Characterising the inhibitory actions of ceramide upon insulin signaling in different skeletal muscle cell models: a mechanistic insight (Q33945735)

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10 March 2020

title

Characterising the inhibitory actions of ceramide upon insulin signaling in different skeletal muscle cell models: a mechanistic insight (English)

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10 March 2020

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Agnieszka Blachnio-Zabielska

3

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10 March 2020

Nicolas Loiseau

5

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10 March 2020

Christopher Lipina

6

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10 March 2020

Olivier Bourron

8

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10 March 2020

Pascal Ferré

9

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10 March 2020

Fabienne Foufelle

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10 March 2020

Harinder S Hundal

11

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10 March 2020

Eric Hajduch

12

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10 March 2020

author name string

Rana Mahfouz

1

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10 March 2020

Rhéa Khoury

2

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10 March 2020

Sophie Turban

4

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10 March 2020

Clare Stretton

7

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10 March 2020

language of work or name

English

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publication date

24 July 2014

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10 March 2020

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10 March 2020

volume

9

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10 March 2020

issue

7

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10 March 2020

page(s)

e101865

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Creative Commons Attribution 4.0 International

10 March 2020

copyright license

start time

24 July 2014

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April 2022 Public Data File from Crossref

copyright status

copyrighted

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cites work

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Endoplasmic reticulum stress does not mediate palmitate-induced insulin resistance in mouse and human muscle cells

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Skeletal muscle triglycerides, diacylglycerols, and ceramides in insulin resistance: another paradox in endurance-trained athletes?

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Plasma membrane subdomain compartmentalization contributes to distinct mechanisms of ceramide action on insulin signaling

5 July 2018

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Insulin resistance is associated with higher intramyocellular triglycerides in type I but not type II myocytes concomitant with higher ceramide content

5 July 2018

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Modulating serine palmitoyl transferase (SPT) expression and activity unveils a crucial role in lipid-induced insulin resistance in rat skeletal muscle cells

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Targeting of PKCzeta and PKB to caveolin-enriched microdomains represents a crucial step underpinning the disruption in PKB-directed signalling by ceramide

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Ceramide disables 3-phosphoinositide binding to the pleckstrin homology domain of protein kinase B (PKB)/Akt by a PKCzeta-dependent mechanism.

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A role for protein phosphatase 2A-like activity, but not atypical protein kinase Czeta, in the inhibition of protein kinase B/Akt and glycogen synthesis by palmitate

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21 January 2018

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21 January 2018

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10.1371/JOURNAL.PONE.0101865

21 January 2018

Identifiers

DOI

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10 March 2020

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10 March 2020

PubMed publication ID

25058613

1 reference

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