Kathleen W. Kinnally spends much of her time researching Cell biology, Mitochondrial apoptosis-induced channel, Mitochondrion, Inner mitochondrial membrane and Voltage-dependent anion channel. Cell biology is closely attributed to Apoptosis in her research. The study incorporates disciplines such as Bcl-2 family, Mitochondrial membrane transport protein and Mitochondrial permeability transition pore in addition to Mitochondrial apoptosis-induced channel.
Her study looks at the relationship between Mitochondrion and fields such as Ion channel, as well as how they intersect with chemical problems. The various areas that she examines in her Inner mitochondrial membrane study include Patch clamp and Inner membrane. She has included themes like Bacterial outer membrane, Biological membrane and Analytical chemistry in her Inner membrane study.
Her primary areas of investigation include Mitochondrion, Cell biology, Mitochondrial apoptosis-induced channel, Apoptosis and Inner mitochondrial membrane. The concepts of her Mitochondrion study are interwoven with issues in Bacterial outer membrane, Voltage-dependent anion channel, Patch clamp and Ion channel. Her Cell biology research includes themes of Molecular biology and Intermembrane space.
Her Mitochondrial apoptosis-induced channel research integrates issues from Bcl-2 family, Intracellular and Mitochondrial permeability transition pore. Her work on Programmed cell death as part of general Apoptosis study is frequently connected to Staurosporine, therefore bridging the gap between diverse disciplines of science and establishing a new relationship between them. In her research, Cyclosporin a is intimately related to Peptide, which falls under the overarching field of Inner mitochondrial membrane.
The scientist’s investigation covers issues in Cell biology, Mitochondrial apoptosis-induced channel, Apoptosis, Mitochondrion and Bacterial outer membrane. Her research integrates issues of Molecular biology, Programmed cell death and Voltage-dependent anion channel in her study of Cell biology. Her work carried out in the field of Mitochondrial apoptosis-induced channel brings together such families of science as Intermembrane space, Patch clamp, Bcl-2 family and Mitochondrial permeability transition pore.
In general Apoptosis, her work in Cytochrome c is often linked to Staurosporine linking many areas of study. She studies Inner mitochondrial membrane, a branch of Mitochondrion. Kathleen W. Kinnally works mostly in the field of Bacterial outer membrane, limiting it down to topics relating to Membrane and, in certain cases, Crystallography and Isolated mitochondria, as a part of the same area of interest.
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A novel, high conductance channel of mitochondria linked to apoptosis in mammalian cells and Bax expression in yeast.
Evgeny V. Pavlov;Muriel Priault;Dawn Pietkiewicz;Emily H.-Y. Cheng.
Journal of Cell Biology (2001)
Is mPTP the gatekeeper for necrosis, apoptosis, or both?
Kathleen W. Kinnally;Pablo M. Peixoto;Shin Young Ryu;Laurent M. Dejean.
Biochimica et Biophysica Acta (2011)
Oligomeric Bax Is a Component of the Putative Cytochrome c Release Channel MAC, Mitochondrial Apoptosis-induced Channel
Laurent M. Dejean;Sonia Martinez-Caballero;Liang Guo;Cynthia Hughes.
Molecular Biology of the Cell (2005)
A tale of two mitochondrial channels, MAC and PTP, in apoptosis
Kathleen W. Kinnally;Bruno Antonsson.
Regulation of the mitochondrial apoptosis-induced channel, MAC, by BCL-2 family proteins.
Laurent M. Dejean;Sonia Martinez-Caballero;Stephen Manon;Kathleen W. Kinnally.
Biochimica et Biophysica Acta (2006)
Mitochondrial benzodiazepine receptor linked to inner membrane ion channels by nanomolar actions of ligands
Kathleen W. Kinnally;Dmitry B. Zorov;Dmitry B. Zorov;Yuri N. Antonenko;Yuri N. Antonenko;Solomon H. Snyder.
Proceedings of the National Academy of Sciences of the United States of America (1993)
Mitochondrial Channel Activity Studied by Patch- Clamping Mitoplasts
Kathleen W. Kinnally;Maria Luisa Campo;Henry Tedeschi.
Journal of Bioenergetics and Biomembranes (1989)
Bax and Bak function as the outer membrane component of the mitochondrial permeability pore in regulating necrotic cell death in mice
Jason Karch;Jennifer Q. Kwong;Adam R. Burr;Michelle A. Sargent.
Is MAC the knife that cuts cytochrome c from mitochondria during apoptosis
L M Dejean;S Martinez-Caballero;K W Kinnally.
Cell Death & Differentiation (2006)
BH3 Death Domain Peptide Induces Cell Type-selective Mitochondrial Outer Membrane Permeability
Brian M. Polster;Kathleen W. Kinnally;Gary Fiskum.
Journal of Biological Chemistry (2001)
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