Phospholipid-Cytochrome c Interaction

Zwischenmolekulare Energiewanderung und Fluoreszenz

Förster, T. (1948) · Annalen der Physik · doi:10.1002/andp.19484370105 · Cited by 8,285 · see citing works

Cytochrome c and dATP-Dependent Formation of Apaf-1/Caspase-9 Complex Initiates an Apoptotic Protease Cascade

Li, P., Nijhawan, D., Budihardjo, I., Srinivasula, S. M., Ahmad, M., Alnemri, E. S., & Wang, X. (1997) · Cell · doi:10.1016/s0092-8674(00)80434-1 · Cited by 7,289 · see citing works

Induction of Apoptotic Program in Cell-Free Extracts: Requirement for dATP and Cytochrome c

Liu, X., Kim, C. N., Yang, J., Jemmerson, R., & Wang, X. (1996) · Cell · doi:10.1016/s0092-8674(00)80085-9 · Cited by 5,167 · see citing works

Prevention of Apoptosis by Bcl-2: Release of Cytochrome c from Mitochondria Blocked

Yang, J., Liu, X., Bhalla, K. N., Kim, C. N., Ibrado, A. M., Cai, J., Peng, T.-I., Jones, D. P., & Wang, X. (1997) · Science · doi:10.1126/science.275.5303.1129 · Cited by 4,913 · see citing works

The Release of Cytochrome c from Mitochondria: A Primary Site for Bcl-2 Regulation of Apoptosis

Kluck, R. M., Bossy‐Wetzel, E., Green, D. R., & Newmeyer, D. D. (1997) · Science · doi:10.1126/science.275.5303.1132 · Cited by 4,715 · see citing works

Fluorescence Energy Transfer as a Spectroscopic Ruler

Stryer, L. (1978) · Annual Review of Biochemistry · doi:10.1146/annurev.bi.47.070178.004131 · Cited by 2,408 · see citing works

Small-volume extrusion apparatus for preparation of large, unilamellar vesicles

MacDonald, R. C., MacDonald, R. I., Menco, B. P. M., Takeshita, K., Subbarao, N. K., & Hu, L. (1991) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/0005-2736(91)90295-j · Cited by 1,494 · see citing works

Biomembranes: molecular structure and function

(1989) · Choice Reviews Online · doi:10.5860/choice.27-0304 · Cited by 1,226 · see citing works

Amyloid fibrillogenesis: themes and variations

Rochet, J., & Lansbury, P. T. (2000) · Current Opinion in Structural Biology · doi:10.1016/s0959-440x(99)00049-4 · Cited by 1,095 · see citing works

High-resolution three-dimensional structure of horse heart cytochrome c

Bushnell, G. W., Louie, G. V., & Brayer, G. D. (1990) · Journal of Molecular Biology · doi:10.1016/0022-2836(90)90200-6 · Cited by 1,056 · see citing works

Ferricytochrome c

Dickerson, R. E., Takano, T., Eisenberg, D. S., Kallai, O. B., Samson, L., Cooper, A., & Margoliash, E. (1971) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)77002-1 · Cited by 875 · see citing works

Appendix—Spectrum of horse-heart cytochrome c

Margoliash, E., & Frohwirt, N. (1959) · Biochemical Journal · doi:10.1042/bj0710570 · Cited by 807 · see citing works

Vesicle Permeabilization by Protofibrillar α-Synuclein: Implications for the Pathogenesis and Treatment of Parkinson's Disease

Volles, M. J., Lee, S., Rochet, J., Shtilerman, M. D., Ding, T. T., Kessler, J. C., & Lansbury, P. T. (2001) · Biochemistry · doi:10.1021/bi0102398 · Cited by 682 · see citing works

α‐lactalbumin: compact state with fluctuating tertiary structure?

Dolgikh, D. A., Gilmanshin, R., Бражников, Е. В., Bychkova, V. E., Semisotnov, G. V., Venyaminov, S. Y., & Ptitsyn, O. B. (1981) · FEBS Letters · doi:10.1016/0014-5793(81)80642-4 · Cited by 616 · see citing works

Cytochromes c: Evolutionary, Structural and Physicochemical Aspects

Moore, G. R., Pettigrew, G. W., & Moore, G. R. (1990) · Medical Entomology and Zoology · Cited by 455 · see citing works

Phosphatidylserine exposure and red cell viability in red cell aging and in hemolytic anemia

Boas, F. E., Forman, L., & Beutler, E. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.6.3077 · Cited by 405 · see citing works

7 Cytochromes c

Dickerson, R. E., & Timkovich, R. (1975) · ˜The œEnzymes · doi:10.1016/s1874-6047(08)60215-2 · Cited by 404 · see citing works

Conversion of α-lactalbumin to a protein inducing apoptosis.

Svensson, M., Håkansson, A., Mossberg, A.-K., Linse, S., & Svanborg, C. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.97.8.4221 · Cited by 355 · see citing works

Injected cytochrome c induces apoptosis

Zhivotovsky, B., Orrenius, S., Brustugun, O. T., & Døskeland, S. O. (1998) · Nature · doi:10.1038/35060 · Cited by 351 · see citing works

Cell-specific Induction of Apoptosis by Microinjection of Cytochrome c

Li, F., Srinivasan, A. N., Wang, Y., Armstrong, R. C., Tomaselli, K. J., & Fritz, L. C. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.48.30299 · Cited by 347 · see citing works

The protofilament substructure of amyloid fibrils11Edited by F. E. Cohen

Serpell, L. C., Sunde, M., Benson, M. D., Tennent, G. A., Pepys, M. B., & Fraser, P. E. (2000) · Journal of Molecular Biology · doi:10.1006/jmbi.2000.3908 · Cited by 342 · see citing works

Is Congo Red an Amyloid-specific Dye?

Khurana, R., Uversky, V. N., Garriques, L. N., & Fink, A. L. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m011499200 · Cited by 323 · see citing works

Cytochromes c: evolutionary structural and physicochemical aspects

Wickstro¨m, M. (1991) · Trends in Biochemical Sciences · doi:10.1016/0968-0004(91)90144-k · Cited by 299 · see citing works

Reversibility of the Binding of Cytochrome c to Liposomes

Rytömaa, M., & Kinnunen, P. K. J. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.7.3197 · Cited by 261 · see citing works

Filter extrusion of liposomes using different devices: comparison of liposome size, encapsulation efficiency, and process characteristics

Berger, N., Sachse, A., Bender, J., Schubert, R., & Brandl, M. (2001) · International Journal of Pharmaceutics · doi:10.1016/s0378-5173(01)00721-9 · Cited by 258 · see citing works

Evidence for two distinct acidic phospholipid-binding sites in cytochrome c.

