutant S-Lap8KK106866, overview
additional information
construction of mutants of lap genes S-Lap1 to S-Lap8, comparisons of the phenotypes of the mutant alleles of S-Lap genes, overview
additional information
construction of mutants of lap genes S-Lap1 to S-Lap8, comparisons of the phenotypes of the mutant alleles of S-Lap genes, overview
additional information
construction of mutants of lap genes S-Lap1 to S-Lap8, comparisons of the phenotypes of the mutant alleles of S-Lap genes, overview
additional information
construction of mutants of lap genes S-Lap1 to S-Lap8, comparisons of the phenotypes of the mutant alleles of S-Lap genes, overview
additional information
construction of mutants of lap genes S-Lap1 to S-Lap8, comparisons of the phenotypes of the mutant alleles of S-Lap genes, overview
additional information
construction of mutants of lap genes S-Lap1 to S-Lap8, comparisons of the phenotypes of the mutant alleles of S-Lap genes, overview
additional information
construction of mutants of lap genes S-Lap1 to S-Lap8, comparisons of the phenotypes of the mutant alleles of S-Lap genes, overview
additional information
construction of mutants of lap genes S-Lap1 to S-Lap8, comparisons of the phenotypes of the mutant alleles of S-Lap genes, overview
additional information
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construction of mutants of lap genes S-Lap1 to S-Lap8, comparisons of the phenotypes of the mutant alleles of S-Lap genes, overview
additional information
construction of mutants of lap genes S-Lap1 to S-Lap8, comparisons of the phenotypes of the mutant alleles of S-Lap genes, overview. Despite the mitochondrial localization, S-Lap1resc-HA construct is not able to rescue the male sterile phenotype of the S-Lap1DELTA7 mutant, indicating that the C-terminal tag may modify the structure of the protein, which could prevent its normal function
additional information
construction of mutants of lap genes S-Lap1 to S-Lap8, comparisons of the phenotypes of the mutant alleles of S-Lap genes, overview. Despite the mitochondrial localization, S-Lap1resc-HA construct is not able to rescue the male sterile phenotype of the S-Lap1DELTA7 mutant, indicating that the C-terminal tag may modify the structure of the protein, which could prevent its normal function
additional information
construction of mutants of lap genes S-Lap1 to S-Lap8, comparisons of the phenotypes of the mutant alleles of S-Lap genes, overview. Despite the mitochondrial localization, S-Lap1resc-HA construct is not able to rescue the male sterile phenotype of the S-Lap1DELTA7 mutant, indicating that the C-terminal tag may modify the structure of the protein, which could prevent its normal function
additional information
construction of mutants of lap genes S-Lap1 to S-Lap8, comparisons of the phenotypes of the mutant alleles of S-Lap genes, overview. Despite the mitochondrial localization, S-Lap1resc-HA construct is not able to rescue the male sterile phenotype of the S-Lap1DELTA7 mutant, indicating that the C-terminal tag may modify the structure of the protein, which could prevent its normal function
additional information
construction of mutants of lap genes S-Lap1 to S-Lap8, comparisons of the phenotypes of the mutant alleles of S-Lap genes, overview. Despite the mitochondrial localization, S-Lap1resc-HA construct is not able to rescue the male sterile phenotype of the S-Lap1DELTA7 mutant, indicating that the C-terminal tag may modify the structure of the protein, which could prevent its normal function
additional information
construction of mutants of lap genes S-Lap1 to S-Lap8, comparisons of the phenotypes of the mutant alleles of S-Lap genes, overview. Despite the mitochondrial localization, S-Lap1resc-HA construct is not able to rescue the male sterile phenotype of the S-Lap1DELTA7 mutant, indicating that the C-terminal tag may modify the structure of the protein, which could prevent its normal function
additional information
construction of mutants of lap genes S-Lap1 to S-Lap8, comparisons of the phenotypes of the mutant alleles of S-Lap genes, overview. Despite the mitochondrial localization, S-Lap1resc-HA construct is not able to rescue the male sterile phenotype of the S-Lap1DELTA7 mutant, indicating that the C-terminal tag may modify the structure of the protein, which could prevent its normal function
additional information
construction of mutants of lap genes S-Lap1 to S-Lap8, comparisons of the phenotypes of the mutant alleles of S-Lap genes, overview. Despite the mitochondrial localization, S-Lap1resc-HA construct is not able to rescue the male sterile phenotype of the S-Lap1DELTA7 mutant, indicating that the C-terminal tag may modify the structure of the protein, which could prevent its normal function
additional information
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construction of mutants of lap genes S-Lap1 to S-Lap8, comparisons of the phenotypes of the mutant alleles of S-Lap genes, overview. Despite the mitochondrial localization, S-Lap1resc-HA construct is not able to rescue the male sterile phenotype of the S-Lap1DELTA7 mutant, indicating that the C-terminal tag may modify the structure of the protein, which could prevent its normal function
additional information
