Combined inhibition of aurora kinases and Bcl-xL induces apoptosis through select BH3-only proteins

[1]  B. Zhivotovsky,et al.  A link between mitotic defects and mitotic catastrophe: detection and cell fate , 2021, Biology Direct.

[2]  J. Shim,et al.  Aurora kinase A, a synthetic lethal target for precision cancer medicine , 2021, Experimental & Molecular Medicine.

[3]  Z. Dong,et al.  Targeting AURKA in Cancer: molecular mechanisms and opportunities for Cancer therapy , 2021, Molecular cancer.

[4]  A. Ugusman,et al.  Clinical Review: Navitoclax as a Pro-Apoptotic and Anti-Fibrotic Agent , 2020, Frontiers in Pharmacology.

[5]  Xu Luo,et al.  The third model of Bax/Bak activation: a Bcl-2 family feud finally resolved? , 2020, F1000Research.

[6]  I. Bellantuono,et al.  Senescence and Cancer: A Review of Clinical Implications of Senescence and Senotherapies , 2020, Cancers.

[7]  R. Poon,et al.  Aurora kinases and DNA damage response. , 2020, Mutation research.

[8]  G. Borgstahl,et al.  BH3-only proteins target BCL-xL/MCL-1, not BAX/BAK, to initiate apoptosis , 2019, Cell Research.

[9]  Sourav Bandyopadhyay,et al.  Aurora kinase A drives the evolution of resistance to third generation EGFR inhibitors in lung cancer , 2018, Nature Medicine.

[10]  B. Rogister,et al.  The functional diversity of Aurora kinases: a comprehensive review , 2018, Cell Division.

[11]  M. Butterworth,et al.  BH3-only proteins are dispensable for apoptosis induced by pharmacological inhibition of both MCL-1 and BCL-XL , 2018, Cell Death & Differentiation.

[12]  S. Cory,et al.  The BCL-2 arbiters of apoptosis and their growing role as cancer targets , 2017, Cell Death and Differentiation.

[13]  D. Green,et al.  MOMP, cell suicide as a BCL-2 family business , 2017, Cell Death and Differentiation.

[14]  Samir Guglani.  Death , 1890, The Lancet.

[15]  H. Bhatt,et al.  A comprehensive review on Aurora kinase: Small molecule inhibitors and clinical trial studies. , 2017, European journal of medicinal chemistry.

[16]  G. Kroemer,et al.  Caspase 2 in mitotic catastrophe: The terminator of aneuploid and tetraploid cells , 2017, Molecular & cellular oncology.

[17]  Junnian Zheng,et al.  Aurora kinases: novel therapy targets in cancers , 2017, Oncotarget.

[18]  Xu Luo,et al.  Inactivation of prosurvival Bcl-2 proteins activates Bax/Bak through the outer mitochondrial membrane , 2016, Genes & development.

[19]  Cory B. Giles,et al.  Identification of a novel senolytic agent, navitoclax, targeting the Bcl‐2 family of anti‐apoptotic factors , 2016, Aging cell.

[20]  K. Schindler,et al.  Functions of Aurora kinase C in meiosis and cancer , 2015, Front. Cell Dev. Biol..

[21]  S. Frank,et al.  Differential retrotranslocation of mitochondrial Bax and Bak , 2015, The EMBO journal.

[22]  M. Malumbres,et al.  Aurora kinase A inhibitors: promising agents in antitumoral therapy , 2014, Expert opinion on therapeutic targets.

[23]  Richard W. Kriwacki,et al.  Many players in BCL-2 family affairs. , 2014, Trends in biochemical sciences.

[24]  Peter E. Czabotar,et al.  Control of apoptosis by the BCL-2 protein family: implications for physiology and therapy , 2013, Nature Reviews Molecular Cell Biology.

[25]  M. Malumbres,et al.  Requirements for Aurora-A in tissue regeneration and tumor development in adult mammals. , 2013, Cancer research.

[26]  Erinna F. Lee,et al.  Bax Crystal Structures Reveal How BH3 Domains Activate Bax and Nucleate Its Oligomerization to Induce Apoptosis , 2013, Cell.

[27]  R. Splittgerber,et al.  Targeting aurora kinases limits tumour growth through DNA damage-mediated senescence and blockade of NF-κB impairs this drug-induced senescence , 2012, EMBO molecular medicine.

