Walter and Eliza Hall Institute of Medical Research
Australia
Ruth M. Kluck mainly focuses on Cell biology, Bcl-2-associated X protein, Mitochondrion, Bcl-2 Homologous Antagonist-Killer Protein and Cytochrome c. Her Cell biology research is multidisciplinary, incorporating elements of Protein structure, Apoptosis, Molecular biology and Apoptosome. The study incorporates disciplines such as Plasma protein binding, Protein multimerization and Caspase-9, Caspase, Caspase 6 in addition to Molecular biology.
Her studies in Apoptosome integrate themes in fields like Intermembrane space, Cytochrome c oxidase and Cytochrome P450 reductase. Her research integrates issues of Endoplasmic reticulum and Organelle in her study of Mitochondrion. Her biological study spans a wide range of topics, including Dimer, Structure–activity relationship, Signal transduction and Binding site.
Her primary areas of investigation include Cell biology, Apoptosis, Bcl-2 Homologous Antagonist-Killer Protein, Mitochondrion and Bcl-2-associated X protein. Ruth M. Kluck interconnects Protein structure, VDAC2 and Programmed cell death in the investigation of issues within Cell biology. Her research in Apoptosis intersects with topics in Molecular biology and Protein multimerization.
Her work deals with themes such as Plasma protein binding, Oligomer, Dimer, Transmembrane domain and Conformational change, which intersect with Bcl-2 Homologous Antagonist-Killer Protein. Her Bcl-2-associated X protein research incorporates elements of Granzyme B, Bcl-2 family, Intrinsic apoptosis, Membrane protein and Binding site. Her Cytochrome c research incorporates themes from Cytochrome c oxidase, Apoptosome and Mitochondrial intermembrane space.
Her main research concerns Cell biology, Apoptosis, Mitochondrion, Bcl-2-associated X protein and Bcl-2 Homologous Antagonist-Killer Protein. Ruth M. Kluck has included themes like Biochemistry and Programmed cell death in her Cell biology study. Her work on Apoptotic cell death and Mitochondrial pathway as part of general Apoptosis study is frequently connected to Protein family and Venetoclax, therefore bridging the gap between diverse disciplines of science and establishing a new relationship between them.
Ruth M. Kluck combines subjects such as Molecular biology and Granzyme B with her study of Mitochondrion. Her Bcl-2-associated X protein study combines topics from a wide range of disciplines, such as Cytochrome c, Intrinsic apoptosis and Binding site. Her work carried out in the field of Bcl-2 Homologous Antagonist-Killer Protein brings together such families of science as BH3 Mimetic ABT-737 and Mitochondrial apoptosis-induced channel, Inner mitochondrial membrane.
Ruth M. Kluck mainly investigates Bcl-2 Homologous Antagonist-Killer Protein, Cell biology, Programmed cell death, Bcl-2-associated X protein and Apoptosis. Her Bcl-2 Homologous Antagonist-Killer Protein research includes elements of Oligomer, Structural biology, Membrane, Transmembrane domain and Conformational change. Ruth M. Kluck performs integrative study on Cell biology and Protein family in her works.
Her studies deal with areas such as Granzyme B and Mitochondrion as well as Programmed cell death. As part of her studies on Bcl-2-associated X protein, Ruth M. Kluck often connects relevant areas like Molecular biology. Her work on Intrinsic apoptosis as part of general Apoptosis research is frequently linked to Carcinogenesis, thereby connecting diverse disciplines of science.
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The Release of Cytochrome c from Mitochondria: A Primary Site for Bcl-2 Regulation of Apoptosis
Ruth M. Kluck;Ella Bossy-Wetzel;Douglas R. Green;Donald D. Newmeyer.
Science (1997)
Ordering the cytochrome c-initiated caspase cascade: hierarchical activation of caspases-2, -3, -6, -7, -8, and -10 in a caspase-9-dependent manner.
Elizabeth A. Slee;Mary T. Harte;Ruth M. Kluck;Beni B. Wolf.
Journal of Cell Biology (1999)
Apoptosis Initiated When BH3 Ligands Engage Multiple Bcl-2 Homologs, Not Bax or Bak
Simon N. Willis;Jamie I. Fletcher;Thomas Kaufmann;Mark F. van Delft;Mark F. van Delft.
Science (2007)
Molecular biology of Bax and Bak activation and action
Dana Westphal;Grant Dewson;Peter E. Czabotar;Ruth M. Kluck.
Biochimica et Biophysica Acta (2011)
Cytochrome c activation of CPP32‐like proteolysis plays a critical role in a Xenopus cell‐free apoptosis system
Ruth M. Kluck;Seamus J. Martin;Brian M. Hoffman;Jian S. Zhou.
The EMBO Journal (1997)
Bax Crystal Structures Reveal How Bh3 Domains Activate Bax and Nucleate its Oligomerization to Induce Apoptosis.
Peter E. Czabotar;Peter E. Czabotar;Dana Westphal;Dana Westphal;Grant Dewson;Grant Dewson;Stephen Ma;Stephen Ma.
Cell (2013)
The Pro-Apoptotic Proteins, Bid and Bax, Cause a Limited Permeabilization of the Mitochondrial Outer Membrane That Is Enhanced by Cytosol
Ruth M Kluck;Mauro Dogli Esposti;Guy Perkins;Christian Renken.
Journal of Cell Biology (1999)
Mechanisms by which Bak and Bax permeabilise mitochondria during apoptosis
Grant Dewson;Ruth M. Kluck.
Journal of Cell Science (2009)
To trigger apoptosis, Bak exposes its BH3 domain and homodimerizes via BH3:groove interactions.
Grant Dewson;Tobias Kratina;Huiyan W. Sim;Hamsa Puthalakath.
Molecular Cell (2008)
Building blocks of the apoptotic pore: how Bax and Bak are activated and oligomerize during apoptosis.
D Westphal;R M Kluck;G Dewson.
Cell Death & Differentiation (2014)
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