Zobrazeno 1 - 8
of 8
pro vyhledávání: '"Ibrahim Chehade"'
Autor:
L. Palanikumar, Laura Karpauskaite, Mohamed Al-Sayegh, Ibrahim Chehade, Maheen Alam, Sarah Hassan, Debabrata Maity, Liaqat Ali, Mona Kalmouni, Yamanappa Hunashal, Jemil Ahmed, Tatiana Houhou, Shake Karapetyan, Zackary Falls, Ram Samudrala, Renu Pasricha, Gennaro Esposito, Ahmed J. Afzal, Andrew D. Hamilton, Sunil Kumar, Mazin Magzoub
Publikováno v:
Nature Communications, Vol 12, Iss 1, Pp 1-24 (2021)
Amyloid aggregation of mutant p53 contributes to its loss of tumor suppressor function and oncogenic gain-of-function. Here, the authors use a protein mimetic to abrogate mutant p53 aggregation and rescue p53 function, which inhibits cancer cell prol
Externí odkaz:
https://doaj.org/article/aabfbc8d47544f739652c54bd2eb3f1f
Autor:
Laura Karpauskaite, Ahmed J. Afzal, Ibrahim Chehade, Jemil Ahmed, Renu Pasricha, Mazin Magzoub, Andrew D. Hamilton, Debabrata Maity, Mona Kalmouni, Loganathan Palanikumar, Sunil Kumar, Maheen Alam, Tatiana Houhou, Gennaro Esposito, Zackary Falls, Shake Karapetyan, Yamanappa Hunashal, Ram Samudrala, Mohamed Al-Sayegh, Liaqat Ali, Sarah Hassan
Publikováno v:
Nature Communications, Vol 12, Iss 1, Pp 1-24 (2021)
Nature Communications
Nature Communications
Missense mutations in p53 are severely deleterious and occur in over 50% of all human cancers. The majority of these mutations are located in the inherently unstable DNA-binding domain (DBD), many of which destabilize the domain further and expose it
Autor:
Mazin Magzoub, Sarah Hassan, Maheen Alam, Yamanappa Hunashal, Gennaro Esposito, Mohamed Al-Sayegh, Ibrahim Chehade, Liaqat Ali, Zackary Falls, Andrew D. Hamilton, Renu Pasricha, Sunil Kumar, Laura Karpauskaite, Ahmed J. Afzal, Mona Kalmouni, Jemil Ahmed, Ram Samudrala, Debabrata Maity, Loganathan Palanikumar, Shake Karapetyan
Missense mutations in p53 are severely deleterious and occur in over 50% of all human cancers. The vast majority of these mutations are located in the inherently unstable DNA-binding domain (DBD), many of which destabilize the domain further and expo
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::8fa961805711ad26790abd3b96f53b97
https://doi.org/10.1101/2020.08.10.243154
https://doi.org/10.1101/2020.08.10.243154
Autor:
Palanikumar Loganathan, Laura Karpauskaite, Mohamed Al-Sayegh, Ibrahim Chehade, Maheen Ali, Sarah Hassan, Debabrata Maity, Liaqat Ali, Mona Kalmouni, Tatiana Houhou, Gennaro Esposito, Ahmed J. Afzal, Andrew D. Hamilton, Sunil Kumar, Mazin Magzoub
Publikováno v:
Biophysical Journal. 121:300a
Autor:
Zhihua An, Lu Zhang, Wael M. Rabeh, Daniel Carelli, Jamie Whelan, Joseph Koussa, Joel Bernstein, Ibrahim Chehade, Adrienne Chang, Merima Sabanovic
Publikováno v:
Journal of Applied Crystallography. 51:1474-1480
The research-driven laboratory experiment described herein has at its core the individual development of students, combining core subject matter with the opportunity to explore, in a research environment, areas outside of traditional curricula; howev
Autor:
Marios S. Katsiotis, Ibrahim Chehade, Christy Maksoudian, Mazin Magzoub, Saeed M. Alhassan, Vineeth Mukundan, Maria C. Vogel
Publikováno v:
Archives of Biochemistry and Biophysics. 613:31-42
Prion diseases are associated with conversion of cellular prion protein (PrPC) into an abnormally folded and infectious scrapie isoform (PrPSc). We previously showed that peptides derived from the unprocessed N-termini of mouse and bovine prion prote
Autor:
Robert, Rutherford, Andrea, Lister, Thijs, Bosker, Tamzin, Blewett, Esteban, Gillio Meina, Ibrahim, Chehade, Thiviya, Kanagasabesan, Deborah, MacLatchy
Publikováno v:
General and comparative endocrinology. 289
The environmental estrogen 17α-ethinylestradiol (EE
Publikováno v:
Journal of the American Chemical Society. 139(47)
The conversion of the native random coil amyloid beta (Aβ) into amyloid fibers is thought to be a key event in the progression of Alzheimer's disease (AD). A significant body of evidence suggests that the highly dynamic Aβ oligomers are the main ca