[28]  Roland L. Dunbrack,et al.  Aurora A kinase (AURKA) in normal and pathological cell division , 2013, Cellular and Molecular Life Sciences.

[29]  S. Geley,et al.  Caspase-2 at a glance , 2012, Journal of Cell Science.

[30]  Stephen L. Brown,et al.  Aurora A is differentially expressed in gliomas, is associated with patient survival in glioblastoma and is a potential chemotherapeutic target in gliomas , 2012, Cell cycle.

[31]  P. Lavia,et al.  Aurora-A inactivation causes mitotic spindle pole fragmentation by unbalancing microtubule-generated forces , 2011, Molecular Cancer.

[32]  L. Zhang,et al.  Selective involvement of BH3-only proteins and differential targets of Noxa in diverse apoptotic pathways , 2011, Cell Death and Differentiation.

[33]  K. Ryan,et al.  Phosphorylation of Puma modulates its apoptotic function by regulating protein stability , 2010, Cell Death and Disease.

[34]  Xu Luo,et al.  Perturbation of the Bcl-2 Network and an Induced Noxa/Bcl-xL Interaction Trigger Mitochondrial Dysfunction after DNA Damage* , 2010, The Journal of Biological Chemistry.

[35]  Jian Yu,et al.  PUMA, a potent killer with or without p53 , 2008, Oncogene.

[36]  Erinna F. Lee,et al.  Apoptosis Initiated When BH3 Ligands Engage Multiple Bcl-2 Homologs, Not Bax or Bak , 2007, Science.

[37]  Xu Luo,et al.  Cleavage by Caspase 8 and Mitochondrial Membrane Association Activate the BH3-only Protein Bid during TRAIL-induced Apoptosis* , 2006, The Journal of Biological Chemistry.

[38]  S. Willis,et al.  Life in the balance: how BH3-only proteins induce apoptosis. , 2005, Current opinion in cell biology.

[39]  Xuejun Jiang,et al.  Essential Roles of the Bcl-2 Family of Proteins in Caspase-2-induced Apoptosis* , 2005, Journal of Biological Chemistry.

[40]  S. Korsmeyer,et al.  An inhibitor of Bcl-2 family proteins induces regression of solid tumours , 2005, Nature.

[41]  Lin Chen,et al.  Proapoptotic Bak is sequestered by Mcl-1 and Bcl-xL, but not Bcl-2, until displaced by BH3-only proteins. , 2005, Genes & development.

[42]  Guido Kroemer,et al.  Cell death by mitotic catastrophe: a molecular definition , 2004, Oncogene.

[43]  S. Korsmeyer,et al.  Distinct BH3 domains either sensitize or activate mitochondrial apoptosis, serving as prototype cancer therapeutics. , 2002, Cancer cell.

[44]  S. Srinivasula,et al.  Caspase-2 Induces Apoptosis by Releasing Proapoptotic Proteins from Mitochondria* , 2002, The Journal of Biological Chemistry.

[45]  S. Korsmeyer,et al.  Proapoptotic BAX and BAK: A Requisite Gateway to Mitochondrial Dysfunction and Death , 2001, Science.

[46]  K. Vousden,et al.  PUMA, a novel proapoptotic gene, is induced by p53. , 2001, Molecular cell.

[47]  K. Kinzler,et al.  PUMA induces the rapid apoptosis of colorectal cancer cells. , 2001, Molecular cell.

[48]  A. Strasser,et al.  BH3-Only Proteins—Essential Initiators of Apoptotic Cell Death , 2000, Cell.

[49]  T. Taniguchi,et al.  Noxa, a BH3-only member of the Bcl-2 family and candidate mediator of p53-induced apoptosis. , 2000, Science.

[50]  Xiaodong Wang,et al.  Bid, a Bcl2 Interacting Protein, Mediates Cytochrome c Release from Mitochondria in Response to Activation of Cell Surface Death Receptors , 1998, Cell.

[51]  Junying Yuan,et al.  Cleavage of BID by Caspase 8 Mediates the Mitochondrial Damage in the Fas Pathway of Apoptosis , 1998, Cell.

[52]  S. Marsters,et al.  Induction of Apoptosis by Apo-2 Ligand, a New Member of the Tumor Necrosis Factor Cytokine Family* , 1996, The Journal of Biological Chemistry.