3.4.23.24: Candidapepsin
This is an abbreviated version!
For detailed information about Candidapepsin, go to the full flat file.
Word Map on EC 3.4.23.24
-
3.4.23.24
-
alzheimer
-
amyloid
-
cathepsins
-
gamma-secretase
-
presenilins
-
pepstatin
-
abeta
-
candidiasis
-
beta-secretase
-
renin
-
intramembrane
-
beta-amyloid
-
hyphal
-
notch
-
nicastrin
-
beta-site
-
parapsilosis
-
beta-peptide
-
bace-1
-
amyloid-beta
-
fluconazole
-
tropicalis
-
peptidomimetic
-
dubliniensis
-
app-cleaving
-
broom
-
ritonavir
-
endoproteolysis
-
witches
-
plasmepsin
-
beta-protein
-
phytoplasmas
-
secretase
-
intramembrane-cleaving
-
indinavir
-
endothiapepsin
-
medicine
-
saquinavir
-
prorenin
-
hydroxyethylamine
-
vulvovaginal
-
isostere
- 3.4.23.24
- alzheimer
-
amyloid
- cathepsins
- gamma-secretase
-
presenilins
- pepstatin
- abeta
- candidiasis
- beta-secretase
- renin
-
intramembrane
- beta-amyloid
- hyphal
- notch
-
nicastrin
-
beta-site
- parapsilosis
- beta-peptide
- bace-1
- amyloid-beta
- fluconazole
- tropicalis
-
peptidomimetic
- dubliniensis
-
app-cleaving
- broom
- ritonavir
-
endoproteolysis
-
witches
-
plasmepsin
- beta-protein
- phytoplasmas
-
secretase
-
intramembrane-cleaving
- indinavir
- endothiapepsin
- medicine
- saquinavir
- prorenin
-
hydroxyethylamine
-
vulvovaginal
-
isostere
Reaction
Preferential cleavage at the carboxyl of hydrophobic amino acids, but fails to cleave Leu15-Tyr, Tyr16-Leu and Phe24-Phe of insulin B chain. Activates trypsinogen, and degrades keratin =
Synonyms
Aspartate protease, aspartic protease, aspartic protease 2, aspartic protease Sap2p, aspartic proteinase 3, aspartyl protease, aspartyl protease Sap2p, aspartyl protease Sap4, aspartyl protease Sap5, aspartyl protease Sap6, aspartyl proteinase, candialbicin, Candida albicans aspartic proteinase, Candida albicans carboxyl proteinase, Candida albicans secretory acid proteinase, Candida albicans-secreted aspartic proteinase, Candida olea acid proteinase, Candidapepsin-1, candidapepsin-2, EC 3.4.23.6, EC 3.4.4.17, Proteinase, Candida albicans aspartic, Proteinase, Candida aspartic, Proteinase, Candida olea aspartic, S-aspartyl proteinase, SAP, SAP1, Sap10, SAP11, Sap1p, SAP2, Sap2p, SAP2X, SAP3, Sap3p, SAP4, Sap4p, SAP5, Sap5p, SAP6, Sap6p, Sap7, Sap7p, Sap8, Sap8p, Sap9, Sap9p, SAPP1, Sapp1p, SAPP2, Sapp2p, SAPP3, SAPT1, Sapt1p, SAPT2, SAPT3, SAPT4, secreted aspartic protease, secreted aspartic protease 1, secreted aspartic protease 2, secreted aspartic proteinase, secreted aspartic proteinase 1, secreted aspartic proteinase 2, secreted aspartic proteinase-2, secreted aspartyl peptidase, secreted aspartyl protease, secreted aspartyl protease 9, secreted aspartyl proteinase, secreted aspartyl proteinase 2, secreted aspartyl proteinase 5, secreted aspartyl proteinase2, secreted aspartyl proteinases, secreted aspartyl-type peptidase, secretory aspartyl proteinase, secretory aspartyl proteinase SAP1, secretory aspartyl proteinase SAP2p, secretory aspartyl proteinase SAP3p, secretory aspartyl proteinase SAP4p, secretory aspartyl proteinase SAP5p, secretory aspartyl proteinase SAP6p, yapsin, Yps
ECTree
3.4.23.24 CandidapepsinAdvanced search results
results (
results (Substrates Products
Substrates Products on EC 3.4.23.24 - Candidapepsin
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SUBSTRATE 
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
4-(4-dimethylaminophenylazo)benzoyl-gamma-aminobutyryl-Ile-His-Pro-Phe-His-Leu-Val-Ile-His-Thr-[5-(2-aminoethyl)-amino]naphthalene-1-sulfonic acid + H2O
4-(4-dimethylaminophenylazo)benzoyl-gamma-aminobutyryl-Ile-His-Pro-Phe-His-Leu-Val-Ile-His + Thr-[5-(2-aminoethyl)-amino]naphthalene-1-sulfonic acid
-
-
-
?