Rytömaa, M., & Kinnunen, P. K. J. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)42094-1 · Cited by 254 · see citing works

Cytochrome c binding to enzymes and membranes

Nicholls, P. J. (1974) · Biochimica et Biophysica Acta (BBA) - Reviews on Bioenergetics · doi:10.1016/0304-4173(74)90003-2 · Cited by 242 · see citing works

Membrane Environment Alters the Conformational Structure of the Recombinant Human Prion Protein

Morillas, M., Świętnicki, W., Gambetti, P. L., & Surewicz, W. K. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.52.36859 · Cited by 241 · see citing works

Bax-type Apoptotic Proteins Porate Pure Lipid Bilayers through a Mechanism Sensitive to Intrinsic Monolayer Curvature

Basáñez, G., Sharpe, J. C., Galanis, J., Brandt, T. B., Hardwick, J. M., & Zimmerberg, J. J. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m206069200 · Cited by 234 · see citing works

Interactions of cytochrome c and [14C]-carboxymethylated cytochrome c with monolayers of phosphatidylcholine, phosphatidic acid and cardiolipin

Quinn, P. J., & DAWSON, R. M. C. (1969) · Biochemical Journal · doi:10.1042/bj1150065 · Cited by 207 · see citing works

Membrane binding induces destabilization of cytochrome c structure

Muga, A., Mantsch, H. H., & Surewicz, W. K. (1991) · Biochemistry · doi:10.1021/bi00243a025 · Cited by 200 · see citing works

Recent advances in capillary electrophoresis/electrospray-mass spectrometry

von Brocke, A., NICHOLSON, G. J., & Bayer, E. (2001) · Electrophoresis · doi:10.1002/1522-2683(200105)22:7 · Cited by 197 · see citing works

Reversible, nonionic, and pH-dependent association of cytochrome c with cardiolipin-phosphatidylcholine liposomes.

Rytömaa, M., Mustonen, P., & Kinnunen, P. K. J. (1992) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)41661-4 · Cited by 181 · see citing works

Ueber eine im Gehirn und Rückenmark des Menschen aufgefundene Substanz mit der chemischen Reaction der Cellulose

Virchow, R. (1854) · Archiv für Pathologische Anatomie und Physiologie und für Klinische Medicin · doi:10.1007/bf01930815 · Cited by 178 · see citing works

Alzheimer .beta.-Amyloid Peptide 25-35: Electrostatic Interactions with Phospholipid Membranes

Terzi, E., Hoelzemann, G., & Seelig, J. (1994) · Biochemistry · doi:10.1021/bi00189a051 · Cited by 173 · see citing works

Diphosphatidylglycerol is required for optimal activity of beef heart cytochrome c oxidase.

Vik, S. B., Georgevich, G., & Capaldi, R. (1981) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.78.3.1456 · Cited by 169 · see citing works

Equilibriums involved in prothrombin- and blood-clotting factor X-membrane binding

Nelsestuen, G. L., & Lim, T. K. (1977) · Biochemistry · doi:10.1021/bi00638a005 · Cited by 166 · see citing works

Metallocytochromes c : Characterization of Electronic Absorption and Emission Spectra of Sn4+ and Zn2+ Cytochromes c

Vanderkooi, J. M., Adar, F., & Erecińska, M. (1976) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1976.tb10312.x · Cited by 164 · see citing works

Quenching of tryptophan fluorescence by brominated phospholipid

Bolen, E. J., & Holloway, P. W. (1990) · Biochemistry · doi:10.1021/bi00493a019 · Cited by 155 · see citing works

The role of protein stability, solubility, and net charge in amyloid fibril formation

Schmittschmitt, J. P., & Scholtz, J. M. (2003) · Protein Science · doi:10.1110/ps.03152903 · Cited by 154 · see citing works

Lipid dynamics and peripheral interactions of proteins with membrane surfaces

Kinnunen, P. K. J., Kõiv, A., Lehtonen, J. Y. A., Rytömaa, M., & Mustonen, P. (1994) · Chemistry and Physics of Lipids · doi:10.1016/0009-3084(94)90181-3 · Cited by 148 · see citing works

Protein surface-distribution and protein-protein interactions in the binding of peripheral proteins to charged lipid membranes

Heimburg, T., & Marsh, D. (1995) · Biophysical Journal · doi:10.1016/s0006-3495(95)80215-8 · Cited by 146 · see citing works

Structural and Kinetic Description of Cytochrome c Unfolding Induced by the Interaction with Lipid Vesicles

Pinheiro, T. J. T., Elöve, G. A., Watts, A. B., & Röder, H. (1997) · Biochemistry · doi:10.1021/bi971235z · Cited by 141 · see citing works

Polar group conformation of phosphatidylcholine. Effect of solvent and aggregation

Hauser, H., Guyer, W., Pascher, I., Skrabal, P., & Sundell, S. (1980) · Biochemistry · doi:10.1021/bi00543a018 · Cited by 130 · see citing works

Optical activity of hemoproteins in the Soret region. Circular dichroism of the heme undecapeptide of cytochrome c in aqueous solution

Blauer, G., Sreerama, N., & Woody, R. W. (1993) · Biochemistry · doi:10.1021/bi00077a021 · Cited by 120 · see citing works

A Conformational Change in Cytochromecof Apoptotic and Necrotic Cells Is Detected by Monoclonal Antibody Binding and Mimicked by Association of the Native Antigen with Synthetic Phospholipid Vesicles

Jemmerson, R., Liu, J., Hausauer, D. L., Lam, K., Mondino, A., & Nelson, R. D. (1999) · Biochemistry · doi:10.1021/bi9809268 · Cited by 119 · see citing works

Cytochrome c Interaction with Membranes

Vanderkooi, J. M., & Erecińska, M. (1975) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1975.tb20992.x · Cited by 119 · see citing works

Binding of cytochrome c to liposomes as revealed by the quenching of fluorescence from pyrene-labeled phospholipids

Mustonen, P., Virtanen, J. A., Somerharju, P. J., & Kinnunen, P. K. J. (1987) · Biochemistry · doi:10.1021/bi00385a006 · Cited by 108 · see citing works

On the molecular-level mechanisms of peripheral protein-membrane interactions induced by lipids forming inverted non-lamellar phases

Kinnunen, P. K. J. (1996) · Chemistry and Physics of Lipids · doi:10.1016/0009-3084(96)02579-0 · Cited by 103 · see citing works

Effect of Heme Iron Valence State on the Conformation of Cytochrome c and Its Association with Membrane Interfaces

Nantes, I. L., Zucchi, M. D. R., Nascimento, O. R., & Faljoni‐Alário, A. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m006338200 · Cited by 101 · see citing works

Preferred conformation and dynamics of the glycerol backbone in phospholipids. An NMR and x-ray single-crystal analysis

Häuser, H., Pascher, I., & Sundell, S. (1988) · Biochemistry · doi:10.1021/bi00426a014 · Cited by 100 · see citing works

Surface plasmon resonance studies of complex formation between cytochrome c and bovine cytochrome c oxidase incorporated into a supported planar lipid bilayer. I. Binding of cytochrome c to cardiolipin/phosphatidylcholine membranes in the absence of oxidase

Salamon, Z., & Tollin, G. (1996) · Biophysical Journal · doi:10.1016/s0006-3495(96)79286-x · Cited by 94 · see citing works

Salt-induced formation of the molten globule state of cytochrome c studied by isothermal titration calorimetry.