construction of mutants of lap genes S-Lap1 to S-Lap8, comparisons of the phenotypes of the mutant alleles of S-Lap genes, overview. Despite the mitochondrial localization, S-Lap1resc-HA construct is not able to rescue the male sterile phenotype of the S-Lap1DELTA7 mutant, indicating that the C-terminal tag may modify the structure of the protein, which could prevent its normal function. Strong reduction of S-Lap1-HAint in the pellet fraction of testis samples from the S-Lap1-HAint-containing S-Lap2MI14597, S-Lap3MB01319, S-Lap4MB11296, S-Lap5DELTA14, and S-Lap6MI06848 mutants, where the S-Lap1-HAint protein is present mainly in the supernatant, suggesting a problem with paracrystalline formation
additional information
construction of mutants of lap genes S-Lap1 to S-Lap8, comparisons of the phenotypes of the mutant alleles of S-Lap genes, overview. Despite the mitochondrial localization, S-Lap1resc-HA construct is not able to rescue the male sterile phenotype of the S-Lap1DELTA7 mutant, indicating that the C-terminal tag may modify the structure of the protein, which could prevent its normal function. Strong reduction of S-Lap1-HAint in the pellet fraction of testis samples from the S-Lap1-HAint-containing S-Lap2MI14597, S-Lap3MB01319, S-Lap4MB11296, S-Lap5DELTA14, and S-Lap6MI06848 mutants, where the S-Lap1-HAint protein is present mainly in the supernatant, suggesting a problem with paracrystalline formation
additional information
construction of mutants of lap genes S-Lap1 to S-Lap8, comparisons of the phenotypes of the mutant alleles of S-Lap genes, overview. Despite the mitochondrial localization, S-Lap1resc-HA construct is not able to rescue the male sterile phenotype of the S-Lap1DELTA7 mutant, indicating that the C-terminal tag may modify the structure of the protein, which could prevent its normal function. Strong reduction of S-Lap1-HAint in the pellet fraction of testis samples from the S-Lap1-HAint-containing S-Lap2MI14597, S-Lap3MB01319, S-Lap4MB11296, S-Lap5DELTA14, and S-Lap6MI06848 mutants, where the S-Lap1-HAint protein is present mainly in the supernatant, suggesting a problem with paracrystalline formation
additional information
construction of mutants of lap genes S-Lap1 to S-Lap8, comparisons of the phenotypes of the mutant alleles of S-Lap genes, overview. Despite the mitochondrial localization, S-Lap1resc-HA construct is not able to rescue the male sterile phenotype of the S-Lap1DELTA7 mutant, indicating that the C-terminal tag may modify the structure of the protein, which could prevent its normal function. Strong reduction of S-Lap1-HAint in the pellet fraction of testis samples from the S-Lap1-HAint-containing S-Lap2MI14597, S-Lap3MB01319, S-Lap4MB11296, S-Lap5DELTA14, and S-Lap6MI06848 mutants, where the S-Lap1-HAint protein is present mainly in the supernatant, suggesting a problem with paracrystalline formation
additional information
construction of mutants of lap genes S-Lap1 to S-Lap8, comparisons of the phenotypes of the mutant alleles of S-Lap genes, overview. Despite the mitochondrial localization, S-Lap1resc-HA construct is not able to rescue the male sterile phenotype of the S-Lap1DELTA7 mutant, indicating that the C-terminal tag may modify the structure of the protein, which could prevent its normal function. Strong reduction of S-Lap1-HAint in the pellet fraction of testis samples from the S-Lap1-HAint-containing S-Lap2MI14597, S-Lap3MB01319, S-Lap4MB11296, S-Lap5DELTA14, and S-Lap6MI06848 mutants, where the S-Lap1-HAint protein is present mainly in the supernatant, suggesting a problem with paracrystalline formation
additional information
construction of mutants of lap genes S-Lap1 to S-Lap8, comparisons of the phenotypes of the mutant alleles of S-Lap genes, overview. Despite the mitochondrial localization, S-Lap1resc-HA construct is not able to rescue the male sterile phenotype of the S-Lap1DELTA7 mutant, indicating that the C-terminal tag may modify the structure of the protein, which could prevent its normal function. Strong reduction of S-Lap1-HAint in the pellet fraction of testis samples from the S-Lap1-HAint-containing S-Lap2MI14597, S-Lap3MB01319, S-Lap4MB11296, S-Lap5DELTA14, and S-Lap6MI06848 mutants, where the S-Lap1-HAint protein is present mainly in the supernatant, suggesting a problem with paracrystalline formation
additional information
construction of mutants of lap genes S-Lap1 to S-Lap8, comparisons of the phenotypes of the mutant alleles of S-Lap genes, overview. Despite the mitochondrial localization, S-Lap1resc-HA construct is not able to rescue the male sterile phenotype of the S-Lap1DELTA7 mutant, indicating that the C-terminal tag may modify the structure of the protein, which could prevent its normal function. Strong reduction of S-Lap1-HAint in the pellet fraction of testis samples from the S-Lap1-HAint-containing S-Lap2MI14597, S-Lap3MB01319, S-Lap4MB11296, S-Lap5DELTA14, and S-Lap6MI06848 mutants, where the S-Lap1-HAint protein is present mainly in the supernatant, suggesting a problem with paracrystalline formation
additional information
construction of mutants of lap genes S-Lap1 to S-Lap8, comparisons of the phenotypes of the mutant alleles of S-Lap genes, overview. Despite the mitochondrial localization, S-Lap1resc-HA construct is not able to rescue the male sterile phenotype of the S-Lap1DELTA7 mutant, indicating that the C-terminal tag may modify the structure of the protein, which could prevent its normal function. Strong reduction of S-Lap1-HAint in the pellet fraction of testis samples from the S-Lap1-HAint-containing S-Lap2MI14597, S-Lap3MB01319, S-Lap4MB11296, S-Lap5DELTA14, and S-Lap6MI06848 mutants, where the S-Lap1-HAint protein is present mainly in the supernatant, suggesting a problem with paracrystalline formation
