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4-nitrophenylphosphate + H2O
4-nitrophenol + phosphate
-
-
-
?
6,8-difluoromethylumbelliferyl phosphate + H2O
6,8-difluoromethylumbelliferone + phosphate
-
-
-
?
a [CheA protein]-N-phospho-L-histidine + H2O
a [CheA protein]-L-histidine + phosphate
a [protein]-N-phospho-L-histidine + H2O
a [protein]-L-histidine + phosphate
AKR-N-phospho-HKV + H2O
AKRHKV + phosphate
-
-
-
-
?
succinyl-L-Ala-N-phospho-L-His-L-Pro-L-Phe 4-nitroanilide + H2O
succinyl-L-Ala-L-His-L-Pro-L-Phe 4-nitroanilide + phosphate
VIFIE-N-phospho-HAKRKG + H2O
VIFIEHAKRKG + phosphate
-
-
-
-
?
[ATP-citrate lyase]-N-phospho-L-histidine + H2O
[ATP-citrate lyase]-L-histidine + phosphate
[beta-subunit of heterotrimeric G-protein]-N-phospho-L-histidine + H2O
[beta-subunit of heterotrimeric G-protein]-L-histidine + phosphate
-
-
-
-
?
[cation channel SK4]-N-phospho-L-histidine + H2O
[cation channel SK4]-L-histidine + phosphate
-
-
-
-
?
[Escherichia coli histidine kinase ArcB]-N-phospho-L-histidine + H2O
[Escherichia coli histidine kinase ArcB]-L-histidine + phosphate
[histidine kinase ArcB]-N-phospho-L-histidine + H2O
[histidine kinase ArcB]-L-histidine + phosphate
-
-
-
-
?
[histone H4]-N-phospho-L-histidine + H2O
[histone H4]-L-histidine + phosphate
[KCa3.1 channel protein]-N-phospho-L-histidine + H2O
[KCa3.1 channel protein]-L-histidine + phosphate
-
the enzyme directly binds and inhibits KCa3.1 by dephosphorylating histidine 358
-
-
?
[nucleoside diphosphate kinase B]-N-phospho-L-histidine + H2O
[nucleoside diphosphate kinase B]-L-histidine + phosphate
the enzyme (PGAM5) specifically associates with and dephosphorylates the catalytic histidine (H118) on nucleoside diphosphate kinase B (NDPK-B). By dephosphorylating NDPK-B, the enzyme (PGAM5) negatively regulates CD4+ T cells by inhibiting NDPK-B mediated histidine phosphorylation and activation of the K+ channel KCa3.1, which is required for T cell receptor stimulated Ca2+ influx and cytokine production
-
-
?
[peptide]-N-phospho-L-histidine + H2O
[peptide]-L-histidine + phosphate
H2O2 exposure induces selective oxidation of hPHPT1 at Met95, a residue within the substrate binding region. H2O2-induced oxidation does not impact hPHPT1 function negatively
-
-
?
[protein]-N-phospho-L-histidine + H2O
[protein]-L-histidine + phosphate
-
-
-
-
?
[TRP channel protein TRPV5]-N-phospho-L-histidine + H2O
[TRP channel protein TRPV5]-L-histidine + phosphate
-
-
-
-
?
additional information
?
-
a [CheA protein]-N-phospho-L-histidine + H2O
a [CheA protein]-L-histidine + phosphate
-
-
-
-
?
a [CheA protein]-N-phospho-L-histidine + H2O
a [CheA protein]-L-histidine + phosphate
-
-
-
-
?
a [CheA protein]-N-phospho-L-histidine + H2O
a [CheA protein]-L-histidine + phosphate
-
-
-
?
a [CheA protein]-N-phospho-L-histidine + H2O
a [CheA protein]-L-histidine + phosphate
-
-
-
-
?
a [protein]-N-phospho-L-histidine + H2O
a [protein]-L-histidine + phosphate
-
-
-
-
?
a [protein]-N-phospho-L-histidine + H2O
a [protein]-L-histidine + phosphate
-
-
-
?
a [protein]-N-phospho-L-histidine + H2O
a [protein]-L-histidine + phosphate
-
-
-
-
?
a [protein]-N-phospho-L-histidine + H2O
a [protein]-L-histidine + phosphate
-
-
-
?
a [protein]-N-phospho-L-histidine + H2O
a [protein]-L-histidine + phosphate
-
-
-
-
?