4-(4-dimethylaminophenylazo)benzoyl-gamma-aminobutyryl-Ile-His-Pro-Phe-His-Leu-Val-Ile-His-Thr-[5-(2-aminoethyl)-amino]naphthalene-1-sulfonic acid + H2O
?
-
-
-
?
4-(4-dimethylaminophenylazo)benzyl-Glu-His-Val-Lys-Leu-Val-Glu-5-(2-aminoethylamino)-1-naphthalenesulfonic acid + H2O
4-(4-dimethylaminophenylazo)benzyl-Glu-His-Val-Lys + Leu-Val-Glu-5-(2-aminoethylamino)-1-naphthalenesulfonic acid
4-(4-dimethylaminophenylazo)benzyl-Glu-His-Val-Lys-Leu-Val-Glu-5-(2-aminoethylamino)-1-naphthalenesulfonic acid + H2O
4-(4-dimethylaminophenylazo)benzyl-Glu-His-Val-Lys-Leu + Val-Glu-5-(2-aminoethylamino)-1-naphthalenesulfonic acid
4-(4-dimethylaminophenylazo)benzyl-Pro-Lys-Val-Glu-Leu-Thr-Gly-Glu-5-(2-aminoethylamino)-1-naphthalenesulfonic acid + H2O
4-(4-dimethylaminophenylazo)benzyl-Pro-Lys-Val-Glu + Leu-Thr-Gly-Glu-5-(2-aminoethylamino)-1-naphthalenesulfonic acid
Ala-Thr-His-Gln-Val-Tyr-4-nitrophenylalanine-Val-Arg-Lys-Ala + H2O
Ala-Thr-His-Gln-Val-Tyr + 4-nitrophenylalanine-Val-Arg-Lys-Ala
-
-
-
-
?
Arg-Glu-[5-(aminoethyl)aminonaphthalene sulfonate]-Ile-His-Pro-Phe-His-Leu-Val-Ile-His-Thr-Lys-[4'-dimethylaminoazobenzene-4-carboxylate]-Arg + H2O
?
complement component 3b + H2O
?
substrate for isoforms Sapp1p and Sapp2p
-
-
?
complement component 4b + H2O
?
substrate for isoforms Sapp1p and Sapp2p
-
-
?
complement components C3b + H2O
?
-
substrate for isoforms Sap1, Sap2, Sap3, but not for Sap9
-
-
?
complement components C4b + H2O
?
-
substrate for isoforms Sap1, Sap2, Sap3, but not for Sap9
-
-
?
complement components C5 + H2O
?
-
substrate for isoforms Sap1, Sap2, Sap3, but not for Sap9
-
-
?
dabcyl-Pro-Lys-Val-Glu-Leu-Thr-Gly-Glu-EDANS
dabcyl-Pro-Lys-Val-Glu-COOH + Leu-Thr-Gly-Glu-EDANS
E-cadherin + H2O
?
-
Candida albicans strains JKC19 and SC5314 degrade E-cadherin at pH 4.0, the 10fold concentrated growth media of the strains HLC-52, HLC-54, 32723 and B1134 cause degradation at pH 4.0, strains HLC-52 and HLC-54 also at pH 6.0
-
-
?
factor H-related protein 5 + H2O
?
substrate for isoform Sapp2p
-
-
?
FRETS-25Ala + H2O
?
isozyme Sap1 shows highest activity towards FRETS-25Ala
-
-
?
FRETS-25Xaa + H2O
?
all Sap isozymes prefer Arg and Lys at the Xaa position
-
-
?