Hamada, D., Kidokoro, S., Fukada, H., Takahashi, K., & Goto, Y. (1994) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.91.22.10325 · Cited by 94 · see citing works

Multiple Conformations of Physiological Membrane-Bound Cytochrome c

Cortese, J. D., Voglino, A. L., & Hackenbrock, C. R. (1998) · Biochemistry · doi:10.1021/bi9730543 · Cited by 91 · see citing works

Cytochrome c-lipid interactions studied by resonance Raman and phosphorus-31 NMR spectroscopy. Correlation between the conformational changes of the protein and the lipid bilayer

Heimburg, T., Hildebrandt, P., & Marsh, D. (1991) · Biochemistry · doi:10.1021/bi00101a025 · Cited by 87 · see citing works

A water-lipid interface induces a highly dynamic folded state in apocytochrome c and cytochrome c, which may represent a common folding intermediate

de Jongh, H. H. J., Killian, J. A., & KRUIJFF, B. D. (1992) · Biochemistry · doi:10.1021/bi00121a008 · Cited by 86 · see citing works

Apocytochrome c: an exceptional mitochondrial precursor protein using an exceptional import pathway

Stuart, R. A., & Neupert, W. (1990) · Biochimie · doi:10.1016/0300-9084(90)90136-5 · Cited by 83 · see citing works

The Soret circular dichroism spectrum as a probe for the heme Fe(III)-Met(80) axial bond in horse cytochrome c

Santucci, R., & Ascoli, F. (1997) · Journal of Inorganic Biochemistry · doi:10.1016/s0162-0134(97)00100-1 · Cited by 82 · see citing works

The interaction of cytochrome c with monolayers of phosphatidylethanolamine

Quinn, P. J., & DAWSON, R. M. C. (1969) · Biochemical Journal · doi:10.1042/bj1130791 · Cited by 81 · see citing works

Reversible unfolding of cytochrome c upon interaction with cardiolipin bilayers. II. Evidence from phosphorus-31 NMR measurements

Spooner, P. J. R., & Watts, A. G. (1991) · Biochemistry · doi:10.1021/bi00230a011 · Cited by 77 · see citing works

Relationship between lipid saturation and lipid-protein interaction in liver mitochondria modified by catalytic hydrogenation with reference to cardiolipin molecular species

Schlame, M., Horvàth, L., & Vìgh, L. (1990) · Biochemical Journal · doi:10.1042/bj2650079 · Cited by 71 · see citing works

Structure of Zinc-Substituted Cytochrome c: Nuclear Magnetic Resonance and Optical Spectroscopic Studies

Anni, H., Vanderkooi, J. M., & Mayne, L. C. (1995) · Biochemistry · doi:10.1021/bi00017a006 · Cited by 70 · see citing works

Phospholipid Determinants for Annexin V Binding Sites and the Role of Tryptophan 187

Meers, P. R., & Mealy, T. R. (1994) · Biochemistry · doi:10.1021/bi00185a022 · Cited by 66 · see citing works

Interaction of Horse Heart Cytochrome c with Lipid Bilayer Membranes: Effects on Redox Potentials

Salamon, Z., & Tollin, G. (1997) · Journal of Bioenergetics and Biomembranes · doi:10.1023/a:1022401825287 · Cited by 58 · see citing works

ATP Induces a Conformational Change in Lipid-bound Cytochrome c

Tuominen, E. K. J., Zhu, K., Wallace, C. J. A., Clark‐Lewis, I., Craig, D. B., Rytömaa, M., & Kinnunen, P. K. J. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m100853200 · Cited by 58 · see citing works

Surface plasmon resonance studies of complex formation between cytochrome c and bovine cytochrome c oxidase incorporated into a supported planar lipid bilayer. II. Binding of cytochrome c to oxidase-containing cardiolipin/phosphatidylcholine membranes

Salamon, Z., & Tollin, G. (1996) · Biophysical Journal · doi:10.1016/s0006-3495(96)79287-1 · Cited by 53 · see citing works

Membrane‐bound states of α‐lactalbumin: Implications for the protein stability and conformation

Cawthern, K. M., Permyakov, E. A., & Berliner, L. J. (1996) · Protein Science · doi:10.1002/pro.5560050718 · Cited by 50 · see citing works

Binding and Dissociation of Cytochrome c to and from Membranes Containing Acidic Phospholipids

Subramanian, M., Jutila, A., & Kinnunen, P. K. J. (1998) · Biochemistry · doi:10.1021/bi9716581 · Cited by 49 · see citing works

Evidence for the Extended Phospholipid Conformation in Membrane Fusion and Hemifusion

Holopainen, J. M., Lehtonen, J. Y. A., & Kinnunen, P. K. J. (1999) · Biophysical Journal · doi:10.1016/s0006-3495(99)77367-4 · Cited by 47 · see citing works

Fluorescence quenching of spectrin and other red cell membrane cytoskeletal proteins. Relation to hydrophobic binding sites

Kahana, E., Pinder, J. C., Smith, K., & Gratzer, W. B. (1992) · Biochemical Journal · doi:10.1042/bj2820075 · Cited by 46 · see citing works

Modulation of cytochrome c spin states by lipid acyl chains: a continuous-wave electron paramagnetic resonance (CW-EPR) study of haem iron

Zucchi, M. D. R., Nascimento, O. R., Faljoni‐Alário, A., Prieto, T., & Nantes, I. L. (2003) · Biochemical Journal · doi:10.1042/bj20021521 · Cited by 46 · see citing works

Control of Nucleotide Pools in Mammalian Cells

Bjursell, G., & Skoog, L. K. (2015) · Antibiotics and chemotherapy/Antibiotica et chemotherapia · doi:10.1159/000386063 · Cited by 39 · see citing works

Studies of 8-Azido-ATP Adducts Reveal Two Mechanisms by Which ATP Binding to Cytochrome c Could Inhibit Respiration

Craig, D. B., & Wallace, C. J. A. (1995) · Biochemistry · doi:10.1021/bi00008a036 · Cited by 35 · see citing works

Role of phospholipid in the low affinity reactions between cytochrome c and cytochrome oxidase

Speck, S. H., Neu, C. A., Swanson, M. S., & Margoliash, E. (1983) · FEBS Letters · doi:10.1016/0014-5793(83)80321-4 · Cited by 34 · see citing works

Fusion and protein-mediated phospholipid exchange studied with single bilayer phosphatidylcholine vesicles of different density

Dawidowicz, E. A., & Rothman, J. E. (1976) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/0005-2736(76)90036-5 · Cited by 34 · see citing works

The interaction of ferrocytochrome c with long-chain fatty acids and their CoA and carnitine esters

Stewart, J. M., Blakely, J. A., & Johnson, M. D. (2000) · Biochemistry and Cell Biology · doi:10.1139/o00-078 · Cited by 30 · see citing works

The interaction of ferrocytochrome c with long-chain fatty acids and their CoA and carnitine esters.