a [protein]-N-phospho-L-histidine + H2O
a [protein]-L-histidine + phosphate
-
-
-
-
?
a [protein]-N-phospho-L-histidine + H2O
a [protein]-L-histidine + phosphate
-
-
-
-
?
succinyl-L-Ala-N-phospho-L-His-L-Pro-L-Phe 4-nitroanilide + H2O
succinyl-L-Ala-L-His-L-Pro-L-Phe 4-nitroanilide + phosphate
-
-
-
?
succinyl-L-Ala-N-phospho-L-His-L-Pro-L-Phe 4-nitroanilide + H2O
succinyl-L-Ala-L-His-L-Pro-L-Phe 4-nitroanilide + phosphate
-
-
-
-
?
succinyl-L-Ala-N-phospho-L-His-L-Pro-L-Phe 4-nitroanilide + H2O
succinyl-L-Ala-L-His-L-Pro-L-Phe 4-nitroanilide + phosphate
-
-
-
-
?
succinyl-L-Ala-N-phospho-L-His-L-Pro-L-Phe 4-nitroanilide + H2O
succinyl-L-Ala-L-His-L-Pro-L-Phe 4-nitroanilide + phosphate
-
-
-
-
?
[ATP-citrate lyase]-N-phospho-L-histidine + H2O
[ATP-citrate lyase]-L-histidine + phosphate
-
-
-
-
?
[ATP-citrate lyase]-N-phospho-L-histidine + H2O
[ATP-citrate lyase]-L-histidine + phosphate
-
-
-
-
?
[ATP-citrate lyase]-N-phospho-L-histidine + H2O
[ATP-citrate lyase]-L-histidine + phosphate
-
-
-
?
[ATP-citrate lyase]-N-phospho-L-histidine + H2O
[ATP-citrate lyase]-L-histidine + phosphate
-
-
-
-
?
[ATP-citrate lyase]-N-phospho-L-histidine + H2O
[ATP-citrate lyase]-L-histidine + phosphate
-
-
-
-
?
[ATP-citrate lyase]-N-phospho-L-histidine + H2O
[ATP-citrate lyase]-L-histidine + phosphate
-
-
-
-
?
[Escherichia coli histidine kinase ArcB]-N-phospho-L-histidine + H2O
[Escherichia coli histidine kinase ArcB]-L-histidine + phosphate
-
-
-
?
[Escherichia coli histidine kinase ArcB]-N-phospho-L-histidine + H2O
[Escherichia coli histidine kinase ArcB]-L-histidine + phosphate
-
-
-
?
[histone H4]-N-phospho-L-histidine + H2O
[histone H4]-L-histidine + phosphate
-
-
-
-
?
[histone H4]-N-phospho-L-histidine + H2O
[histone H4]-L-histidine + phosphate
-
-
-
-
?
additional information
?
-
-
the enzyme also dephosphorylates phospholysine of chemically phosphorylated histone H1.2 and polylysine
-
-
?
additional information
?
-
-
the enzyme does not dephosphorylate free phosphoarginine
-
-
?
additional information
?
-
-
the enzyme is unable to catalyse the dephosphorylation of histone H4 that has been phosphorylated with a histone H4 histidine kinase
-
-
?
additional information
?
-
-
histidine phosphoproteins of 40000 and 20000 Da are not dephosphorylated by the enzyme
-
-
?
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a [CheA protein]-N-phospho-L-histidine + H2O
a [CheA protein]-L-histidine + phosphate
a [protein]-N-phospho-L-histidine + H2O
a [protein]-L-histidine + phosphate
[ATP-citrate lyase]-N-phospho-L-histidine + H2O
[ATP-citrate lyase]-L-histidine + phosphate
[beta-subunit of heterotrimeric G-protein]-N-phospho-L-histidine + H2O
[beta-subunit of heterotrimeric G-protein]-L-histidine + phosphate
-
-
-
-
?
[cation channel SK4]-N-phospho-L-histidine + H2O
[cation channel SK4]-L-histidine + phosphate
-
-
-
-
?
[Escherichia coli histidine kinase ArcB]-N-phospho-L-histidine + H2O
[Escherichia coli histidine kinase ArcB]-L-histidine + phosphate
[histidine kinase ArcB]-N-phospho-L-histidine + H2O
[histidine kinase ArcB]-L-histidine + phosphate
-
-
-
-
?