Lys-Pro-Ala-Arg-Phe-Nph-Arg-Leu + H2O
Lys-Pro-Ala-Arg-Phe + Nph-Arg-Leu
-
-
-
?
Lys-Pro-Ala-Glu-Phe-4-nitrophenylalanine-Ala-Leu + H2O
Lys-Pro-Ala-Glu-Phe + 4-nitrophenylalanine-Ala-Leu
-
-
-
-
?
Lys-Pro-Leu-Glu-Met-4-nitrophenylalanine-Ala-Leu + H2O
Lys-Pro-Leu-Glu-Met + 4-nitrophenylalanine-Ala-Leu
-
-
-
-
?
macrophage factor H-receptor CR3 + H2O
?
-
the enzyme cleaves and inactivates macrophage factor H-receptor CR3
-
-
?
macrophage factor H-receptor CR4 + H2O
?
-
the enzyme cleaves and inactivates macrophage factor H-receptor CR4
-
-
?
oxidized insulin B chain + H2O
?
cleavage sites of Sap2p: FV-/-NQHLCGSHL-/-V-/-EA-/-LYLVCGERGFF-/-YTPKA
-
-
?
Oxidized insulin B-chain + H2O
?
-
low side-chain specificity, preferential attack on hydrophobic amino acid residues
-
-
?
PMVELAGE + H2O
PMVEL + AGE
cleavage of Sapp1p, 100% conversion
-
-
?
PMVELQGE + H2O
PMVE + L-Leu + QGE
cleavage of Sapp2p, 18% conversion
-
-
?
PMVELQGE + H2O
PMVEL + QGE
cleavage of Sapp1p, 100% conversion
-
-
?
PMVELTGE + 2 H2O
PMVE + L-Leu + TGE
cleavage of Sapp2p, 35% conversion
-
-
?
PMVELTGE + H2O
PMVEL + TGE
cleavage of Sapp1p, 100% conversion
-
-
?
PMVELWGE + H2O
PMVE + L-Leu + WGE
cleavage of Sapp2p, 40% conversion
-
-
?
PMVELWGE + H2O
PMVEL + WGE
cleavage of Sapp1p, 76% conversion
-
-
?
4-(4-dimethylaminophenylazo)benzyl-Glu-His-Val-Lys-Leu-Val-Glu-5-(2-aminoethylamino)-1-naphthalenesulfonic acid + H2O
4-(4-dimethylaminophenylazo)benzyl-Glu-His-Val-Lys + Leu-Val-Glu-5-(2-aminoethylamino)-1-naphthalenesulfonic acid
Sapp2p preferentially cleaves the Lys-Leu bond
-
-
?
4-(4-dimethylaminophenylazo)benzyl-Glu-His-Val-Lys-Leu-Val-Glu-5-(2-aminoethylamino)-1-naphthalenesulfonic acid + H2O
4-(4-dimethylaminophenylazo)benzyl-Glu-His-Val-Lys + Leu-Val-Glu-5-(2-aminoethylamino)-1-naphthalenesulfonic acid
Sapp2p preferentially cleaves the Lys-Leu bond
-
-
?
4-(4-dimethylaminophenylazo)benzyl-Glu-His-Val-Lys-Leu-Val-Glu-5-(2-aminoethylamino)-1-naphthalenesulfonic acid + H2O
4-(4-dimethylaminophenylazo)benzyl-Glu-His-Val-Lys-Leu + Val-Glu-5-(2-aminoethylamino)-1-naphthalenesulfonic acid
Sapp1p preferentially cleaves the Leu-Val bond
-
-
?
4-(4-dimethylaminophenylazo)benzyl-Glu-His-Val-Lys-Leu-Val-Glu-5-(2-aminoethylamino)-1-naphthalenesulfonic acid + H2O
4-(4-dimethylaminophenylazo)benzyl-Glu-His-Val-Lys-Leu + Val-Glu-5-(2-aminoethylamino)-1-naphthalenesulfonic acid
Sapp1p preferentially cleaves the Leu-Val bond
-
-
?
4-(4-dimethylaminophenylazo)benzyl-Pro-Lys-Val-Glu-Leu-Thr-Gly-Glu-5-(2-aminoethylamino)-1-naphthalenesulfonic acid + H2O
4-(4-dimethylaminophenylazo)benzyl-Pro-Lys-Val-Glu + Leu-Thr-Gly-Glu-5-(2-aminoethylamino)-1-naphthalenesulfonic acid
the substrate is hydrolyzed preferentially at the Glu-Leu bond, however, when reaction times are prolonged, additional cleavage occurs at the Lys-Val position
-
-
?
