Zobrazeno 1 - 10
of 15
pro vyhledávání: '"Mohammed, Fadlalla"'
Publikováno v:
Journal of Student Research.
Humans have taken the (scarecrow) as a protector for these crops from the birds. There are various different types and designs for the scarecrows around the world. In this project we will develop the traditional scarecrows to become electronic and do
Autor:
Rufida Salih, Mohammed Abdalla, Abdallah Mustafa, Mohammed Fadlalla, Lina Ahmed, Abbasher Hussien, Aziza Alrayah, Fatimaalzahra Abdelgadir, Anas Mohammed, Mawahib Mergani
Publikováno v:
Journal of the Neurological Sciences. 429:119201
Autor:
Alfadl, Abubakr Abdelraouf, Ali, Gamal Khalafalla Mohamed, Yousif, Mirghani A., Ahmed Babekir, Mohammed Fadlalla
Publikováno v:
In Pharmacy Practice in Developing Countries 2016:319-341
This chapter introduces the concept of adequate pharmaceutical service, ideally provided by pharmacists, as a vital component of the health care system in Sudan. The chapter starts with a comprehensive description of Sudan's health care system in gen
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::8d68d339da6f899d9fbd48499b52609a
https://doi.org/10.1016/b978-0-12-801714-2.00016-2
https://doi.org/10.1016/b978-0-12-801714-2.00016-2
Autor:
Patricia Acuna, Muhammad Adnan, Mohammed Fadlalla Ahmed Babekir, Kadir Alam, Qais Alefan, Abubakr Abdelraouf Alfadl, Mahmoud S. Al-Haddad, Ahmed Al-Jedai, Ahmad Almeman, Yaser Mohammed Ali Al-Worafi, Sybil Nana Ama Ossei-Agyeman-Yeboah, Tri Murti Andayani, Mukhtar Ansari, Ahmed Awaisu, Nathorn Chaiyakunapruk, Teerapon Dhippayom, Mahmoud Elmahdawy, Tarek Mohamed Elsayed, Gihan H. Elsisi, Yu Fang, Ahmed Ibrahim Fathelrahman, Abdulsalam Halboup, Mohamed Azmi Ahmad Hassali, Azhar Hussain, Inas Rifaat Ibrahim, Mohamed Izham Mohamed Ibrahim, Shazia Jamshed, Sirada M. Jones, Shahid Karim, Nadir Kheir, Nadeesha Lakmali, Shafiu Mohammed, Gamal Khalafalla Mohamed Ali, Dhakshila Niyangoda, Satibi Satibi, Ooi Guat See, Asrul Akmal Shafie, Nithima Sumpradit, Waleed M. Sweileh, Abdul Rasoul Wayyes, Albert I. Wertheimer, Rabiu Yakubu, Mirghani A. Yousif, Shukry Zawahir, Zhi Yen Wong, Sa’ed H. Zyoud
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::6981cb6a2c45452ac482a1965e3af7c9
https://doi.org/10.1016/b978-0-12-801714-2.01002-9
https://doi.org/10.1016/b978-0-12-801714-2.01002-9
Autor:
Kulwant S. Aulak, Mohammed Fadlalla, Arnab Ghosh, Mohammad Mahfuzul Haque, Dennis J. Stuehr, Deborah Durra
Publikováno v:
Journal of Biological Chemistry. 287:30105-30116
In nitric-oxide synthases (NOSs), two flexible hinges connect the FMN domain to the rest of the enzyme and may guide its interactions with partner domains for electron transfer and catalysis. We investigated the role of the FMN-FAD/NADPH hinge in rat
Autor:
Mohammed Fadlalla, David A. Greenberg, Cheuk Wun Li, Yaron Tomer, Eric M. Jacobson, Kenneth Ho, Mihaela Stefan, Amanda K. Huber, Luce Skrabanek, Erlinda Conception
Publikováno v:
Journal of Biological Chemistry. 286:31168-31179
Autoimmune thyroid diseases (AITD) arise from complex interactions between genetic, epigenetic, and environmental factors. Whole genome linkage scans and association studies have established thyroglobulin (TG) as a major AITD susceptibility gene. How
Autor:
Kulwant S. Aulak, Koustubh Panda, Jesús Tejero, Mohammad Mahfuzul Haque, Mohammed Fadlalla, Anthony T. Mustovich, Dennis J. Stuehr
Publikováno v:
Proceedings of the National Academy of Sciences. 104:9254-9259
In mammals, endothelial nitric oxide synthase (eNOS) has the weakest activity, being one-tenth and one-sixth as active as the inducible NOS (iNOS) and the neuronal NOS (nNOS), respectively. The basis for this weak activity is unclear. We hypothesized
Autor:
Mekki Bayachou, Zhi Qiang Wang, Dennis J. Stuehr, Mohammad Mahfuzul Haque, Jesús Tejero, Mohammed Fadlalla
NO synthase (NOS) enzymes convert L-arginine to NO in two sequential reactions whose rates (k(cat1) and k(cat2)) are both limited by the rate of ferric heme reduction (k(r)). An enzyme ferric heme-NO complex forms as an immediate product complex and
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8a20864ef1c1ca9666e28c7028eb3fdd
https://europepmc.org/articles/PMC3767175/
https://europepmc.org/articles/PMC3767175/
Publikováno v:
The Biochemical journal. 450(3)
The NOS (nitric oxide synthase; EC 1.14.13.39) enzymes contain a C-terminal flavoprotein domain [NOSred (reductase domain of NOS)] that binds FAD and FMN, and an N-terminal oxygenase domain that binds haem. Evidence suggests that the FMN-binding doma