Stewart, J. M., Blakely, J. A., & Johnson, M. D. (2000) · PubMed · Cited by 29 · see citing works

The specificity and Kd at physiological ionic strength of an ATP-binding site on cytochrome c suit it to a regulatory role

Craig, D. B., & Wallace, C. J. A. (1991) · Biochemical Journal · doi:10.1042/bj2790781 · Cited by 29 · see citing works

Definition of a Nucleotide Binding Site on Cytochrome c by Photoaffinity Labeling

McIntosh, D. B., Parrish, J. C., & Wallace, C. J. A. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.31.18379 · Cited by 24 · see citing works

The oxidation-state-dependent ATP-binding site of cytochrome c. A possible physiological significance

Corthésy, B., & Wallace, C. J. A. (1986) · Biochemical Journal · doi:10.1042/bj2360359 · Cited by 23 · see citing works

The semisynthesis of analogues of cytochrome c. Modifications of arginine residues 38 and 91

Wallace, C. J. A., & Rose, K. (1983) · Biochemical Journal · doi:10.1042/bj2150651 · Cited by 21 · see citing works

Structural investigation of the covalent and electrostatic binding of yeast cytochrome c to the surface of various ultrathin lipid multilayers using x-ray diffraction

Pachence, J. M., & Blasie, J. K. (1991) · Biophysical Journal · doi:10.1016/s0006-3495(91)82302-5 · Cited by 18 · see citing works

The interaction of fatty acids with mammalian cytochrome c

Hardesty, B. D., & Mitchell, H. K. (1963) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(63)90025-0 · Cited by 17 · see citing works

Thermodynamic parameters for the reduction reaction of membrane-bound cytochrome c in comparison with those of the membrane-free form: spectropotentiostatic determination with use of an optically transparent thin-layer electrode

Huang, Y. Y., & Kimura, T. (1984) · Biochemistry · doi:10.1021/bi00305a021 · Cited by 17 · see citing works

The oxidation-state-dependent ATP-binding site of cytochrome c. Implication of an essential arginine residue and the effect of occupancy on the oxidation-reduction potential

Corthésy, B., & Wallace, C. J. A. (1988) · Biochemical Journal · doi:10.1042/bj2520349 · Cited by 15 · see citing works

Biomembranes. Molecular Structure and Function.

Sokolov, V. S., & Chizmadzhev, Y. A. (1989) · Bioelectrochemistry and Bioenergetics · doi:10.1016/0302-4598(89)87067-9 · Cited by 15 · see citing works

8-Azido-ATP Modification of Cytochrome c: Retardation of Its Electron-Transfer Activity to Cytochrome c Oxidase

Lin, J., Wu, S., Lau, W., & Chan, N. (1995) · Biochemistry · doi:10.1021/bi00008a035 · Cited by 8 · see citing works

Significance of reduced dimensionality in reaction kinetics: impact of multi-site particles

Nelsestuen, G. L. (1999) · Chemistry and Physics of Lipids · doi:10.1016/s0009-3084(99)00053-5 · Cited by 6 · see citing works

Editorial

Kinnunen, P. K. (1999) · Chemistry and Physics of Lipids · doi:10.1016/s0009-3084(99)00051-1 · Cited by 6 · see citing works

Mitochondria, oxidative stress and cell death

Ott, M., Gogvadze, V. G., Orrenius, S., & Zhivotovsky, B. (2007) · APOPTOSIS · doi:10.1007/s10495-007-0756-2 · Cited by 1,976 · see citing works

Mitochondrial Oxidative Stress: Implications for Cell Death

Orrenius, S., Gogvadze, V. G., & Zhivotovsky, B. (2006) · The Annual Review of Pharmacology and Toxicology · doi:10.1146/annurev.pharmtox.47.120505.105122 · Cited by 1,266 · see citing works

Cytochrome c acts as a cardiolipin oxygenase required for release of proapoptotic factors

Kagan, V. E., Tyurin, V. A., Jiang, J., Tyurina, Y. Y., Ritov, V. B., Amoscato, A. A., Osipov, A. N., Belikova, N. A., Kapralov, A. A., Kini, V., et al. (2005) · Nature Chemical Biology · doi:10.1038/nchembio727 · Cited by 1,256 · see citing works

Phosphoinositide Regulation of the Actin Cytoskeleton

Yin, H. L., & Janmey, P. A. (2003) · Annual Review of Physiology · doi:10.1146/annurev.physiol.65.092101.142517 · Cited by 662 · see citing works

Role of cardiolipin alterations in mitochondrial dysfunction and disease

Chicco, A. J., & Sparagna, G. C. (2006) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00243.2006 · Cited by 641 · see citing works

Structural basis for targeting HIV-1 Gag proteins to the plasma membrane for virus assembly

Saad, J. S., Miller, J., Tai, J., Kim, A., Ghanam, R. H., & Summers, M. F. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0602818103 · Cited by 545 · see citing works

The multiple functions of cytochrome c and their regulation in life and death decisions of the mammalian cell: From respiration to apoptosis

Hüttemann, M., Pecina, P., Rainbolt, M., Sanderson, T. H., Kagan, V. E., Samavati, L., Doan, J. W., & Lee, I. (2011) · Mitochondrion · doi:10.1016/j.mito.2011.01.010 · Cited by 522 · see citing works

Functional role of cardiolipin in mitochondrial bioenergetics

Paradies, G., Paradies, V., Benedictis, V. D., Ruggiero, F. M., & Petrosillo, G. (2013) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2013.10.006 · Cited by 505 · see citing works

Role of Cardiolipin in Mitochondrial Function and Dynamics in Health and Disease: Molecular and Pharmacological Aspects

Paradies, G., Paradies, V., Ruggiero, F. M., & Petrosillo, G. (2019) · Cells · doi:10.3390/cells8070728 · Cited by 504 · see citing works

Mitochondrial regulation of apoptotic cell death

Orrenius, S. (2004) · Toxicology Letters · doi:10.1016/j.toxlet.2003.12.017 · Cited by 482 · see citing works

Nonbilayer lipids affect peripheral and integral membrane proteins via changes in the lateral pressure profile

der Laan, E. V. D. B.-V., Killian, J. A., & KRUIJFF, B. D. (2004) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2004.06.010 · Cited by 461 · see citing works

Membranes: A meeting point for lipids, proteins and therapies

Escribá, P. V., González‐Ros, J. M., Goñi, F. M., Kinnunen, P. K. J., Vigh, L., Sánchez‐Magraner, L., Fernández, A. M., Busquets, X., Horváth, I., & Barceló‐Coblijn, G. (2008) · Journal of Cellular and Molecular Medicine · doi:10.1111/j.1582-4934.2008.00281.x · Cited by 454 · see citing works

Cytochrome c/cardiolipin relations in mitochondria: a kiss of death

Kagan, V. E., Bayır, H., Belikova, N. A., Kapralov, A. A., Tyurina, Y. Y., Tyurin, V. A., Jiang, J., Stoyanovsky, D. A., Wipf, P., Kochanek, P. M., et al. (2009) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2009.03.004 · Cited by 445 · see citing works

Biophysical properties of lipids and dynamic membranes

Janmey, P. A., & Kinnunen, P. K. J. (2006) · Trends in Cell Biology · doi:10.1016/j.tcb.2006.08.009 · Cited by 431 · see citing works

Reactive Oxygen Species in Mitochondria-Mediated Cell Death

Orrenius, S. (2007) · Drug metabolism reviews (Softcover ed.) · doi:10.1080/03602530701468516 · Cited by 455 · see citing works