[histone H4]-N-phospho-L-histidine + H2O
[histone H4]-L-histidine + phosphate
[KCa3.1 channel protein]-N-phospho-L-histidine + H2O
[KCa3.1 channel protein]-L-histidine + phosphate
-
the enzyme directly binds and inhibits KCa3.1 by dephosphorylating histidine 358
-
-
?
[nucleoside diphosphate kinase B]-N-phospho-L-histidine + H2O
[nucleoside diphosphate kinase B]-L-histidine + phosphate
the enzyme (PGAM5) specifically associates with and dephosphorylates the catalytic histidine (H118) on nucleoside diphosphate kinase B (NDPK-B). By dephosphorylating NDPK-B, the enzyme (PGAM5) negatively regulates CD4+ T cells by inhibiting NDPK-B mediated histidine phosphorylation and activation of the K+ channel KCa3.1, which is required for T cell receptor stimulated Ca2+ influx and cytokine production
-
-
?
[protein]-N-phospho-L-histidine + H2O
[protein]-L-histidine + phosphate
-
-
-
-
?
[TRP channel protein TRPV5]-N-phospho-L-histidine + H2O
[TRP channel protein TRPV5]-L-histidine + phosphate
-
-
-
-
?
additional information
?
-
a [CheA protein]-N-phospho-L-histidine + H2O
a [CheA protein]-L-histidine + phosphate
-
-
-
-
?
a [CheA protein]-N-phospho-L-histidine + H2O
a [CheA protein]-L-histidine + phosphate
-
-
-
-
?
a [CheA protein]-N-phospho-L-histidine + H2O
a [CheA protein]-L-histidine + phosphate
-
-
-
?
a [CheA protein]-N-phospho-L-histidine + H2O
a [CheA protein]-L-histidine + phosphate
-
-
-
-
?
a [protein]-N-phospho-L-histidine + H2O
a [protein]-L-histidine + phosphate
-
-
-
-
?
a [protein]-N-phospho-L-histidine + H2O
a [protein]-L-histidine + phosphate
-
-
-
?
a [protein]-N-phospho-L-histidine + H2O
a [protein]-L-histidine + phosphate
-
-
-
-
?
a [protein]-N-phospho-L-histidine + H2O
a [protein]-L-histidine + phosphate
-
-
-
?
a [protein]-N-phospho-L-histidine + H2O
a [protein]-L-histidine + phosphate
-
-
-
-
?
a [protein]-N-phospho-L-histidine + H2O
a [protein]-L-histidine + phosphate
-
-
-
-
?
a [protein]-N-phospho-L-histidine + H2O
a [protein]-L-histidine + phosphate
-
-
-
-
?
[ATP-citrate lyase]-N-phospho-L-histidine + H2O
[ATP-citrate lyase]-L-histidine + phosphate
-
-
-
-
?
[ATP-citrate lyase]-N-phospho-L-histidine + H2O
[ATP-citrate lyase]-L-histidine + phosphate
-
-
-
-
?
[ATP-citrate lyase]-N-phospho-L-histidine + H2O
[ATP-citrate lyase]-L-histidine + phosphate
-
-
-
?
[ATP-citrate lyase]-N-phospho-L-histidine + H2O
[ATP-citrate lyase]-L-histidine + phosphate
-
-
-
-
?
[ATP-citrate lyase]-N-phospho-L-histidine + H2O
[ATP-citrate lyase]-L-histidine + phosphate
-
-
-
-
?
[ATP-citrate lyase]-N-phospho-L-histidine + H2O
[ATP-citrate lyase]-L-histidine + phosphate
-
-
-
-
?
[Escherichia coli histidine kinase ArcB]-N-phospho-L-histidine + H2O
[Escherichia coli histidine kinase ArcB]-L-histidine + phosphate
-
-
-
?
[Escherichia coli histidine kinase ArcB]-N-phospho-L-histidine + H2O
[Escherichia coli histidine kinase ArcB]-L-histidine + phosphate
-
-
-
?
[histone H4]-N-phospho-L-histidine + H2O
[histone H4]-L-histidine + phosphate
-
-
-
-
?
[histone H4]-N-phospho-L-histidine + H2O
[histone H4]-L-histidine + phosphate
-
-
-
-
?
additional information
?
