Identification of palmitoyl protein thioesterase 1 in human THP1 monocytes and macrophages and characterization of unique biochemical activities for this enzyme (Q33917127)

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English	Identification of palmitoyl protein thioesterase 1 in human THP1 monocytes and macrophages and characterization of unique biochemical activities for this enzyme	scientific article

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scholarly article

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Europe PubMed Central

30 July 2017

Identification of palmitoyl protein thioesterase 1 in human THP1 monocytes and macrophages and characterization of unique biochemical activities for this enzyme (English)

1 reference

Europe PubMed Central

30 July 2017

Mariola J. Ferraro

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Mariola J Edelmann

5

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author name string

Ran Wang

1

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Europe PubMed Central

30 July 2017

Abdolsamad Borazjani

2

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Europe PubMed Central

30 July 2017

Anberitha T Matthews

3

1 reference

Europe PubMed Central

30 July 2017

Lee C Mangum

4

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Europe PubMed Central

30 July 2017

Matthew K Ross

6

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Europe PubMed Central

30 July 2017

language of work or name

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publication date

18 October 2013

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Europe PubMed Central

30 July 2017

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Europe PubMed Central

30 July 2017

52

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Europe PubMed Central

30 July 2017

43

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Europe PubMed Central

30 July 2017

7559-7574

1 reference

Europe PubMed Central

30 July 2017

Controlling 2-arachidonoylglycerol metabolism as an anti-inflammatory strategy

1 reference

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DAGLβ inhibition perturbs a lipid network involved in macrophage inflammatory responses

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1 reference

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1 reference

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Examination of the carboxylesterase phenotype in human liver

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1 reference

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1 reference

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Inactivation of lipid glyceryl ester metabolism in human THP1 monocytes/macrophages by activated organophosphorus insecticides: role of carboxylesterases 1 and 2

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Human recombinant palmitoyl-protein thioesterase-1 (PPT1) for preclinical evaluation of enzyme replacement therapy for infantile neuronal ceroid lipofuscinosis

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Inhibition of carboxylesterase 1 is associated with cholesteryl ester retention in human THP-1 monocyte/macrophages.

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Glycosylation, transport, and complex formation of palmitoyl protein thioesterase 1 (PPT1)--distinct characteristics in neurons

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Identification of a novel endocannabinoid-hydrolyzing enzyme expressed by microglial cells

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Inefficient cleavage of palmitoyl-protein thioesterase (PPT) substrates by aminothiols: implications for treatment of infantile neuronal ceroid lipofuscinosis

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Current state of clinical and morphological features in human NCL.

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Palmitoyl protein thioesterase 1 is targeted to the axons in neurons

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Disruption of PPT1 or PPT2 causes neuronal ceroid lipofuscinosis in knockout mice

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Biochemical analysis of mutations in palmitoyl-protein thioesterase causing infantile and late-onset forms of neuronal ceroid lipofuscinosis

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Developmental expression of palmitoyl protein thioesterase in normal mice

1 reference

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1 reference

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Lysosomal targeting of palmitoyl-protein thioesterase

1 reference

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Purification and properties of a palmitoyl-protein thioesterase that cleaves palmitate from H-Ras

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The expression of palmitoyl-protein thioesterase is developmentally regulated in neural tissues but not in nonneural tissues.

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https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=4102699

29 October 2018

Enzymatic activity of human carboxylesterases

1 reference

https://pubmed.ncbi.nlm.nih.gov/24083319

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Expression of palmitoyl protein thioesterase in neurons

1 reference

https://pubmed.ncbi.nlm.nih.gov/24083319

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Identifiers

10.1021/BI401138S

1 reference

Europe PubMed Central

30 July 2017

1 reference

Europe PubMed Central

30 July 2017

1 reference

Europe PubMed Central

30 July 2017

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