Lipids do influence protein function—the hydrophobic matching hypothesis revisited

Jensen, M. Ø., & Mouritsen, O. G. (2004) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2004.06.009 · Cited by 412 · see citing works

Cell Death Mechanisms and Their Implications in Toxicology

Orrenius, S., Nicotera, P., & Zhivotovsky, B. (2010) · Toxicological Sciences · doi:10.1093/toxsci/kfq268 · Cited by 412 · see citing works

How biology handles nitrite

Maia, L. B., & Moura, J. J. G. (2014) · Chemical Reviews · doi:10.1021/cr400518y · Cited by 401 · see citing works

Peroxidase Activity and Structural Transitions of Cytochrome<i>c</i>Bound to Cardiolipin-Containing Membranes

Belikova, N. A., Vladimirov, Y. A., Osipov, A. N., Kapralov, A. A., Tyurin, V. A., Potapovich, M. V., Basova, L. V., Peterson, J., Kurnikov, I. V., & Kagan, V. E. (2006) · Biochemistry · doi:10.1021/bi0525573 · Cited by 398 · see citing works

Glutathione and apoptosis

Circu, M. L., & Aw, T. Y. (2008) · Free Radical Research · doi:10.1080/10715760802317663 · Cited by 392 · see citing works

Role of reactive oxygen species and cardiolipin in the release of cytochrome c from mitochondria

Petrosillo, G., Ruggiero, F. M., & Paradies, G. (2003) · The FASEB Journal · doi:10.1096/fj.03-0012com · Cited by 384 · see citing works

Oxidative lipidomics of apoptosis: redox catalytic interactions of cytochrome c with cardiolipin and phosphatidylserine

Kagan, V. E., Borisenko, G. G., Tyurina, Y. Y., Tyurin, V. A., Jiang, J., Potapovich, A. I., Kini, V., Amoscato, A. A., & Fujii, Y. (2004) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2004.08.016 · Cited by 342 · see citing works

ROLE of MITOCHONDRIA in TOXIC OXIDATIVE STRESS

Fariss, M. W. (2005) · Molecular Interventions · doi:10.1124/mi.5.2.7 · Cited by 288 · see citing works

Cardiolipin and apoptosis

McMillin, J. B., & Dowhan, W. (2002) · Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids · doi:10.1016/s1388-1981(02)00329-3 · Cited by 266 · see citing works

Cardiolipin acts as a mitochondrial signalling platform to launch apoptosis

Schug, Z. T., & Gottlieb, E. (2009) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2009.05.004 · Cited by 259 · see citing works

Multifunctional Cytochrome c : Learning New Tricks from an Old Dog

Álvarez-Paggi, D., Hannibal, L., Castro, M. A., Rouco, S. O., Demicheli, V., Tórtora, V., Tomasina, F., Radí, R., & Murgida, D. H. (2017) · Chemical Reviews · doi:10.1021/acs.chemrev.7b00257 · Cited by 253 · see citing works

Cytochrome c: An extreme multifunctional protein with a key role in cell fate

Santucci, R., Sinibaldi, F., Cozza, P., Polticelli, F., & Fiorucci, L. (2019) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2019.06.180 · Cited by 250 · see citing works

Mitochondrial dysfunction in heart failure

Rosca, M. G., & Hoppel, C. L. (2012) · Heart Failure Reviews · doi:10.1007/s10741-012-9340-0 · Cited by 250 · see citing works

The cardiolipin–cytochrome c interaction and the mitochondrial regulation of apoptosis

Iverson, S. L., & Orrenius, S. (2004) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2003.12.002 · Cited by 235 · see citing works

Neuronal Apoptosis in Neurodegeneration

Okouchi, M., Ekshyyan, O. Y., Maracine, M., & Aw, T. Y. (2007) · Antioxidants and Redox Signaling · doi:10.1089/ars.2007.1511 · Cited by 219 · see citing works

Nitrite reductase activity of cytochrome c

Basu, S., Azarova, N. A., Font, M. D., King, S. B., Hogg, N., Gladwin, M. T., Shiva, S., & Kim-Shapiro, D. B. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m806934200 · Cited by 214 · see citing works

Oxidative stress and cell death

Rumora, L., Petrik, J., & Žanić‐Grubišić, T. (2003) · Cited by 192 · see citing works

Melatonin protects against heart ischemia-reperfusion injury by inhibiting mitochondrial permeability transition pore opening

Petrosillo, G., Colantuono, G., Moro, N., Ruggiero, F. M., Tiravanti, E., Venosa, N. D., Fiore, T., & Paradies, G. (2009) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.00163.2009 · Cited by 168 · see citing works

Cardiolipin and Its Different Properties in Mitophagy and Apoptosis

Li, X.-X., Tsoi, B., Li, Y.-F., Kurihara, H., & He, R. (2015) · Journal of Histochemistry & Cytochemistry · doi:10.1369/0022155415574818 · Cited by 169 · see citing works

Cytochrome c polymerization by successive domain swapping at the C-terminal helix

Hirota, S., Hattori, Y., Nagao, S., Taketa, M., Komori, H., Kamikubo, H., Wang, Z., Takahashi, I., Negi, S., Sugiura, Y., et al. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1001839107 · Cited by 164 · see citing works

Overexpression of glutaredoxin 2 attenuates apoptosis by preventing cytochrome c release

Enoksson, M., Fernandes, A. P., Prast‐Nielsen, S., Lillig, C. H., Holmgren, A., & Orrenius, S. (2004) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2004.12.067 · Cited by 162 · see citing works

Mechanisms of nitrite bioactivation

Kim-Shapiro, D. B., & Gladwin, M. T. (2014) · Nitric Oxide · doi:10.1016/j.niox.2013.11.002 · Cited by 157 · see citing works

Ca2+-induced Reactive Oxygen Species Production Promotes Cytochrome c Release from Rat Liver Mitochondria via Mitochondrial Permeability Transition (MPT)-dependent and MPT-independent Mechanisms

Petrosillo, G., Ruggiero, F. M., Pistolese, M., & Paradies, G. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m407500200 · Cited by 154 · see citing works

Redox Control of the Survival of Healthy and Diseased Cells

Zhang, Y., Du, Y., Le, W., Wang, K., Kieffer, N., & Zhang, J. (2011) · Antioxidants and Redox Signaling · doi:10.1089/ars.2010.3685 · Cited by 156 · see citing works

Oxidative Stress, Mitochondrial Dysfunction, and Neuroprotection of Polyphenols with Respect to Resveratrol in Parkinson’s Disease

Kung, H., Lin, K.-J., Kung, C., & Lin, T. (2021) · Biomedicines · doi:10.3390/biomedicines9080918 · Cited by 160 · see citing works

Cardiolipin deficiency releases cytochrome c from the inner mitochondrial membrane and accelerates stimuli-elicited apoptosis

Choi, S.-Y., Gonzalvez, F., Jenkins, G. M., Slomianny, C., Chrétien, D., Arnoult, D., PETIT, P. X., & Frohman, M. A. (2006) · Cell Death and Differentiation · doi:10.1038/sj.cdd.4402020 · Cited by 151 · see citing works

