Zobrazeno 1 - 10
of 23
pro vyhledávání: '"Gulam M. Rather"'
Publikováno v:
Frontiers in Oncology, Vol 9 (2019)
Matriptase is a transmembrane serine protease, synthesized as an inactive single-chain zymogen on the endoplasmic reticulum and transported to the plasma membrane. Matriptase is activated in different epithelial and some B-cell malignancies and chang
Externí odkaz:
https://doaj.org/article/ed9517bd3eb145bc8156d8ec322620cc
Publikováno v:
Biomolecules, Vol 10, Iss 3, p 358 (2020)
Actively proliferating cancer cells require sufficient amount of NADH and NADPH for biogenesis and to protect cells from the detrimental effect of reactive oxygen species. As both normal and cancer cells share the same NAD biosynthetic and metabolic
Externí odkaz:
https://doaj.org/article/69440bc133a94c96b6bb4404e0fee88d
Autor:
Siang-Yo Lin, Mehdi Javanmard, Chen-Yong Lin, Joseph R. Bertino, Zhongtian Lin, Gulam M. Rather, Pengfei Xie
Publikováno v:
Scientific Reports, Vol 10, Iss 1, Pp 1-10 (2020)
Scientific Reports
Scientific Reports
The rapid qualitative assessment of surface markers on cancer cells can allow for point-of-care prediction of patient response to various cancer drugs. Preclinical studies targeting cells with an antibody to “activated” matriptase conjugated to a
Autor:
Joseph R. Bertino, Gulam M. Rather, Michael Anyanwu, Tamara Minko, Olga B. Garbuzenko, Zoltan Szekely
Publikováno v:
Cancers
Volume 13
Issue 5
Cancers, Vol 13, Iss 972, p 972 (2021)
Volume 13
Issue 5
Cancers, Vol 13, Iss 972, p 972 (2021)
Simple Summary The E2F family of transcription factors are essential for cell proliferation, differentiation, and DNA repair. They are commonly overexpressed or dysregulated in cancer as a consequence of inactivation or mutations in the retinoblastom
Publikováno v:
International Journal of Biological Macromolecules. 116:173-181
Polo-like kinase-1 (PLK-1) plays a key role in cell cycle progression during mitosis. Overexpression/dysfunction of PLK-1 is directly associated with cancerous transformation and has been reported in different cancer types. Here, we employed high thr
Autor:
Nitu Bansal, Tazeem Shaik, Debabrata Banerjee, John E. Kerrigan, Zoltan Szekely, Joseph R. Bertino, Kathleen W. Scotto, Tamara Minko, Gulam M. Rather, Olga B. Garbuzenko, Emine Ercikan Abali
Publikováno v:
Oncotarget
E2F1-3a overexpression due to amplification or to mutation or loss of the retinoblastoma gene, induces genes involved in DNA synthesis and leads to abnormal cellular proliferation, tumor growth, and invasion. Therefore, inhibiting the overexpression
Autor:
Gulam M. Rather, Philip M. Tedeschi, Zoltan Szekely, Joseph R. Bertino, Alvinsyah Adhityo Pramono
Publikováno v:
Pharmacology & Therapeutics. 226:107864
Cancer cells require increased levels of NADPH for increased nucleotide synthesis and for protection from ROS. Recent studies show that increased NADPH is generated in several ways. Activated AKT phosphorylates NAD kinase (NADK), increasing its activ
Autor:
Xuyang Lu, Suresh Venkatesh, Hooman Saeidi, Gulam M. Rather, Chen-Yong Lin, Hao Tang, Kaushik Sengupta, Mehdi Javanmard, Zhongtian Lin, Joseph R. Bertino
Publikováno v:
CICC
In this article, we present a 2D oscillator array-based magnetic sensor CMOS IC for flow cytometry. The CMOS IC packaged with a microfluidic channel eliminates the need for hydro-focusing by allowing uninhibited flow over the 2D chip surface. The chi
Publikováno v:
International Journal of Molecular Sciences
Volume 20
Issue 4
International Journal of Molecular Sciences, Vol 20, Iss 4, p 819 (2019)
Volume 20
Issue 4
International Journal of Molecular Sciences, Vol 20, Iss 4, p 819 (2019)
The bacteria expressing New Delhi Metallo-&beta
lactamase-1 (NDM-1) can hydrolyze all &beta
lactam antibiotics including carbapenems, causing multi-drug resistance. The worldwide emergence and dissemination of gene blaNDM-1 (produces NDM-1)
lactamase-1 (NDM-1) can hydrolyze all &beta
lactam antibiotics including carbapenems, causing multi-drug resistance. The worldwide emergence and dissemination of gene blaNDM-1 (produces NDM-1)
Publikováno v:
Cancer Research. 80:2212-2212
Matriptase, is a serine protease type II transmembrane protein. Matriptase forms a cognate pair with its Kunitz type endogenous inhibitor HAI-1 and is commonly deregulated and ubiquitously expressed in a variety of human carcinomas and in particular,