4-(4-dimethylaminophenylazo)benzyl-Pro-Lys-Val-Glu-Leu-Thr-Gly-Glu-5-(2-aminoethylamino)-1-naphthalenesulfonic acid + H2O
4-(4-dimethylaminophenylazo)benzyl-Pro-Lys-Val-Glu + Leu-Thr-Gly-Glu-5-(2-aminoethylamino)-1-naphthalenesulfonic acid
the substrate is hydrolyzed preferentially at the Glu-Leu bond, however, when reaction times are prolonged, additional cleavage occurs at the Lys-Val position
-
-
?
Albumin + H2O
?
-
low side-chain specificity, preferential attack on hydrophobic amino acid residues
-
-
?
Albumin + H2O
?
cleavage by Sap2p shows a low side-chain specificity
-
-
?
Arg-Glu-[5-(aminoethyl)aminonaphthalene sulfonate]-Ile-His-Pro-Phe-His-Leu-Val-Ile-His-Thr-Lys-[4'-dimethylaminoazobenzene-4-carboxylate]-Arg + H2O
?
-
-
-
?
Arg-Glu-[5-(aminoethyl)aminonaphthalene sulfonate]-Ile-His-Pro-Phe-His-Leu-Val-Ile-His-Thr-Lys-[4'-dimethylaminoazobenzene-4-carboxylate]-Arg + H2O
?
-
-
-
?
Bovine serum albumin + H2O
?
-
-
-
-
?
Bovine serum albumin + H2O
Hydrolyzed bovine serum albumin
-
-
-
?
casein + H2O
?
isozyme Sap6 shows highest activity towards casein
-
-
?
dabcyl-Glu-His-Val-Lys-Leu-Val-Glu-EDANS
dabcyl-Glu-His-Val-Lys-COOH + Leu-Val-Glu-EDANS
-
-
-
?
dabcyl-Glu-His-Val-Lys-Leu-Val-Glu-EDANS
dabcyl-Glu-His-Val-Lys-COOH + Leu-Val-Glu-EDANS
-
-
-
?
dabcyl-Glu-His-Val-Lys-Leu-Val-Glu-EDANS + H2O
dabcyl-Glu-His-Val-Lys-Leu + Val-Glu-EDANS
-
-
-
-
?
dabcyl-Glu-His-Val-Lys-Leu-Val-Glu-EDANS + H2O
dabcyl-Glu-His-Val-Lys-Leu + Val-Glu-EDANS
-
-
-
-
?
dabcyl-Pro-Lys-Val-Glu-Leu-Thr-Gly-Glu-EDANS
dabcyl-Pro-Lys-Val-Glu-COOH + Leu-Thr-Gly-Glu-EDANS
-
-
-
?
dabcyl-Pro-Lys-Val-Glu-Leu-Thr-Gly-Glu-EDANS
dabcyl-Pro-Lys-Val-Glu-COOH + Leu-Thr-Gly-Glu-EDANS
-
-
-
?
ELSKRSSPS + H2O
ELSK + L-Arg + SSPS
98% conversion
-
-
?
factor H + H2O
?
-
the enzyme cleaves and inactivates factor H, diminishing its complement regulatory activity
-
-
?
L-Arg-7-amido-4-methylcoumarin + H2O
L-Arg + 7-amino-4-methylcoumarin
-
-
-
?
L-Arg-7-amido-4-methylcoumarin + H2O
L-Arg + 7-amino-4-methylcoumarin
[Candida] glabrata T-1639
-
-
-
?
LTEKRDSIS + H2O
LTEKR + L-Asp + Ser-Ile-Ser
100% conversion
-
-
?
LTEKRDSIS + H2O
LTEKR + L-Asp + Ser-Ile-Ser
100% conversion
-
-
?
PMVELAGE + H2O
PMVE + L-Leu + AGE
cleavage of Sapp2p, 81% conversion
-
-
?
PMVELAGE + H2O
PMVE + L-Leu + AGE
cleavage of Sapp2p, 81% conversion
-
-
?
additional information
?