Cell membranes and apoptosis: role of cardiolipin, phosphatidylcholine, and anticancer lipid analogues

Wright, M. M., Howe, A. G., & Zaremberg, V. (2004) · Biochemistry and Cell Biology · doi:10.1139/o03-092 · Cited by 151 · see citing works

Mitochondrial mislocalization and altered assembly of a cluster of Barth syndrome mutant tafazzins

Claypool, S. M., McCaffery, J. M., & Koehler, C. M. (2006) · The Journal of Cell Biology · doi:10.1083/jcb.200605043 · Cited by 150 · see citing works

Metalloprotein entatic control of ligand-metal bonds quantified by ultrafast x-ray spectroscopy

Mara, M. W., Hadt, R. G., Reinhard, M., Kröll, T., Lim, H., Hartsock, R. W., Alonso‐Mori, R., Chollet, M., Glownia, J. M., Nelson, S., et al. (2017) · Science · doi:10.1126/science.aam6203 · Cited by 143 · see citing works

Oxidized phosphatidylcholines in membrane‐level cellular signaling: from biophysics to physiology and molecular pathology

Volinsky, R., & Kinnunen, P. K. J. (2013) · FEBS Journal · doi:10.1111/febs.12247 · Cited by 141 · see citing works

Mitochondrial bioenergetics and cardiolipin alterations in myocardial ischemia-reperfusion injury: implications for pharmacological cardioprotection

Paradies, G., Paradies, V., Ruggiero, F. M., & Petrosillo, G. (2018) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.00028.2018 · Cited by 143 · see citing works

Cytochrome c causes pore formation in cardiolipin-containing membranes

Bergstrom, C. L., Beales, P. A., Lv, Y., Vanderlick, T. K., & Groves, J. T. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1303819110 · Cited by 138 · see citing works

Interaction of peroxidized cardiolipin with rat‐heart mitochondrial membranes: Induction of permeability transition and cytochrome <i>c</i> release

Petrosillo, G., Casanova, G., Matera, M., Ruggiero, F. M., & Paradies, G. (2006) · FEBS Letters · doi:10.1016/j.febslet.2006.10.036 · Cited by 137 · see citing works

Lipids, curvature, and nano‐medicine

Mouritsen, O. G. (2011) · European Journal of Lipid Science and Technology · doi:10.1002/ejlt.201100050 · Cited by 137 · see citing works

Improving mitochondrial function with SS-31 reverses age-related redox stress and improves exercise tolerance in aged mice

Campbell, M. D., Duan, J., Samuelson, A. T., Gaffrey, M. J., Merrihew, G. E., Egertson, J. D., Wang, L., Bammler, T. K., Moore, R. J., White, C. C., et al. (2018) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2018.12.031 · Cited by 134 · see citing works

Alternative Conformations of Cytochrome c : Structure, Function, and Detection

Hannibal, L., Tomasina, F., Capdevila, D. A., Demicheli, V., Tórtora, V., Álvarez-Paggi, D., Jemmerson, R., Murgida, D. H., & Radí, R. (2015) · Biochemistry · doi:10.1021/acs.biochem.5b01385 · Cited by 132 · see citing works

Cardiolipin and Mitochondrial Function in Health and Disease

Paradies, G., Paradies, V., Ruggiero, F. M., & Petrosillo, G. (2013) · Antioxidants and Redox Signaling · doi:10.1089/ars.2013.5280 · Cited by 131 · see citing works

Cardiolipin Interactions with Proteins

Planas-Iglesias, J., Dwarakanath, H., Mohammadyani, D., Yanamala, N. V. K., Kagan, V. E., & Klein‐Seetharaman, J. (2015) · Biophysical Journal · doi:10.1016/j.bpj.2015.07.034 · Cited by 127 · see citing works

Insights into Cytochrome c−Cardiolipin Interaction. Role Played by Ionic Strength

Sinibaldi, F., Fiorucci, L., Patriarca, A., Lauceri, R., Ferri, T., Coletta, M., & Santucci, R. (2008) · Biochemistry · doi:10.1021/bi800048v · Cited by 129 · see citing works

Cytochrome c impaled: investigation of the extended lipid anchorage of a soluble protein to mitochondrial membrane models

Kalanxhi, E., & Wallace, C. J. A. (2007) · Biochemical Journal · doi:10.1042/bj20070459 · Cited by 128 · see citing works

Characterization of Two Oxidatively Modified Phospholipids in Mixed Monolayers with DPPC

Sabatini, K., Mattila, J.-P., Megli, F. M., & Kinnunen, P. K. J. (2006) · Biophysical Journal · doi:10.1529/biophysj.105.080176 · Cited by 126 · see citing works

Mass‐spectrometry based oxidative lipidomics and lipid imaging: applications in traumatic brain injury

Sparvero, L. J., Amoscato, A. A., Kochanek, P. M., Pitt, B. R., Kagan, V. E., & Bayır, H. (2010) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2010.07055.x · Cited by 121 · see citing works

Extended cardiolipin anchorage to cytochrome c: a model for protein–mitochondrial membrane binding

Sinibaldi, F., Howes, B. D., Piro, M. C., Polticelli, F., Bombelli, C., Ferri, T., Coletta, M., Smulevich, G., & Santucci, R. (2010) · JBIC Journal of Biological Inorganic Chemistry · doi:10.1007/s00775-010-0636-z · Cited by 117 · see citing works

The Hierarchy of Structural Transitions Induced in Cytochrome c by Anionic Phospholipids Determines Its Peroxidase Activation and Selective Peroxidation during Apoptosis in Cells

Kapralov, A. A., Kurnikov, I. V., Vlasova, I. I., Belikova, N. A., Tyurin, V. A., Basova, L. V., Zhao, Q., Tyurina, Y. Y., Jiang, J., Bayır, H., et al. (2007) · Biochemistry · doi:10.1021/bi701237b · Cited by 117 · see citing works

Melatonin inhibits cardiolipin peroxidation in mitochondria and prevents the mitochondrial permeability transition and cytochrome c release

Petrosillo, G., Moro, N., Ruggiero, F. M., & Paradies, G. (2009) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2009.06.032 · Cited by 117 · see citing works

Known unknowns of cardiolipin signaling: The best is yet to come

Maguire, J. J., Tyurina, Y. Y., Mohammadyani, D., Kapralov, A. A., Anthonymuthu, T. S., Qu, F., Amoscato, A. A., Sparvero, L. J., Tyurin, V. A., Planas-Iglesias, J., et al. (2016) · Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids · doi:10.1016/j.bbalip.2016.08.001 · Cited by 116 · see citing works

Caspase-2 Permeabilizes the Outer Mitochondrial Membrane and Disrupts the Binding of Cytochrome c to Anionic Phospholipids

Enoksson, M., Robertson, J. D., Gogvadze, V. G., Bu, P., Kropotov, A., Zhivotovsky, B., & Orrenius, S. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.c400374200 · Cited by 115 · see citing works

pH-dependent Interaction of Cytochrome c with Mitochondrial Mimetic Membranes

Kawai, C., Prado, F. M., Nunes, G. L. C., Mascio, P. D., Carmona‐Ribeiro, A. M., & Nantes, I. L. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m412532200 · Cited by 113 · see citing works

