Kinetic characterization of mammalian ceramide synthases: Determination of K m values towards sphinganine

By S. Lahiri, Hyunmi Lee, Judith Mesicek, Z. Fuks, A. Haimovitz-Friedman, R. Kolesnick, A. Futerman. 2007

85 citations recorded by the source corpus.

Subfields: Biochemistry, Molecular Biology, Physiology

How researchers see this paper

The researchers whose trusted networks rank it highest, strongest advocate first. Every researcher gets a different order.

In Biochemistry

1. Yusuf A. Hannun
2. Michal Levy
3. LM Obeid
4. A. Futerman
5. S. Alexander
6. Hannah Alexander
7. Elad L. Laviad
8. Y. Pewzner‐Jung

In Molecular Biology

1. A. Futerman
2. Michal Levy
3. Yusuf A. Hannun
4. LM Obeid
5. S. Alexander
6. Hannah Alexander
7. Elad L. Laviad
8. Mark Hannink

In Physiology

1. A. Futerman
2. Yusuf A. Hannun
3. LM Obeid
4. Michal Levy
5. Craig Gault
6. Elad L. Laviad
7. S. Alexander
8. Hannah Alexander

Citations in the corpus

• Mammalian Ceramide Synthases (2010, methodology): “Thus, each CerS shows a similar Km toward sphinganine (21), even when different CoAs are used; for instance, CerS4, which can use either C18- or C20-CoA (10), has a similar Km toward sphinganine of 2 lM irrespective of the fatty acid (21), sug-”
• CERAMIDE SYNTHASE 1 IS REGULATED BY PROTEASOMAL MEDIATED TURNOVER (2009, methodology): “In vitro ceramide synthase assay was performed as described [17,25].”
• An overview of sphingolipid metabolism: from synthesis to breakdown (2010, background): “In mammals, six distinct (dihydro)ceramide synthases abbreviated as CerS1-6 have been identified and are encoded by six distinct genes [18], [19].”