additional information
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construction of mutants of lap genes S-Lap1 to S-Lap8, comparisons of the phenotypes of the mutant alleles of S-Lap genes, overview. Despite the mitochondrial localization, S-Lap1resc-HA construct is not able to rescue the male sterile phenotype of the S-Lap1DELTA7 mutant, indicating that the C-terminal tag may modify the structure of the protein, which could prevent its normal function. Strong reduction of S-Lap1-HAint in the pellet fraction of testis samples from the S-Lap1-HAint-containing S-Lap2MI14597, S-Lap3MB01319, S-Lap4MB11296, S-Lap5DELTA14, and S-Lap6MI06848 mutants, where the S-Lap1-HAint protein is present mainly in the supernatant, suggesting a problem with paracrystalline formation
additional information
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reduction of the numbers of laid eggs in the HlLAP gene knockdown ticks may be due to the degeneration of immature oocytes following deprivation of nutrients such as amino acids supplied not only by midgut HlLAP but also by the ovarian HlLAP
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knockdown of A-LAP expression by siRNA
additional information
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overexpression and knockdown of the enzyme in breast cancer cells indicate that LAP3 can promote metastasis. A lentiviral vector is introduced to overexpression or knockdown LAP3 in MDA-MB-231 and MCF-7 cells
additional information
RNAi-mediated depletion of LAP-A, phenotype, overview
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construction of an enzyme deletion mutant DELTApaaP
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construction of an enzyme deletion mutant DELTApaaP
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construction of an enzyme deletion mutant DELTApaaP
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construction of an enzyme deletion mutant DELTApaaP
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construction of an enzyme deletion mutant DELTApaaP
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construction of an enzyme deletion mutant DELTApaaP
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additional information
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construction of an enzyme deletion mutant DELTApaaP
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construction of an enzyme deletion mutant DELTApaaP
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additional information
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construction of an enzyme deletion mutant DELTApaaP
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additional information
RNA interference targeting leucine aminopeptidase blocks hatching of Schistosoma mansoni eggs, overview. Knockdown of eitherSmLAP1 orSmLAP2, or both together, is accompanied by over 80% inhibition of hatching of schistosome eggs
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RNA interference targeting leucine aminopeptidase blocks hatching of Schistosoma mansoni eggs, overview. Knockdown of eitherSmLAP1 orSmLAP2, or both together, is accompanied by over 80% inhibition of hatching of schistosome eggs
additional information
construction of transgenic P35S:LapA tomato lines that are silenced in LapA or overexpress LapA. LapAManduca sexta larvae damage less foliage and display delays in growth and development when feeding on LapA-overexpressing transgenic plant leaves. Transgenic ectopic expression of LapA is not sufficient to induce Ser proteinase inhibitor Pin or polyphenol oxidase transcripts in non-wounded leaves. Larvae consume more foliage and attain larger masses when feeding on LapA-SI plants. Jasmonic acid does not complement the wound-signaling phenotype of LapA-SI plants. Phenotypes, overview
additional information
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construction of transgenic P35S:LapA tomato lines that are silenced in LapA or overexpress LapA. LapAManduca sexta larvae damage less foliage and display delays in growth and development when feeding on LapA-overexpressing transgenic plant leaves. Transgenic ectopic expression of LapA is not sufficient to induce Ser proteinase inhibitor Pin or polyphenol oxidase transcripts in non-wounded leaves. Larvae consume more foliage and attain larger masses when feeding on LapA-SI plants. Jasmonic acid does not complement the wound-signaling phenotype of LapA-SI plants. Phenotypes, overview
additional information
LAP-A exhibits chaperone activity which is independant of its peptidase activity
additional information
LAP-A exhibits chaperone activity which is independant of its peptidase activity
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LAP-A exhibits chaperone activity which is independant of its peptidase activity
additional information
knockdown of TbLAP1 by RNAi resulting in a growth defect
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RNA interference (RNAi), double knockout (dKO), and overexpression of the protein in bloodstream form (BF) and procyclic form (PF) Trypanosoma brucei subsp. brucei parasites in culture. RNAi-mediated depletion of LAP-A, phenotype, overview
additional information
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knockdown of TbLAP1 by RNAi resulting in a growth defect
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additional information
RNAi-mediated depletion of LAP-A, phenotype, overview