J. Chipuk

Molecular Biology · 2004–2018

A researcher in the Science corpus: 10 papers; trusts 9 researchers and is trusted by 10 researchers here, as inferred from the citation graph.

Subfields

• Molecular Biology — 403 citations into it; #4,014 of 17,773 by trust here, #1,878 by citations

Whom J. Chipuk trusts overall

Their strongest outbound trust, strongest first, inferred from their citations.

1. T. Kuwana
2. A. Letai
3. L. Bouchier-Hayes
4. Douglas R. Green
5. W. Zong
6. Michael C. Bassik
7. S. Korsmeyer
8. D. Newmeyer
9. L. Scorrano
10. Simon N. Willis

Who trusts J. Chipuk overall

1. Douglas R. Green
2. Guido Kroemer
3. Angelina V. Vaseva
4. L. Galluzzi
5. R. Youle
6. R. Kang
7. V. Gogvadze
8. J. Martinou
9. K. Yip
10. S. Tait

Papers from J. Chipuk's perspective

Ordered by how strongly the researchers J. Chipuk trusts endorse each paper. Same corpus, a different order for every researcher.

1. Noxa, a BH3-only member of the Bcl-2 family and candidate mediator of p53-induced apoptosis. (Science)
2. The combined functions of proapoptotic Bcl-2 family members bak and bax are essential for normal development of multiple tissues. (Molecules and Cells)
3. Distinct BH3 domains either sensitize or activate mitochondrial apoptosis, serving as prototype cancer therapeutics. (Cancer Cell)
4. Differential targeting of prosurvival Bcl-2 proteins by their BH3-only ligands allows complementary apoptotic function. (Molecules and Cells)
5. PUMA, a novel proapoptotic gene, is induced by p53. (Molecules and Cells)
6. Elimination of Mcl-1 is required for the initiation of apoptosis following ultraviolet irradiation. (Genes & Development)
7. BH3-only proteins that bind pro-survival Bcl-2 family members fail to induce apoptosis in the absence of Bax and Bak. (Genes & Development)
8. An inhibitor of Bcl-2 family proteins induces regression of solid tumours (Nature)
9. BH3 domains of BH3-only proteins differentially regulate Bax-mediated mitochondrial membrane permeabilization both directly and indirectly. (Molecules and Cells)
10. BCL-2, BCL-X(L) sequester BH3 domain-only molecules preventing BAX- and BAK-mediated mitochondrial apoptosis. (Molecules and Cells)

Their papers

• Direct Activation of Bax by p53 Mediates Mitochondrial Membrane Permeabilization and Apoptosis (2004) — 2,147 citations
• Chemical inhibition of the mitochondrial division dynamin reveals its role in Bax/Bak-dependent mitochondrial outer membrane permeabilization. (2008) — 1,159 citations
• BH3 domains of BH3-only proteins differentially regulate Bax-mediated mitochondrial membrane permeabilization both directly and indirectly. (2005) — 1,255 citations
• Do inducers of apoptosis trigger caspase-independent cell death? (2005) — 341 citations
• Molecular mechanisms of cell death: recommendations of the Nomenclature Committee on Cell Death 2018 (2018) — 5,732 citations
• Essential versus accessory aspects of cell death: recommendations of the NCCD 2015 (2014) — 970 citations
• The BCL-2 Family Reunion (2010) — 1,486 citations
• How do BCL-2 proteins induce mitochondrial outer membrane permeabilization? (2008) — 1,023 citations
• Mitochondrial outer membrane permeabilization during apoptosis: the innocent bystander scenario (2006) — 614 citations
• Nanotubular Highways for Intercellular Organelle Transport (2004) — 754 citations