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Ceramidase
Known as:
N-Acylsphingosine Amidohydrolase
, Ceramidases [Chemical/Ingredient]
, Ceramidases
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Amidohydrolases that are specific for the cleavage of the N-acyl linkage of CERAMIDES. Ceramidases are classified as acidic, neutral or basic…
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National Institutes of Health
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Related topics
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9 relations
Acid Ceramidase
In Blood
Process of secretion
antagonists & inhibitors
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Broader (1)
Amidohydrolases
Papers overview
Semantic Scholar uses AI to extract papers important to this topic.
2008
2008
Novel analogs of D-e-MAPP and B13. Part 1: synthesis and evaluation as potential anticancer agents.
Z. Szulc
,
Nalini Mayroo
,
+5 authors
A. Bielawska
Bioorganic & Medicinal Chemistry
2008
Corpus ID: 24374690
Highly Cited
2007
Highly Cited
2007
Role of acid ceramidase in resistance to FasL: therapeutic approaches based on acid ceramidase inhibitors and FasL gene therapy.
S. Elojeimy
,
Xiang Liu
,
+13 authors
J. Norris
Molecular Therapy
2007
Corpus ID: 41798274
Head and neck squamous cell cancers (HNSCC) are particularly aggressive and are resistant to many forms of treatment. Ceramide…
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Review
2007
Review
2007
Targeting the conversion of ceramide to sphingosine 1-phosphate as a novel strategy for cancer therapy.
A. Huwiler
,
U. Zangemeister‐Wittke
Critical reviews in oncology/hematology
2007
Corpus ID: 26995350
Highly Cited
2003
Highly Cited
2003
O-Glycosylation of Mucin-like Domain Retains the Neutral Ceramidase on the Plasma Membranes as a Type II Integral Membrane Protein*
M. Tani
,
H. Iida
,
Makoto Ito
Journal of Biological Chemistry
2003
Corpus ID: 30017434
Ceramidase is a key enzyme involved in regulating cellular levels of ceramide, sphingosine, and possibly sphigosine 1-phosphate…
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Highly Cited
2001
Highly Cited
2001
Purification, Characterization, Molecular Cloning, and Subcellular Distribution of Neutral Ceramidase of Rat Kidney*
S. Mitsutake
,
M. Tani
,
+6 authors
M. Ito
Journal of Biological Chemistry
2001
Corpus ID: 37542206
Previously, we reported two types of neutral ceramidase in mice, one solubilized by freeze-thawing and one not. The former was…
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Highly Cited
2001
Highly Cited
2001
Biochemical Characterization of the Reverse Activity of Rat Brain Ceramidase
S. el Bawab
,
H. Birbes
,
P. Roddy
,
Z. Szulc
,
A. Bielawska
,
Y. Hannun
Journal of Biological Chemistry
2001
Corpus ID: 24365874
We have previously purified a membrane-bound ceramidase from rat brain and recently cloned the human homologue. We also observed…
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Highly Cited
2000
Highly Cited
2000
Molecular Cloning of the Full-length cDNA Encoding Mouse Neutral Ceramidase
M. Tani
,
N. Okino
,
K. Mori
,
T. Tanigawa
,
H. Izu
,
Makoto Ito
Journal of Biological Chemistry
2000
Corpus ID: 77320
We report here the molecular cloning, sequencing, and expression of the gene encoding the mouse neutral ceramidase, which has…
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Highly Cited
2000
Highly Cited
2000
Involvement of Sphingosine in Mitochondria-dependent Fas-induced Apoptosis of Type II Jurkat T Cells*
O. Cuvillier
,
L. Edsall
,
S. Spiegel
Journal of Biological Chemistry
2000
Corpus ID: 35439337
Exposure to anti-Fas antibody in Jurkat cells (type II cells), which are characterized by a weak caspase-8 activation at the…
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Highly Cited
1997
Highly Cited
1997
Alkaline sphingomyelinase activity is decreased in human colorectal carcinoma
E. Hertervig
,
A. Nilsson
,
L. Nyberg
,
R. Duan
Cancer
1997
Corpus ID: 32446993
The metabolism of sphingomyelin generates important signals regulating cell proliferation and apoptosis. Previous studies found…
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Highly Cited
1989
Highly Cited
1989
Free sphingosine formation from endogenous substrates by a liver plasma membrane system with a divalent cation dependence and a neutral pH optimum.
C. W. Slife
,
Elaine Wang
,
+4 authors
Alfred H. Merrill
Journal of Biological Chemistry
1989
Corpus ID: 8087260
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