Thomas W. Comollo
Rutgers University
9 Papers
2 Citations
Thomas W. Comollo is an academic researcher from Rutgers University. The author has contributed to research in topics: Chemistry & Medicine. The author has an hindex of 1, co-authored 5 publications. Previous affiliations of Thomas W. Comollo include Columbia University.
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Papers
Small molecule inhibitors block Gas6-inducible TAM activation and tumorigenicity
Stanley G. Kimani,Sushil Kumar,Nitu Bansal,Kamalendra Singh,Vladyslav Kholodovych,Thomas W. Comollo,Youyi Peng,Sergei V. Kotenko,Stefan G. Sarafianos,Joseph R. Bertino,William J. Welsh,Raymond B. Birge +11 more
TL;DR: Observations establish that small molecules that bind to the interface between TAM Ig1 domain and Gas6 Lg1 domain can inhibit TAM activation, and support the further development of small molecule Gas6-TAM interaction inhibitors as a novel class of cancer therapeutics.
Deficiency of mitochondrial calcium uniporter abrogates iron overload-induced cardiac dysfunction by reducing ferroptosis
Nadezhda Fefelova,Suwakon Wongjaikam,Sri Harika Pamarthi,Natthaphat Siri-Angkul,Thomas W. Comollo,Anshu Kumari,Andreas S. Ivessa,Siriporn C. Chattipakorn,Nipon Chattipakorn,Judith K. Gwathmey,Lai-Hua Xie +10 more
TL;DR: It is concluded that mitochondrial iron uptake is dependent on MCU, which plays an essential role in causing mitochondrial dysfunction and ferroptosis under iron overload conditions in the heart.
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Exploring mutation specific beta blocker pharmacology of the pathogenic late sodium channel current from patient-specific pluripotent stem cell myocytes derived from long QT syndrome mutation carriers
Thomas W. Comollo,Xinle Zou,Chuangeng Zhang,Divya Kesters,Thomas Hof,Kevin J. Sampson,Robert S. Kass +6 more
TL;DR: Investigation of the effects of the beta blocker propranolol on INaL expressed by ΔKPQ and E1784K channels in induced pluripotent stem cells derived from patients carrying these mutations suggests that the protective effects of proPRanolol in treating LQT3 patients is due in part to modulation of InaL.
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Molecular Modeling Suggests Homologous 2-APB Binding Sites in Connexins 26 and 32
TL;DR: Virtual screening results imply molecules with similar activity on Cx26 and Cx32 as 2- APB can be found, and modeling suggests that 2-APB binds to similar sites inside the pores of Cx 26 and CX32.
The β1'-β2' Motif of the RNase H Domain of Human Immunodeficiency Virus Type 1 Reverse Transcriptase Is Responsible for Conferring Open Conformation to the p66 Subunit by Displacing the Connection Domain from the Polymerase Cleft.
TL;DR: Results indicate that the β1'-β2' motif of the RNase H domain may be responsible for displacing the connection domain from the polymerase cleft of putative monomeric p66, which may then readily dimerize with p51 to assume a stable dimeric conformation.
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