Zobrazeno 1 - 10
of 38
pro vyhledávání: '"Atta Ahmad"'
Autor:
Mahvish Muzaffar, Atta Ahmad
Publikováno v:
PLoS ONE, Vol 6, Iss 11, p e27906 (2011)
The high propensity of insulin to fibrillate causes severe biomedical and biotechnological complications. Insulin fibrillation studies attain significant importance considering the prevalence of diabetes and the requirement of functional insulin in e
Externí odkaz:
https://doaj.org/article/5742083916e0407985895dc2fcf23ce5
Autor:
Abdelrahman, Foll-Alnada A. F., El-Sayed, Shafika A., Abuel-Atta, Ahmad A., Ghonimi, Wael A. M.
Publikováno v:
Open Veterinary Journal; 2023, Vol. 13 Issue 6, p723-731, 9p
Publikováno v:
Biophys J
Stress-induced unfolding and fibrillation of insulin represent serious medical and biotechnological problems. Despite many attempts to elucidate the molecular mechanisms of insulin fibrillation, there is no general agreement on how this process takes
Autor:
David F. Jahad, Cindy Putnam-Evans, Jean-Luc Scemama, Mary A. Farwell, Atta Ahmad, Hamzah Karimi
Publikováno v:
BIO-PROTOCOL. 9
Publikováno v:
Structural Concrete. Sep2016, Vol. 17 Issue 3, p408-424. 17p.
Autor:
Chiara Melis, Esperanza Arias, Victor Chatterjee, Kateryna Morozova, Jason E. Gestwicki, Erik R. P. Zuiderweg, Susmita Kaushik, Atta Ahmad, Brian Scharf, Ana Maria Cuervo, Jennifer N. Rauch, Barbara Stiller, Cristina C. Clement, Laura Santambrogio
Publikováno v:
The Journal of biological chemistry, vol 291, iss 35
hsc-70 (HSPA8) is a cytosolic molecular chaperone, which plays a central role in cellular proteostasis, including quality control during protein refolding and regulation of protein degradation. hsc-70 is pivotal to the process of macroautophagy, chap
Autor:
Atta Ahmad, Bryan M. Dunyak, Misol Ahn, Chad A. Dickey, Jennifer N. Rauch, Victoria A. Assimon, Umesh K. Jinwal, Erik R. P. Zuiderweg, Sharan R. Srinivasan, George A. Carlson, Zapporah T. Young, Xiaokai Li, Jason E. Gestwicki
Publikováno v:
Cell chemical biology, vol 23, iss 8
Heat shock protein 70 (Hsp70) is a chaperone that normally scans the proteome and initiates the turnover of some proteins (termed “clients”) by linking them to the degradation pathways. This activity is critical to normal protein homeostasis, yet
Autor:
Atta Ahmad, Bryce A. Nordhues, Jason E. Gestwicki, Isabelle R. Taylor, Erik R. P. Zuiderweg, Taia Wu, Anup Bhullar
Publikováno v:
The Journal of biological chemistry, vol 293, iss 27
Hsp70 chaperones bind to various protein substrates for folding, trafficking, and degradation. Considerable structural information is available about how prokaryotic Hsp70 (DnaK) binds substrates, but less is known about mammalian Hsp70s, of which th
Autor:
Duxin Sun, Atta Ahmad, Xiaokai Li, Adam M. Kabza, Jamie N. Connarn, Jason E. Gestwicki, Erik R. P. Zuiderweg, Zapporah T. Young, Sharan R. Srinivasan
Publikováno v:
ACS Medicinal Chemistry Letters. 4:1042-1047
The rhodacyanine, MKT-077, has antiproliferative activity against cancer cell lines through its ability to inhibit members of the heat shock protein 70 (Hsp70) family of molecular chaperones. However, MKT-077 is rapidly metabolized, which limits its
Autor:
Atta Ahmad, Mahvish Muzaffar
Publikováno v:
Journal of Molecular Pharmaceutics & Organic Process Research. 4
Cancer is a devastating disease that has affected millions of people, consumed tremendous efforts in the treatment/care and is incurable. Statistics from www.seer.cancer.gov show 14,140,254 people were living with cancer in 2013 in US with 1,685,210