-
-
the enzyme plays an important role in superficial infection by affecting the human stratum corneum of the skin and nail
-
-
?
additional information
?
-
-
the enzyme enables Candida albicans to use exogenous proteins as the sole source of nitrogen
-
-
?
additional information
?
-
candidapepsin is implicated in the degradation of host proteins involved in defense and barrier function
-
-
?
additional information
?
-
candidapepsin is implicated in the degradation of host proteins involved in defense and barrier function
-
-
?
additional information
?
-
candidapepsin is implicated in the degradation of host proteins involved in defense and barrier function. Sap2p degrades the Fc portion of IgG, IgA, complement factor C3 and endogenous protease inhibitors in human serum
-
-
?
additional information
?
-
candidapepsin is implicated in the degradation of host proteins involved in defense and barrier function. Sap2p degrades the Fc portion of IgG, IgA, complement factor C3 and endogenous protease inhibitors in human serum
-
-
?
additional information
?
-
-
distinct secreted aspartic proteinase plays a crucial role in the induction of chemokine response during Candida albicans vaginal infections
-
-
?
additional information
?
-
isoenzyme SAP1 is related to the vaginopathic potential of Candida albicans
-
-
?
additional information
?
-
isoenzyme SAP1 is related to the vaginopathic potential of Candida albicans
-
-
?
additional information
?
-
isoenzyme SAP1 is related to the vaginopathic potential of Candida albicans
-
-
?
additional information
?
-
isoenzyme SAP1 is related to the vaginopathic potential of Candida albicans
-
-
?
additional information
?
-
isoenzyme SAP1 is related to the vaginopathic potential of Candida albicans
-
-
?
additional information
?
-
isoenzyme SAP1 is related to the vaginopathic potential of Candida albicans
-
-
?
additional information
?
-
-
isoenzyme SAP1 is related to the vaginopathic potential of Candida albicans
-
-
?
additional information
?
-
isoenzyme SAP2 is related to the vaginopathic potential of Candida albicans
-
-
?
additional information
?
-
isoenzyme SAP2 is related to the vaginopathic potential of Candida albicans
-
-
?
additional information
?
-
isoenzyme SAP2 is related to the vaginopathic potential of Candida albicans
-
-
?
additional information
?
-
isoenzyme SAP2 is related to the vaginopathic potential of Candida albicans
-
-
?
additional information
?
-
isoenzyme SAP2 is related to the vaginopathic potential of Candida albicans
-
-
?
additional information
?
-
isoenzyme SAP2 is related to the vaginopathic potential of Candida albicans
-
-
?
additional information
?
-
-
isoenzyme SAP2 is related to the vaginopathic potential of Candida albicans
-
-
?
additional information
?
-
isoenzyme SAP3 is related to the vaginopathic potential of Candida albicans
-
-
?
additional information
?
-
isoenzyme SAP3 is related to the vaginopathic potential of Candida albicans
-
-
?
additional information
?
-
isoenzyme SAP3 is related to the vaginopathic potential of Candida albicans
-
-
?
additional information
?
-
isoenzyme SAP3 is related to the vaginopathic potential of Candida albicans
-
-
?
additional information
?
-
isoenzyme SAP3 is related to the vaginopathic potential of Candida albicans
-
-
?
additional information
?
-
isoenzyme SAP3 is related to the vaginopathic potential of Candida albicans
-
-
?
additional information
?
-
-
isoenzyme SAP3 is related to the vaginopathic potential of Candida albicans
-
-
?
additional information
?
-
isoenzyme SAP4 is correlated with systemic infections by Candida albicans
-
-
?
additional information
?
-
isoenzyme SAP4 is correlated with systemic infections by Candida albicans
-
-
?
additional information
?
-
isoenzyme SAP4 is correlated with systemic infections by Candida albicans
-
-
?
additional information
?
-
isoenzyme SAP4 is correlated with systemic infections by Candida albicans
-
-
?
additional information
?
-
isoenzyme SAP4 is correlated with systemic infections by Candida albicans
-
-
?
additional information
?
-
isoenzyme SAP4 is correlated with systemic infections by Candida albicans
-
-
?
additional information
?
-
-
isoenzyme SAP4 is correlated with systemic infections by Candida albicans
-
-
?
additional information
?