-
-
the enzyme also dephosphorylates phospholysine of chemically phosphorylated histone H1.2 and polylysine
-
-
?
additional information
?
-
-
the enzyme does not dephosphorylate free phosphoarginine
-
-
?
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Atherosclerosis
Nucleoside diphosphate kinase B-activated intermediate conductance potassium channels are critical for neointima formation in mouse carotid arteries.
Carcinogenesis
Knockdown of 14-kDa phosphohistidine phosphatase expression suppresses lung cancer cell growth in vivo possibly through inhibition of NF-?B signaling pathway.
Carcinoma
Nuclear expression and clinical significance of phosphohistidine phosphatase 1 in clear-cell renal cell carcinoma.
Carcinoma, Hepatocellular
14-kDa Phosphohistidine phosphatase plays an important role in hepatocellular carcinoma cell proliferation.
Carcinoma, Hepatocellular
LHPP suppresses proliferation, migration, and invasion and promotes apoptosis in pancreatic cancer.
Carcinoma, Renal Cell
Nuclear expression and clinical significance of phosphohistidine phosphatase 1 in clear-cell renal cell carcinoma.
Colorectal Neoplasms
Differential expression of alternatively spliced transcripts related to energy metabolism in colorectal cancer.
Infections
Primary hyperparathyroidism characterized by diffuse homogeneous metastatic pulmonary calcification: A case report.
Liver Cirrhosis
14-kDa phosphohistidine phosphatase is a potential therapeutic target for liver fibrosis.
Liver Cirrhosis
PHP14 regulates hepatic stellate cells migration in liver fibrosis via mediating TGF-?1 signaling to PI3K?/AKT/Rac1 pathway.
Lung Neoplasms
14-kDa phosphohistidine phosphatase and its role in human lung cancer cell migration and invasion.
Lung Neoplasms
14-kDa Phosphohistidine phosphatase plays an important role in hepatocellular carcinoma cell proliferation.
Lung Neoplasms
Clinical significance of PHPT1 protein expression in lung cancer.
Lung Neoplasms
Knockdown of 14-kDa phosphohistidine phosphatase expression suppresses lung cancer cell growth in vivo possibly through inhibition of NF-?B signaling pathway.
Lymphatic Metastasis
Clinical significance of PHPT1 protein expression in lung cancer.
Neoplasm Metastasis
14-kDa phosphohistidine phosphatase and its role in human lung cancer cell migration and invasion.
Neoplasm Metastasis
Clinical significance of PHPT1 protein expression in lung cancer.
Neoplasms
14-kDa Phosphohistidine phosphatase plays an important role in hepatocellular carcinoma cell proliferation.
Neoplasms
Down-regulation of LHPP in cervical cancer influences cell proliferation, metastasis and apoptosis by modulating AKT.
Neoplasms
Immunohistochemistry (IHC): Chromogenic Detection of 3-Phosphohistidine Proteins in Formaldehyde-Fixed, Frozen Mouse Liver Tissue Sections.
Neoplasms
Knockdown of 14-kDa phosphohistidine phosphatase expression suppresses lung cancer cell growth in vivo possibly through inhibition of NF-?B signaling pathway.
Neoplasms
LHPP suppresses proliferation, migration, and invasion and promotes apoptosis in pancreatic cancer.
Neoplasms
Nuclear expression and clinical significance of phosphohistidine phosphatase 1 in clear-cell renal cell carcinoma.
Neoplasms
Specific Fluorescent Probe for Protein Histidine Phosphatase Activity.
Neoplasms
The protein histidine phosphatase LHPP is a tumour suppressor.
Respiratory Tract Infections
Primary hyperparathyroidism characterized by diffuse homogeneous metastatic pulmonary calcification: A case report.
Urinary Bladder Neoplasms
LHPP suppresses proliferation, migration, and invasion and promotes apoptosis in pancreatic cancer.
Uterine Cervical Neoplasms
LHPP suppresses proliferation, migration, and invasion and promotes apoptosis in pancreatic cancer.