Peripheral and Integral Binding of Cytochrome c to Phospholipids Vesicles

Oellerich, S., Lecomte, S., Paternostre, M., Heimburg, T., & Hildebrandt, P. (2004) · The Journal of Physical Chemistry B · doi:10.1021/jp036799t · Cited by 111 · see citing works

Membrane Synthesis, Specific Lipid Requirements, and Localized Lipid Composition Changes Associated with a Positive-Strand RNA Virus RNA Replication Protein

Lee, W.-M., & Ahlquist, P. (2003) · Journal of Virology · doi:10.1128/jvi.77.23.12819-12828.2003 · Cited by 110 · see citing works

Cytochrome c: the Achilles’ heel in apoptosis

Kulikov, A. V., Shilov, E. S., Mufazalov, I. A., Gogvadze, V. G., Nedospasov, S. A., & Zhivotovsky, B. (2011) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-011-0895-z · Cited by 109 · see citing works

The “pro-apoptotic genies” get out of mitochondria: Oxidative lipidomics and redox activity of cytochrome c/cardiolipin complexes

Kagan, V. E., Tyurina, Y. Y., Bayır, H., Chu, C. T., Kapralov, A. A., Vlasova, I. I., Belikova, N. A., Tyurin, V. A., Amoscato, A. A., Epperly, M. W., et al. (2006) · Chemico-Biological Interactions · doi:10.1016/j.cbi.2006.04.019 · Cited by 109 · see citing works

Mitochondrial regulation of apoptotic cell death

Gogvadze, V. G., & Orrenius, S. (2006) · Chemico-Biological Interactions · doi:10.1016/j.cbi.2006.04.010 · Cited by 109 · see citing works

Hemigramicidin–TEMPO conjugates: Novel mitochondria-targeted anti-oxidants

Fink, M. P., Macias, C. A., Xiao, J., Tyurina, Y. Y., Jiang, J., Belikova, N. A., Delude, R. L., Greenberger, J. S., Kagan, V. E., & Wipf, P. (2007) · Biochemical Pharmacology · doi:10.1016/j.bcp.2007.05.019 · Cited by 107 · see citing works

Oxidative stress in neurodegeneration and available means of protection

Fatokun, A. A. (2008) · Frontiers in bioscience · doi:10.2741/2926 · Cited by 105 · see citing works

Appetizing rancidity of apoptotic cells for macrophages: oxidation, externalization, and recognition of phosphatidylserine

Kagan, V. E., Borisenko, G. G., Serinkan, B. F., Tyurina, Y. Y., Tyurin, V. A., Jiang, J., Liu, S. X., Shvedova, A. A., Fabisiak, J. P., Uthaisang, W., et al. (2003) · American Journal of Physiology-Lung Cellular and Molecular Physiology · doi:10.1152/ajplung.00365.2002 · Cited by 105 · see citing works

The interactions of peripheral membrane proteins with biological membranes

Whited, A. M., & Johs, A. (2015) · Chemistry and Physics of Lipids · doi:10.1016/j.chemphyslip.2015.07.015 · Cited by 104 · see citing works

Disruption of the M80-Fe ligation stimulates the translocation of cytochrome c to the cytoplasm and nucleus in nonapoptotic cells

Godoy, L. C., Muñoz‐Pinedo, C., Castro, L., Cardaci, S., Schonhoff, C. M., King, M., Tórtora, V., Marı́n, M., Miao, Q., Jiang, J. F., et al. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0809279106 · Cited by 101 · see citing works

Coenzyme Q supplementation or over-expression of the yeast Coq8 putative kinase stabilizes multi-subunit Coq polypeptide complexes in yeast coq null mutants

He, C. H., Xie, L. X., Allan, C. M., Tran, U. C., & Clarke, C. F. (2014) · Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids · doi:10.1016/j.bbalip.2013.12.017 · Cited by 95 · see citing works

Structure of the myristylated human immunodeficiency virus type 2 matrix protein and the role of phosphatidylinositol-(4,5)-bisphosphate in membrane targeting

Saad, J. S., Ablan, S. D., Ghanam, R. H., Kim, A., Andrews, K., Nagashima, K., Soheilian, F., Freed, E. O., & Summers, M. F. (2008) · Journal of Molecular Biology · doi:10.1016/j.jmb.2008.07.027 · Cited by 95 · see citing works

Mitochondria‐targeted disruptors and inhibitors of cytochrome c /cardiolipin peroxidase complexes: A new strategy in anti‐apoptotic drug discovery

Kagan, V. E., Bayır, A. G., Bayır, H., Stoyanovsky, D. A., Borisenko, G. G., Tyurina, Y. Y., Wipf, P., Atkinson, J., Greenberger, J. S., Chapkin, R. S., et al. (2008) · Molecular Nutrition & Food Research · doi:10.1002/mnfr.200700402 · Cited by 90 · see citing works

Structural and Molecular Determinants of Membrane Binding by the HIV-1 Matrix Protein

Mercredi, P. Y., Bucca, N., Loeliger, B., Gaines, C. R., Mehta, M., Bhargava, P., Tedbury, P. R., Charlier, L., Floquet, N., Muriaux, D. M., et al. (2016) · Journal of Molecular Biology · doi:10.1016/j.jmb.2016.03.005 · Cited by 87 · see citing works

Mitochondrial kinases and their molecular interaction with cardiolipin

Schlattner, U., Tokarska-Schlattner, M., Ramírez‐Ríos, S., Brückner, A., Kay, L., Polge, C., Epand, R. F., Lee, R. M., Lacombe, M., & Epand, R. M. (2009) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2009.04.018 · Cited by 89 · see citing works

Role of Lysines in Cytochrome c–Cardiolipin Interaction

Sinibaldi, F., Howes, B. D., Droghetti, E., Polticelli, F., Piro, M. C., Pierro, D. D., Fiorucci, L., Coletta, M., Smulevich, G., & Santucci, R. (2013) · Biochemistry · doi:10.1021/bi400324c · Cited by 89 · see citing works

Cardiac mitochondria in heart failure: Normal cardiolipin profile and increased threonine phosphorylation of complex IV

Rosca, M. G., Minkler, P. E., & Hoppel, C. L. (2011) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2011.02.003 · Cited by 88 · see citing works

The hydrogen-peroxide-induced radical behaviour in human cytochrome c–phospholipid complexes: implications for the enhanced pro-apoptotic activity of the G41S mutant

Rajagopal, B. S., Edzuma, A. N., Hough, M. A., Blundell, K. L. I. M., Kagan, V. E., Kapralov, A. A., Fraser, L. A., Butt, J. N., Silkstone, G. G. A., Wilson, M. T., et al. (2013) · Biochemical Journal · doi:10.1042/bj20130758 · Cited by 88 · see citing works

Structural Changes and Proapoptotic Peroxidase Activity of Cardiolipin-Bound Mitochondrial Cytochrome c