-
isoenzyme SAP5 is correlated with systemic infections by Candida albicans
-
-
?
additional information
?
-
isoenzyme SAP5 is correlated with systemic infections by Candida albicans
-
-
?
additional information
?
-
isoenzyme SAP5 is correlated with systemic infections by Candida albicans
-
-
?
additional information
?
-
isoenzyme SAP5 is correlated with systemic infections by Candida albicans
-
-
?
additional information
?
-
isoenzyme SAP5 is correlated with systemic infections by Candida albicans
-
-
?
additional information
?
-
isoenzyme SAP5 is correlated with systemic infections by Candida albicans
-
-
?
additional information
?
-
-
isoenzyme SAP5 is correlated with systemic infections by Candida albicans
-
-
?
additional information
?
-
isoenzyme SAP6 is correlated with systemic infections by Candida albicans
-
-
?
additional information
?
-
isoenzyme SAP6 is correlated with systemic infections by Candida albicans
-
-
?
additional information
?
-
isoenzyme SAP6 is correlated with systemic infections by Candida albicans
-
-
?
additional information
?
-
isoenzyme SAP6 is correlated with systemic infections by Candida albicans
-
-
?
additional information
?
-
isoenzyme SAP6 is correlated with systemic infections by Candida albicans
-
-
?
additional information
?
-
isoenzyme SAP6 is correlated with systemic infections by Candida albicans
-
-
?
additional information
?
-
-
isoenzyme SAP6 is correlated with systemic infections by Candida albicans
-
-
?
additional information
?
-
-
Candida albicans strain SC5314 Sap1-6 mutants do not degrade E-cadherin
-
-
?
additional information
?
-
-
isoform Sap9 preferentially cleaves a peptide backbone at adjacent basic residues e.g. Lys-Arg or Arg-Arg when these are followed by an acidic amino acid residue
-
-
?
additional information
?
-
sapp2p fails to cleave Lys-Pro-Ala-Glu-Phe-Phe(p-NO2)-Ala-Leu
-
-
?
additional information
?
-
-
sapp2p fails to cleave Lys-Pro-Ala-Glu-Phe-Phe(p-NO2)-Ala-Leu
-
-
?
additional information
?
-
isoform Sapp2p has a more restricted substrate specificity and significantly lower catalytic activity than isoform Sapp1p
-
-
?
additional information
?
-
isoform Sapp2p has a more restricted substrate specificity and significantly lower catalytic activity than isoform Sapp1p
-
-
?
additional information
?
-
-
isoform Sapp2p has a more restricted substrate specificity and significantly lower catalytic activity than isoform Sapp1p
-
-
?
additional information
?
-
no hydrolysis of PMVELPGE, PMVELHGE, PMVELGGE, PMVEMWGE, LPVNATSE, LTEKRDSIS, and ELSKRSSPS
-
-
?
additional information
?
-
no hydrolysis of PMVELPGE, PMVELHGE, PMVELGGE, PMVEMWGE, LPVNATSE, LTEKRDSIS, and ELSKRSSPS
-
-
?
additional information
?
-
-
no hydrolysis of PMVELPGE, PMVELHGE, PMVELGGE, PMVEMWGE, LPVNATSE, LTEKRDSIS, and ELSKRSSPS
-
-
?
additional information
?
-
sapp2p fails to cleave Lys-Pro-Ala-Glu-Phe-Phe(p-NO2)-Ala-Leu
-
-
?
additional information
?
-
isoform Sapp2p has a more restricted substrate specificity and significantly lower catalytic activity than isoform Sapp1p
-
-
?
additional information
?
-
isoform Sapp2p has a more restricted substrate specificity and significantly lower catalytic activity than isoform Sapp1p
-
-
?
additional information
?
-
no hydrolysis of PMVELPGE, PMVELHGE, PMVELGGE, PMVEMWGE, LPVNATSE, LTEKRDSIS, and ELSKRSSPS
-
-
?
additional information
?
-
no hydrolysis of PMVELPGE, PMVELHGE, PMVELGGE, PMVEMWGE, LPVNATSE, LTEKRDSIS, and ELSKRSSPS
-
-
?
additional information
?
-
-
Candida glabrata does not degrade E-cadherin
-
-
?