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malfunction
-
cell proliferation is inhibited and cell apoptosis is significantly increased following knockdown of 14kDa phosphohistidine phosphatase
malfunction
-
decreased expression of PHPT-1 in human CD4 T cells results in an increase in KCa3.1 channel activity and increases Ca2+ influx and proliferation after T cell receptor activation
malfunction
-
depletion of the enzyme significantly reduces glucose- and mitochondrial fuel- but not KCl-induced insulin secretion
malfunction
-
enzyme downregulation does not induce cell death, but significantly increases the acetylcholine content in SN-56 cells
malfunction
enzyme knockdown in highly metastatic lung cancer CL1-5 cells inhibits migration and invasion in vitro, but does not alter cell proliferation rates, while enzyme overexpression in H1299 cells promotes migration and invasion in vitro, but again does not alter cell proliferation
malfunction
DELTAsixA cells have lower intracellular potassium levels than wild-type cells
malfunction
Pgam5-/- T cells cause accelerated and more severe Graft versus host disease (GvHD) in mice
malfunction
PHP14 knockdown impairs Arp3 localization at the leading edge of lamellipodia, as well as lamellipodia formation
malfunction
PHPT-1(-/-) mice exhibit neonatal hyperinsulinemic hypoglycemia due to impaired trafficking of K(ATP) channels to the plasma membrane in pancreatic beta-cells in response to low glucose and leptin. The defect in K(ATP) channel trafficking in PHPT-1(-/-) beta-cells is due to the failure of PHPT-1 to directly activate transient receptor potential channel 4 (TRPC4), resulting in decreased Ca2+ influx and impaired downstream activation of AMPK
malfunction
-
DELTAsixA cells have lower intracellular potassium levels than wild-type cells
-
metabolism
-
the enzyme downregulates the activity of ATP-citrate lyase by dephosphorylation
metabolism
-
the enzyme reduces the activity of ATP-citrate lyase by dephosphorylation at His760 in the active site and, thus controls the main intermediate metabolism of the cell
metabolism
LHPP is a protein histidine phosphatase and tumour suppressor, suggesting that deregulated histidine phosphorylation is oncogenic
metabolism
LHPP is a protein histidine phosphatase and tumour suppressor, suggesting that deregulated histidine phosphorylation is oncogenic
metabolism
PHP14 promotes hepatic stellate cell migration, especially, promotes 3D floating collagen matrices contraction but inhibits stress released matrices contraction. Mechanistically, the PI3Kgamma/AKT/Rac1 pathway is involved in migration regulated by PHP14. Moreover, PHP14 specifically mediates the TGF-beta1 signaling to PI3Kgamma/AKT pathway and regulates HSC migration, and thus participates in liver fibrosis
metabolism
the enzyme targets a phosphotransferase system. A model is suggested in which SixA removes phosphoryl groups from the PTSNtr by acting on NPr. The PTSNtr is a widely conserved bacterial pathway that regulates diverse metabolic processes through the phosphorylation states of its protein components, EINtr, NPr, and EIIANtr, which receive phosphoryl groups on histidine residues
metabolism
-
the enzyme targets a phosphotransferase system. A model is suggested in which SixA removes phosphoryl groups from the PTSNtr by acting on NPr. The PTSNtr is a widely conserved bacterial pathway that regulates diverse metabolic processes through the phosphorylation states of its protein components, EINtr, NPr, and EIIANtr, which receive phosphoryl groups on histidine residues
-
physiological function
enzyme overexpression induces apoptosis in umbilical-vein endothelial cells
physiological function
-
enzyme overexpression reduces the acetylcholine level and induces cell death
physiological function
-
the endogenous enzyme negatively regulates CD4 T cells
physiological function
the enzyme is involved in cytoskeletal reorganization and therfore is functionally important in lung cancer cell migration and the invasion of lung cancer cells, mediated partly through modulation of actin cytoskeleton rearrangement
physiological function
-
the enzyme plays a regulatory role in a G protein-sensitive step involved in nutrient-induced insulin secretion. The enzyme is not involved in metabolic cell viability and cell proliferation
physiological function
critical role for PHPT-1 in normal pancreatic b-cell function
physiological function
role for PHP14 in the dynamic regulation of the actin cytoskeleton and cell migration
physiological function
the enzyme (PHP14) regulates hepatic stellate cells migration in liver fibrosis via mediating TGF-beta1 signaling to PI3Kgamma/AKT/Rac1 pathway
physiological function
the enzyme does not affects ArcB/ArcA signaling in vivo
physiological function
the enzyme plays a central role to negatively regulate CD4+ T cells. It specifically associates with and dephosphorylates the catalytic histidine (H118) on nucleoside diphosphate kinase B (NDPK-B). By dephosphorylating NDPK-B, the enzyme (PGAM5) negatively regulates CD4+ T cells by inhibiting NDPK-B mediated histidine phosphorylation and activation of the K+ channel KCa3.1, which is required for T cell receptor stimulated Ca2+ influx and cytokine production
physiological function
-
the enzyme does not affects ArcB/ArcA signaling in vivo
-
additional information
H2O2 exposure induces selective oxidation of hPHPT1 at Met95, a residue within the substrate binding region. H2O2-induced oxidation does not impact hPHPT1 function negatively
additional information
-
H2O2 exposure induces selective oxidation of hPHPT1 at Met95, a residue within the substrate binding region. H2O2-induced oxidation does not impact hPHPT1 function negatively
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Hamada, K.; Kato, M.; Mizuno, T.; Hakoshima, T.