Mandal, A., Hoop, C. L., DeLucia, M., Kodali, R. B., Kagan, V. E., Ahn, J., & van der Wel, P. C. A. (2015) · Biophysical Journal · doi:10.1016/j.bpj.2015.09.016 · Cited by 87 · see citing works

Mitochondria in the elderly: Is acetylcarnitine a rejuvenator?☆

Rosca, M. G., Lemieux, H., & Hoppel, C. L. (2009) · Advanced Drug Delivery Reviews · doi:10.1016/j.addr.2009.06.009 · Cited by 87 · see citing works

Treatment With a Novel Hemigramicidin-TEMPO Conjugate Prolongs Survival in a Rat Model of Lethal Hemorrhagic Shock

Macias, C. A., Chiao, J. W., Xiao, J., Arora, D. S., Tyurina, Y. Y., Delude, R. L., Wipf, P., Kagan, V. E., & Fink, M. P. (2007) · Annals of Surgery · doi:10.1097/01.sla.0000236626.57752.8e · Cited by 86 · see citing works

Hemigramicidin-TEMPO conjugates: Novel mitochondria-targeted antioxidants

Fink, M. P., Macias, C. A., Xiao, J., Tyurina, Y. Y., Delude, R. L., Greenberger, J. S., Kagan, V. E., & Wipf, P. (2007) · Critical Care Medicine · doi:10.1097/01.ccm.0000279192.96303.e7 · Cited by 79 · see citing works

Evolution of cytochrome bc complexes: From membrane-anchored dehydrogenases of ancient bacteria to triggers of apoptosis in vertebrates

Dibrova, D. V., Cherepanov, D. A., Galperin, M. Y., Skulachev, V. P., & Mulkidjanian, A. Y. (2013) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2013.07.006 · Cited by 76 · see citing works

New insights into mitochondrial structure during cell death

Perkins, G. A., Bossy‐Wetzel, E., & Ellisman, M. H. (2009) · Experimental Neurology · doi:10.1016/j.expneurol.2009.05.021 · Cited by 76 · see citing works

Protein-oxidized phospholipid interactions in cellular signaling for cell death: From biophysics to clinical correlations

Kinnunen, P. K. J., Kaarniranta, K., & Mahalka, A. K. (2012) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2012.04.008 · Cited by 75 · see citing works

Dynamic death decisions: How mitochondrial dynamics shape cellular commitment to apoptosis and ferroptosis

Khatun, J., Gelles, J. D., & Chipuk, J. E. (2024) · Developmental Cell · doi:10.1016/j.devcel.2024.09.004 · Cited by 75 · see citing works

Interaction of Carbon Monoxide with the Apoptosis-Inducing Cytochrome c−Cardiolipin Complex

Kapetanaki, S. M., Silkstone, G. G. A., Husu, I., Liebl, U., Wilson, M. T., & Vos, M. H. (2009) · Biochemistry · doi:10.1021/bi801817v · Cited by 75 · see citing works

Cytochrome c Interaction with Cardiolipin/Phosphatidylcholine Model Membranes: Effect of Cardiolipin Protonation

Gorbenko, G. P., Molotkovsky, J. G., & Kinnunen, P. K. J. (2006) · Biophysical Journal · doi:10.1529/biophysj.105.080150 · Cited by 75 · see citing works

Structural transformations of cytochrome c upon interaction with cardiolipin

Muenzner, J., & Pletneva, E. V. (2014) · Chemistry and Physics of Lipids · doi:10.1016/j.chemphyslip.2013.11.002 · Cited by 74 · see citing works

Increased susceptibility to Ca 2+ ‐induced permeability transition and to cytochrome c release in rat heart mitochondria with aging: effect of melatonin

Petrosillo, G., Moro, N., Paradies, V., Ruggiero, F. M., & Paradies, G. (2010) · Journal of Pineal Research · doi:10.1111/j.1600-079x.2010.00758.x · Cited by 73 · see citing works

Cardiolipin Is Not Required for Bax-mediated Cytochrome c Release from Yeast Mitochondria

Iverson, S. L., Enoksson, M., Gogvadze, V. G., Ott, M., & Orrenius, S. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m305020200 · Cited by 73 · see citing works

Single Vesicle Observations of the Cardiolipin−CytochromecInteraction: Induction of Membrane Morphology Changes

Beales, P. A., Bergstrom, C. L., Geerts, N., Groves, J. T., & Vanderlick, T. K. (2011) · Langmuir · doi:10.1021/la104924c · Cited by 72 · see citing works

Emerging roles of lipids in BCL-2 family-regulated apoptosis

Zhang, T., & Saghatelian, A. (2013) · Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids · doi:10.1016/j.bbalip.2013.03.001 · Cited by 72 · see citing works

Resonance Raman Investigations of Cytochrome c Conformational Change upon Interaction with the Membranes of Intact and Ca2+-Exposed Mitochondria

Berezhna, S. Y., Wohlrab, H., & Champion, P. M. (2003) · Biochemistry · doi:10.1021/bi027387y · Cited by 70 · see citing works

Betulinic acid induces a novel cell death pathway that depends on cardiolipin modification

Potze, L., Franco, S. D., Grandela, C., Pras‐Raves, M. L., Picavet, D. I., van Veen, H. A., van LENTHE, H., Mullauer, F. B., van der Wel, N. N., Luyf, A. C. M., et al. (2015) · Oncogene · doi:10.1038/onc.2015.102 · Cited by 69 · see citing works

Model Answers to Lipid Membrane QuestionsPreprint

Mouritsen, O. G. (2011) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a004622 · Cited by 69 · see citing works

Cytochrome c-induced lymphocyte death from the outside in: inhibition by serum leucine-rich alpha-2-glycoprotein-1

Codina, R., Vanasse, A., Kelekar, A., Vezys, V., & Jemmerson, R. (2009) · APOPTOSIS · doi:10.1007/s10495-009-0412-0 · Cited by 68 · see citing works

Cytochrome c impaled: investigation of the extended lipid anchorage of a soluble protein to mitochondrial membrane models

Kalanxhi, E., & Wallace, C. J. A. (2007) · Biochemical Journal · doi:10.1042/bj20070459 · Cited by 128 · see citing works

Phospholipid cytochrome c interactions

Tuominen, E. (2010) · Työväentutkimus Vuosikirja

Binding and Dissociation of Cytochrome c to and from Membranes Containing Acidic Phospholipids

Subramanian, M., Jutila, A., & Kinnunen, P. K. J. (1998) · Biochemistry · doi:10.1021/bi9716581 · Cited by 49 · see citing works

Binding of cytochrome c to liposomes as revealed by the quenching of fluorescence from pyrene-labeled phospholipids

Mustonen, P., Virtanen, J. A., Somerharju, P. J., & Kinnunen, P. K. J. (1987) · Biochemistry · doi:10.1021/bi00385a006 · Cited by 108 · see citing works

Interaction of cytochrome c and its precursor apocytochrome c with various phospholipids

Rietveld, A. G., Sijens, P., Verkleij, A. J., & KRUIJFF, B. D. (1983) · The EMBO Journal · doi:10.1002/j.1460-2075.1983.tb01520.x · Cited by 91 · see citing works