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Showing 1–5 of 5 results

Advanced filters: Author: Mindong Ren Clear advanced filters

Characterization of proteins that interact with the cell-cycle regulatory protein Ran/TC4

Elias Coutavas
Mindong Ren
Mark G. Rush
Research09 Dec 1993
Nature

Volume: 366, P: 585-587
The physical state of lipid substrates provides transacylation specificity for tafazzin

Tafazzin, the mitochondrial transacylase that is deficient in Barth syndrome, selects lipid substrates in the inverted hexagonal phase but does not react with bilayer lipids.

Michael Schlame
Devrim Acehan
Richard M Epand
Research02 Sept 2012
Nature Chemical Biology

Volume: 8, P: 862-869
Loss of protein association causes cardiolipin degradation in Barth syndrome

Monolyso-cardiolipin (MLCL) accumulates in individuals with Barth syndrome, but this can be mitigated by stabilization of cardiolipin from metabolism to MLCL via assembly into supercomplexes of oxidative phosphorylation proteins. This process was found to be defective in subjects with Barth syndrome.

Yang Xu
Colin K L Phoon
Michael Schlame
Research27 Jun 2016
Nature Chemical Biology

Volume: 12, P: 641-647
Author Correction: Upregulation of the AMPK-FOXO1-PDK4 pathway is a primary mechanism of pyruvate dehydrogenase activity reduction in tafazzin-deficient cells

Zhuqing Liang
Tyler Ralph-Epps
Miriam L. Greenberg
Amendments and CorrectionsOpen Access25 Jun 2024
Scientific Reports

Volume: 14, P: 1
Upregulation of the AMPK-FOXO1-PDK4 pathway is a primary mechanism of pyruvate dehydrogenase activity reduction in tafazzin-deficient cells

Zhuqing Liang
Tyler Ralph-Epps
Miriam L. Greenberg
ResearchOpen Access20 May 2024
Scientific Reports

Volume: 14, P: 1-15