Zobrazeno 1 - 10
of 42
pro vyhledávání: '"Patricia M. Sokolove"'
Publikováno v:
Archives of Biochemistry and Biophysics. 366:107-115
We have reported that the signal presequence of cytochrome oxidase subunit IV from Neurospora crassa increases the permeability of isolated rat liver mitochondria [P. M. Sokolove and K. W. Kinnally (1996) Arch. Biochem. Biophys. 336, 69] and regulate
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0ed10b4a9845125d7b959dcd3b1bdc17
https://doi.org/10.1006/abbi.1999.1190
https://doi.org/10.1006/abbi.1999.1190
Publikováno v:
Archives of Biochemistry and Biophysics. 363:155-162
Under a variety of conditions, the permeability of the inner mitochondrial membrane to small solutes can be nonselectively increased. A classic mitochondrial permeability transition (MPT) was originally identified based on its dependence on matrix Ca
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e7f84ce2fa805d57471aaa01cc82c488
https://doi.org/10.1006/abbi.1998.1039
https://doi.org/10.1006/abbi.1998.1039
Publikováno v:
Archives of Biochemistry and Biophysics. 336:69-76
Mitochondria that contain Ca 2+ can be induced by a variety of triggering agents and conditions to undergo a permeability transition (PT); the inner membrane becomes nonselectively permeable to small solutes. Mastoparan, an amphipathic peptide from w
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6129b497b35c6fc47ae188a30c4b5d01
https://doi.org/10.1006/abbi.1996.0533
https://doi.org/10.1006/abbi.1996.0533
Publikováno v:
Archives of Biochemistry and Biophysics. 331:225-231
A Ca 2+ -dependent inner mitochondrial membrane permeability transition is induced by a number of agents, an effect which is thought to cause cytotoxicity. This transition involves formation of a pore allowing the passage of solutes of up to 1500 Da;
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::63589317da0ec7f7c1c89906dd99b1e9
https://doi.org/10.1006/abbi.1996.0302
https://doi.org/10.1006/abbi.1996.0302
Autor:
Zhao H-Liao, J.Adrian Tyndall, Rahel Gebrehiwot, Eugene Mensah, Patricia M. Sokolove, Tekum Fonong, Cynthia A. Torrence, Cuthbert O. Simpkins, Samuel C. Balderman
Publikováno v:
Life Sciences. 58:2091-2099
Previously, we reported that the stress-induced protein metallothionein I (MT) modulated the oxygen consumption (VO2) of isolated rat liver mitochondria [Life Sci. 55 221-226, 1994]. We now present confirmation of this finding, and the additional obs
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::be387dbf0abb83ad1e4d67399a445130
https://doi.org/10.1016/0024-3205(96)00203-2
https://doi.org/10.1016/0024-3205(96)00203-2
Autor:
Lisa M. Haley, Patricia M. Sokolove
Publikováno v:
Journal of Bioenergetics and Biomembranes. 28:199-206
Mitochondria undergo a permeability transition (PT)2, i.e., become nonselectively permeable to small solutes, in response to a wide range of conditions/compounds. In general, opening of the permeability transition pore (PTP) is Ca2+- and P(i)-depende
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b07d9a2f675ec961d3df447cee6a7107
https://doi.org/10.1007/bf02110651
https://doi.org/10.1007/bf02110651
Publikováno v:
Archives of Biochemistry and Biophysics. 315:548-554
This study investigates the role of polymorphic or nonbilayer lipids in the function of an integral membrane protein which is a key component of the mitochondrial energy transduction apparatus. The adenine nucleotide translocator (AdNT) has been isol
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7392a5af80aaa498e112923a40c46bd9
https://doi.org/10.1006/abbi.1994.1535
https://doi.org/10.1006/abbi.1994.1535
Autor:
Patricia M. Sokolove
Publikováno v:
International Journal of Biochemistry. 26:1341-1350
Adriamycin and related anthracyclines are potent oncolytic agents, the clinical utility of which is limited by severe cardiotoxicity. Aglycone metabolites of Adriamycin (5-20 microM) induce a Ca(2+)-dependent increase in the permeability of the inner
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::74224da4b6145920632f599dc2093231
https://doi.org/10.1016/0020-711x(94)90176-7
https://doi.org/10.1016/0020-711x(94)90176-7
Publikováno v:
Biochemical Pharmacology. 46:691-697
Adriamycin (AdM) aglycones have dramatic effects on isolated heart mitochondria, oxidizing pyridine nucleotides, modifying sulfhydryl groups, and triggering a permeability transition of the inner membrane that results in free passage of solutes small
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::245501361c56c030fedd6f02f6e9b857
https://doi.org/10.1016/0006-2952(93)90556-c
https://doi.org/10.1016/0006-2952(93)90556-c
Publikováno v:
Archives of Biochemistry and Biophysics. 287:180-185
The polypeptide antibiotic duramycin has been reported to interact selectively with phosphatidylethanolamine (PE) and monogalactosyldiacylglycerol (Navarro et al., 1985, Biochemistry 24, 4645-4650). PE is a major component of mitochondrial membranes.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::0415316d0ebebcbfaaaca479c3a95a8c
https://doi.org/10.1016/0003-9861(91)90404-7
https://doi.org/10.1016/0003-9861(91)90404-7