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- Positive residues involved in the voltage-gating of the mitochondrial porin-channel are localized in the external moiety of the pore (2)
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Articles 31 - 33 of 33
Full-Text Articles in Physical Sciences and Mathematics
Isoprenylation Is Required For The Processing Of The Lamin A Precursor, Michael Sinensky, L. A. Beck, T. J. Hosick
Isoprenylation Is Required For The Processing Of The Lamin A Precursor, Michael Sinensky, L. A. Beck, T. J. Hosick
Michael Sinensky
The nuclear lamina proteins, prelamin A, lamin B, and a 70-kD lamina-associated protein, are posttranslationally modified by a metabolite derived from mevalonate. This modification can be inhibited by treatment with (3-R,S)-3-fluoromevalonate, demonstrating that it is isoprenoid in nature. We have examined the association between isoprenoid metabolism and processing of the lamin A precursor in human and hamster cells. Inhibition of 3-hydroxy-3-methylglutaryl coenzyme A reductase by mevinolin (lovastatin) specifically depletes endogenous isoprenoid pools and inhibits the conversion of prelamin A to lamin A. Prelamin A processing is also blocked by mevalonate starvation of Mev-1, a CHO cell line auxotrophic for mevalonate. …
A Warning For The Wagner Polarization Cell, Michael Setter, J. Akridge, M. Balkanski
A Warning For The Wagner Polarization Cell, Michael Setter, J. Akridge, M. Balkanski
Michael P. Setter
No abstract provided.
Positive Residues Involved In The Voltage-Gating Of The Mitochondrial Porin-Channel Are Localized In The External Moiety Of The Pore, Philadelphia University
Positive Residues Involved In The Voltage-Gating Of The Mitochondrial Porin-Channel Are Localized In The External Moiety Of The Pore, Philadelphia University
Philadelphia University, Jordan
No abstract provided.