Political Islam has been at the forefront of political discussions in and of the Middle East and has often been associated with violence and 'terrorism'. Much has been written on political Islam, but there has been little work on how Arab audiences respond to and view political Islam and the groups seen to be acting under this generic framework, including al-Qa'eda. In the absence of serious audience research that would give us a better idea about attitudes, this article examines how Arab popular culture frames active Islamist groups; in particular we focus on Egyptian films that help shape Arab audiences' perspectives of political Islam. The article analyzes how political Islam is discussed in these films and by film producers, directors and media owners, and how Islamist groups are often framed as the 'other'.

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This study seeks to find answers pertaining to the unique lexical choices in describing Heavens /Gardens "Al-Jinan" in the Quranic Surah "Al – Rahman". In this Surah, a detailed, descriptive representation of four Heavens is employed via a distinguished lexicon that appears very similar for the four Heavens in general, but very different when it comes to details of the structural context of the two heavens depicted first and represented of lower rank, in comparison with the second two. The research adopted two parameters of analysis in an attempt to explaining the lexical selection of language that describes Heavens in Al – Rahman. First, the internal structure of the Surah; second, the extra-linguistic and cultural context of the Arabs in the time span of the Quranic Surah. تسعى الدراسة للإجابة عن سؤال المعجم الخاص بوصف الجنان الوارد ذكرها في سورة الرحمن، فقد عرض الله سبحانه وتعالى تفصيلاً تمثيلياً لجنان أربعة في سورة الرحمن؛ جنتين أخبرنا عن صفاتهما أولا، وجنتين أخريين أخبرنا عن صفاتهما ثانيا- مع تأكيد من قبله عزّ وجلّ على أنّهما أقل مرتبةً ومكانةً- ووضح الله سبحانه هذه الصورة التمثيلية من خلال معجم خاص، جاء متشابها في صورته العامة ومختلفاً في صورته التفصيلية بين الجنتين في السياق التركيبي الأول والجنتين في السياق التركيبي الثاني. وستتخذ الدراسة من المرجعيْن: البنيوي الداخلي؛ الذي يقرأ الاختيار المعجمي من خلال بنية السورة الداخلية، والثقافي الخارجي الذي يقرأ الاختيار المعجمي من خلال ثقافة العرب زمن التلقي الأول للنص القرآني، مرجعيها الرئيسين في التفسير.

The Fanconi anemia (FA) pathway is a major player in the control of DNA replication integrity in response to replication stress. Germline defect in the pathway results in the FA syndrome characterized by developmental abnormalities, bone marrow (BM) failure, and genome instability which greatly elevates the incidence of cancers. A pivotal step in the activation of the FA DNA repair pathway is the monoubiquitination of the FANCD2 and FANCI proteins (ID2) by the FA core complex, a unique ubiquitin ligase complex which includes eight proteins (FANCA-FANCG, FANCL, and FAAP100) and UBE2T/FANCT. This monoubiquitination event enables the recruitment of the ID2 complex to chromatin and nuclear foci at sites of DNA damage. Cells with mutations in any of the FA core complex proteins lack the ability to monoubiquitinated ID2, making ID2 ubiquitination a convergence point in the pathway, with an estimation of>90% FA patients defective in this step. Additionally, somatic mutations In FA genes render tumor cells sensitive to DNA crosslinking agents, so identification of FA pathway defects provides an opportunity for therapeutic targeting. In search for additional potential target/substrate of this unique FA core ubiquitin ligase complex, we performed a high throughput genome-wide ubiquitin-specific proteomics (UbiScan) screen and found, in addition to the ID2 complex, many ubiquitinated proteins are dysregulated (mostly downregulated) in FA deficient cells compared with that of FA proficient cells. We used a Ubiquitin Remnant Motif (K- ∑-GG) Antibody Bead Conjugate (Cell Signaling Technology), a proprietary ubiquitin branch ("K- ∑-GG") antibody with specificity for a di-glycine tag that is the remnant of ubiquitin left on protein substrates after trypsin digestion, to enrich ubiquitinated peptides from trypsin digested cell samples (shNT vs shFANCA). This enrichment is followed by LC-MS/MS analysis for quantitative profiles of hundreds to over a thousand nonredundant ubiquitinated sequences. We were successful in demonstrating that under steady-state conditions (without proteasome inhibitor treatment), the ubiquitinated forms of both FANCD2 and FANCI proteins are much higher in control (shNT) HeLa cells compared with that of the cells depleted of FANCA (shFANCA). We then collaborated with the Cell signaling technology to perform a high throughput UbiScan® analysis of total ubiquitinated proteins both in total nuclei and chromatin fractions under replicative stress conditions. UbiScan® enables researchers to isolate, identify and quantitate large numbers of ubiquitin-modified cellular peptides with a high degree of specificity and sensitivity, providing a global overview of the ubiquitination sites in cellular proteins in cell and tissue samples without preconceived biases about where these modified sites occur. A total of 16,249 redundant modified peptide assignments to 7,856 modified sites for the Ubiquitin K-GG Remnant Motif Antibody were obtained. As expected, the amount of monoubiquitinated FANCD2 (at K651) and FANCI (at K523) were highly reduced in both the nuclear and chromatin fractions of Hela cells depleted of FANCA (shA). Consistent with the earlier findings, the amount of ubiquitinated ID2 proteins were extremely low in the chromatin fraction of the Hela cells depleted of FANCA. Since there are numerous ubiquitinated proteins found to be dysregulated in our UbiScan analyses, we used the following criteria to select the target proteins based on; a) -fold changes, and b) proteins that are known to participate in the DNA repair signaling pathways. We validated our UbiScan results by using an assay system to detect endogenous protein ubiquitination. We also found a significant reduction in the ubiquitination of several DNA repair-related proteins (found in our UbiScan analysis) in FANCA deficient cells. To assess FA pathway functions, we generated HAP1 and appropriate cells knock out of these select ubiquitinated target proteins by using CRISPR-Cas9 system. Then, the KO cells were examined for FA pathway functions. These results will be discussed. In conclusion, our findings reveal that the FA core ubiquitin ligase complex regulates (directly or indirectly) the ubiquitinated levels of many novel proteins outside of the ID2 complex, and these novel target proteins may provide important additional mechanistic insights into the FA DNA repair pathway. Disclosures No relevant conflicts of interest to declare.