Crystallographic characterization of a novel protein SixA which exhibits phospho-histidine phosphatase activity in the multistep His-Asp phosphorelay
Acta Crystallogr. Sect. D
55
269-271
1999
Escherichia coli (P76502), Escherichia coli
brenda
Kamath, V.; Kyathanahalli, C.N.; Jayaram, B.; Syed, I.; Olson, L.K.; Ludwig, K.; Klumpp, S.; Krieglstein, J.; Kowluru, A.
Regulation of glucose- and mitochondrial fuel-induced insulin secretion by a cytosolic protein histidine phosphatase in pancreatic beta-cells
Am. J. Physiol. Endocrinol. Metab.
299
E276-E286
2010
Rattus norvegicus
brenda
Klumpp, S.; Bechmann, G.; Maeurer, A.; Selke, D.; Krieglstein, J.
ATP-citrate lyase as a substrate of protein histidine phosphatase in vertebrates
Biochem. Biophys. Res. Commun.
306
110-115
2003
Oryctolagus cuniculus
brenda
Ma, R.; Kanders, E.; Sundh, U.B.; Geng, M.; Ek, P.; Zetterqvist, O.; Li, J.P.
Mutational study of human phosphohistidine phosphatase: effect on enzymatic activity
Biochem. Biophys. Res. Commun.
337
887-891
2005
Homo sapiens (Q9NRX4), Homo sapiens
brenda
Wong, C.; Faiola, B.; Wu, W.; Kennelly, P.J.
Phosphohistidine and phospholysine phosphatase activities in the rat: potential protein-lysine and protein-histidine phosphatases?
Biochem. J.
296
293-296
1993
Rattus norvegicus
brenda
Gong, W.; Li, Y.; Cui, G.; Hu, J.; Fang, H.; Jin, C.; Xia, B.
Solution structure and catalytic mechanism of human protein histidine phosphatase 1
Biochem. J.
418
337-344
2009
Homo sapiens (Q9NRX4), Homo sapiens
brenda
Attwood, P.V.; Ludwig, K.; Bergander, K.; Besant, P.G.; Adina-Zada, A.; Krieglstein, J.; Klumpp, S.
Chemical phosphorylation of histidine-containing peptides based on the sequence of histone H4 and their dephosphorylation by protein histidine phosphatase
Biochim. Biophys. Acta
1804
199-205
2010
Homo sapiens
brenda
Klumpp, S.; Ma, N.T.; Baeumer, N.; Bechmann, G.; Krieglstein, J.
Relevance of glycine and cysteine residues as well as N- and C-terminals for the activity of protein histidine phosphatase
Biochim. Biophys. Acta
1804
206-211
2010
Homo sapiens
brenda
Eissing, A.; Fischer, D.; Rauch, I.; Baumann, A.; Schebb, N.H.; Karst, U.; Rose, K.; Klumpp, S.; Krieglstein, J.
Acetylcholine content and viability of cholinergic neurons are influenced by the activity of protein histidine phosphatase
BMC Neurosci.
13
31
2012
Mus musculus
brenda
Klumpp, S.; Faber, D.; Fischer, D.; Litterscheid, S.; Krieglstein, J.
Role of protein histidine phosphatase for viability of neuronal cells
Brain Res.
1264
7-12
2009
Homo sapiens
brenda
Seeger, A.; Rose, K.; Ma, N.T.; Kremmer, E.; Klumpp, S.; Krieglstein, J.
Influence of protein histidine phosphatase overexpression and down-regulation on human umbilical-vein endothelial cell viability
Cell Biol. Int.
36
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