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Ruth M. Kluck

Ruth M. Kluck

Walter and Eliza Hall Institute of Medical Research
Australia

Overview

What is she best known for?

The fields of study she is best known for:

  • Amino acid
  • Apoptosis
  • Mitochondrion

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 most cited work include:

  • The Release of Cytochrome c from Mitochondria: A Primary Site for Bcl-2 Regulation of Apoptosis (4266 citations)
  • Ordering the Cytochrome c–initiated Caspase Cascade: Hierarchical Activation of Caspases-2, -3, -6, -7, -8, and -10 in a Caspase-9–dependent Manner (1704 citations)
  • Apoptosis Initiated When BH3 Ligands Engage Multiple Bcl-2 Homologs, Not Bax or Bak (983 citations)

What are the main themes of her work throughout her whole career to date?

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.

She most often published in these fields:

  • Cell biology (108.60%)
  • Apoptosis (58.06%)
  • Bcl-2 Homologous Antagonist-Killer Protein (70.97%)

What were the highlights of her more recent work (between 2016-2021)?

  • Cell biology (108.60%)
  • Apoptosis (58.06%)
  • Mitochondrion (63.44%)

In recent papers she was focusing on the following fields of study:

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.

Between 2016 and 2021, her most popular works were:

  • Disordered clusters of Bak dimers rupture mitochondria during apoptosis. (48 citations)
  • Disordered clusters of Bak dimers rupture mitochondria during apoptosis. (48 citations)
  • VDAC2 enables BAX to mediate apoptosis and limit tumor development. (47 citations)

In her most recent research, the most cited papers focused on:

  • Amino acid
  • Apoptosis
  • Biochemistry

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.

This overview was generated by a machine learning system which analysed the scientist’s body of work. If you have any feedback, you can contact us here.

Best Publications

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)

5995 Citations

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)

2455 Citations

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)

1403 Citations

Molecular biology of Bax and Bak activation and action

Dana Westphal;Grant Dewson;Peter E. Czabotar;Ruth M. Kluck.
Biochimica et Biophysica Acta (2011)

603 Citations

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)

565 Citations

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)

545 Citations

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)

399 Citations

Mechanisms by which Bak and Bax permeabilise mitochondria during apoptosis

Grant Dewson;Ruth M. Kluck.
Journal of Cell Science (2009)

362 Citations

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)

356 Citations

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)

343 Citations

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