King Saud University

About: King Saud University is a education organization based out in Riyadh, Saudi Arabia. It is known for research contribution in the topics: Population & Adsorption. The organization has 22106 authors who have published 57908 publications receiving 1042234 citations. The organization is also known as: Riyadh University.

Localization Techniques in Wireless Sensor Networks

Abstract: The important function of a sensor network is to collect and forward data to destination. It is very important to know about the location of collected data. This kind of information can be obtained using localization technique in wireless sensor networks (WSNs). Localization is a way to determine the location of sensor nodes. Localization of sensor nodes is an interesting research area, and many works have been done so far. It is highly desirable to design low-cost, scalable, and efficient localization mechanisms for WSNs. In this paper, we discuss sensor node architecture and its applications, different localization techniques, and few possible future research directions.

Interactions of anticancer Pt compounds with proteins: an overlooked topic in medicinal inorganic chemistry?

Abstract: A critical discussion is presented about the possible role of Pt–protein interactions in the mechanisms of action of platinum anticancer compounds. Although, since 40 years from its discovery, cisplatin and analogues are believed to exert their therapeutic effects via direct interactions with nucleic acids, several proteins/enzymes have recently appeared to be involved in the compounds' overall pharmacological and toxicological profiles, apart from classical serum transport proteins and metal detoxification systems. As an example, the emerging role of zinc finger proteins is noteworthy in the activity of platinum drugs. Moreover, the pursuit of novel platinum candidates that selectively target enzymes is now the subject of intense investigation in medicinal bioinorganic chemistry and chemical biology. An overview is presented of the most representative studies in the field, with particular focus on the characterization of the Pt–protein interactions at a molecular level, using different biophysical and analytical methods.

Advances in Oral Drug Delivery.

Abstract: The oral route is the most common route for drug administration. It is the most preferred route, due to its advantages, such as non-invasiveness, patient compliance and convenience of drug administration. Various factors govern oral drug absorption including drug solubility, mucosal permeability, and stability in the gastrointestinal tract environment. Attempts to overcome these factors have focused on understanding the physicochemical, biochemical, metabolic and biological barriers which limit the overall drug bioavailability. Different pharmaceutical technologies and drug delivery systems including nanocarriers, micelles, cyclodextrins and lipid-based carriers have been explored to enhance oral drug absorption. To this end, this review will discuss the physiological, and pharmaceutical barriers influencing drug bioavailability for the oral route of administration, as well as the conventional and novel drug delivery strategies. The challenges and development aspects of pediatric formulations will also be addressed.

Site- and kinase-specific phosphorylation-mediated activation of SLAC1, a guard cell anion channel stimulated by abscisic acid.

Abstract: Under drought stress, abscisic acid (ABA) triggers closure of leaf cell pores called stomata, which are formed by two specialized cells called guard cells in plant epidermis. Two pathways downstream of ABA stimulate phosphorylation of the S-type anion channels SLAC1 (slow anion channel associated 1) and SLAH3 (SLAC1 homolog 3), which causes these channels to open, reducing guard cell volume and triggering stomatal closure. One branch involves OST1 (open stomata 1), a calcium-independent SnRK2-type kinase, and the other branch involves calcium-dependent protein kinases of the CPK (calcium-dependent protein kinase) family. We used coexpression analyses in Xenopus oocytes to show that the calcineurin B-like (CBL) calcium sensors CBL1 and CBL9 and their interacting protein kinase CIPK23 also triggered SLAC1 and SLAH3 opening. We analyzed whether regulation of SLAC1 opening by these different families of kinases involved the same or different sites on SLAC1 by measuring channel conductance of SLAC1 with mutations in the putative phosphorylation sites in the amino or carboxyl termini coexpressed with specific kinases in Xenopus oocytes. SLAC1 mutants lacking the OST1-phosphorylated site were still activated by CPK or by CBL/CIPK complexes. Phosphorylation and activation of SLAC1 by any of the kinases were inhibited by the phosphatase ABI1 (ABA insensitive 1), which is inactivated in response to ABA signaling. These findings identified CBL/CIPK complexes as potential regulators of stomatal aperture through S-type anion channels and indicated that phosphorylation at distinct sites enables SLAC1 activation by both calcium-dependent and calcium-independent pathways downstream of ABA.