Timothy Marlowe
Roswell Park Cancer Institute
10 Papers
127 Citations
Timothy Marlowe is an academic researcher from Roswell Park Cancer Institute. The author has contributed to research in topics: Focal adhesion & Apoptosis. The author has an hindex of 6, co-authored 10 publications. Previous affiliations of Timothy Marlowe include University of Arizona.
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Papers
Oxidative phosphorylation-dependent regulation of cancer cell apoptosis in response to anticancer agents.
Neelu Yadav,Sandeep Kumar,Timothy Marlowe,Ajay K. Chaudhary,Rahul Kumar,Jianmin Wang,Jordan O'Malley,Patrick McKay Boland,Srinivas Jayanthi,Thallapuranam Krishnaswamy Suresh Kumar,Nagendra Yadava,Dhyan Chandra +11 more
TL;DR: It is concluded that DNA-damaging agents (etoposide and doxorubicin), ER stressor, and histone deacetylase inhibitor (apicidin) target oxidative phosphorylation (OXPHOS) for apoptosis induction, whereas other anticancer agents including staurosporine, taxol, and sorafenib induce apoptosis in an OXPHOS-independent manner.
Disrupting the scaffold to improve focal adhesion kinase-targeted cancer therapeutics.
TL;DR: Targeting the scaffold of focal adhesion kinase is a therapeutic opportunity to inhibit signaling pathways selectively in cancer cells and a feasible and promising approach for developing highly specific therapeutics that disrupt FAK signaling pathways in cancer.
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Reduced mitochondrial DNA content associates with poor prognosis of prostate cancer in African American men.
TL;DR: The data suggest that AA men possess lower mtDNA levels in normal and tumor tissues compared to CA men, which could contribute to higher risk and more aggressive prostate cancer in AA men.
Oncogenic Receptor Tyrosine Kinases Directly Phosphorylate Focal Adhesion Kinase (FAK) as a Resistance Mechanism to FAK-Kinase Inhibitors
TL;DR: It is demonstrated that receptor tyrosine kinases (RTK) can directly bypass FAK-kinase inhibition in cancer cells through phosphorylation of FAK's critical tyrosin 397 (Y397), and it is shown that HER2 forms a direct protein–protein interaction with theFAK-FERM-F1 lobe, promoting direct phosphorylations of Y397.
Mechanism of neem limonoids-induced cell death in cancer: Role of oxidative phosphorylation.
Neelu Yadav,Sandeep Kumar,Rahul Kumar,Pragya Srivastava,Leimin Sun,Péter Rapali,Timothy Marlowe,Andrea Schneider,Joseph R. Inigo,Jordan O'Malley,Ramesh Londonkar,Raghu Gogada,Ajay K. Chaudhary,Nagendra Yadava,Dhyan Chandra +14 more
TL;DR: It is demonstrated that neem limonoids target OXPHOS system to induce cancer cell death, which does not require upregulation or activation of proapoptotic Bcl-2 family proteins.
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