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2. Casemix, management, and mortality of patients receiving emergency neurosurgery for traumatic brain injury in the Global Neurotrauma Outcomes Study: a prospective observational cohort study

Author

Abbas, Ghayur, Abdallah, Omar Ibrahim, Abdel-Lateef, Ahmed, Abdifatah, Khalif, Abdullateef, Awfa, Abeygunaratne, Ruvini, Aboellil, Mostafa, Adam, Abass, Adams, Robert, Adeleye, Amos, Adeolu, Augustine, Adji, Novan Krisno, Afianti, Nur, Agarwal, Sudarsan, Aghadi, Ifeanyi Kene, Aguilar, Paúl Martín Méndez, Ahmad, Syeda Rida, Ahmed, Daniyal, Ahmed, Nafees, Aizaz, Haider, Aji, Yunus Kuntawi, Alamri, Alex, Alberto, Augusto Jacinto Mussindo, Alcocer, Luis Alcocer, Alfaro, Lesly Gonzales, Al-Habib, Amro, Alhourani, Ahmad, Ali, Syed Muhammad Rafay, Alkherayf, Fahad, AlMenabbawy, Ahmed, Alshareef, Aliyah, Aminullah, Muhammad Adil s/o, Amjad, Madeha, Amorim, Robson Luis Oliveira de, Anbazhagan, Sathiaprabhu, Andrade, Almir, Antar, Waleed, Anyomih, Theophilus T.K., Aoun, Salah, Apriawan, Tedy, Armocida, Daniele, Arnold, Paul, Arraez, Miguel, Assefa, Temesgen, Asser, Andres, Athiththan, S.P., Attanayake, Deepal, Aung, Maung Maung, Avi, Allan, Ayala, Victor Enrique Antolinez, Azab, Mohammed, Azam, Gaousul, Azharuddin, Mohd, Badejo, Olukemi, Badran, Mohamed, Baig, Azam Ali, Baig, Rehman Ali, Bajaj, Ankur, Baker, Paul, Bala, Renu, Balasa, Artur, Balchin, Ross, Balogun, James, Ban, Vin Shen, Bandi, Bharath Kumar Reddy, Bandyopadhyay, Soham, Bank, Matthew, Barthelemy, Ernest, Bashir, Mohammed Talha, Basso, Luciano Silveira, Basu, Surajit, Batista, Auricelio, Bauer, Marlies, Bavishi, Devi, Beane, Abi, Bejell, Shmuel, Belachew, Anteneh, Belli, Antonio, Belouaer, Amani, Bendahane, Najia El Abbadi, Benjamin, Okanga, Benslimane, Youssef, Benyaiche, Chaymae, Bernucci, Claudio, Berra, Luigi Valentino, Bhebe, Arnold, Bimpis, Alexios, Blanaru, Diana, Bonfim, Jean Claude, Borba, Luis A B, Borcek, Alp Ozgun, Borotto, Erika, Bouhuwaish, Ahmad Elmabri Mohammad, Bourilhon, Facundo, Brachini, Gioia, Breedon, Joshua, Broger, Maximilian, Brunetto, Giacoma Maria Floriana, Bruzzaniti, Placido, Budohoska, Natalia, Burhan, Hira, Calatroni, Maximiliano Luis, Camargo, Catherine, Cappai, Pier Francesco, Cardali, Salvatore Massimiliano, Castaño-Leon, Ana M, Cederberg, David, Celaya, Mikel, Cenzato, Marco, Challa, Lakshmi Madhavi, Charest, Dhanny, Chaurasia, Bipin, Chenna, Rabah, Cherian, Iype, Ching'o, Juliana Henry, Chotai, Tejas, Choudhary, Ajay, Choudhary, Nabeel, Choumin, Florence, Cigic, Tomislav, Ciro, Juan, Conti, Carlo, Corrêa, Antônio Carlos de Souza, Cossu, Giulia, Couto, Maíra Piani, Cruz, Aurora, D'Silva, Divya, D'Aliberti, Giuseppe Antonio, Dampha, Lamin, Daniel, Roy Thomas, Dapaah, Andrew, Darbar, Aneela, Dascalu, Gabriel, Dauda, Happy Amos, Davies, Owain, Delgado-Babiano, Andrea, Dengl, Markus, Despotovic, Marko, Devi, Indira, Dias, Celeste, Dirar, Mohamed, Dissanayake, Melina, Djimbaye, Hananiah, Dockrell, Simon, Dolachee, Ali, Dolgopolova, Julija, Dolgun, Muge, Dow, Abdalrouf, Drusiani, Davide, Dugan, Artjom, Duong, Dinh Tuan, Duong, Trung Kien, Dziedzic, Tomasz, Ebrahim, Ali, El Fatemi, Nizar, El Helou, Antonios El, El Maaqili, Rachid El, El Mostarchid, Brahim El, El Ouahabi, Abdessamad El, Elbaroody, Mohammad, El-Fiki, Ahmed, El-Garci, Ahmed, El-Ghandour, Nasser M.F., Elhadi, Muhammed, Elleder, Vanessa, Elrais, Safa, El-shazly, Mohamed, Elshenawy, Mohamed, Elshitany, Hesham, El-Sobky, Omar, Emhamed, Marwa, Enicker, Basil, Erdogan, Onur, Ertl, Sebastian, Esene, Ignatius, Espinosa, Omar Ocampo, Fadalla, Tarig, Fadelalla, Mohammed, Faleiro, Rodrigo Moreira, Fatima, Nida, Fawaz, Charbel, Fentaw, Assefa, Fernandez, Carla Eiriz, Ferreira, Ana, Ferri, Francesco, Figaji, Tony, Filho, Emerson L B, Fin, Loic, Fisher, Benjamin, Fitra, Fitra, Flores, Alexis Palpan, Florian, Ioan Stefan, Fontana, Vincenzo, Ford, Lauren, Fountain, Daniel, Frade, Jose Maria Roda, Fratto, Antonio, Freyschlag, Christian, Gabin, Aranzazu Sánchez, Gallagher, Clare, Ganau, Mario, Gandia-Gonzalez, Maria Luisa, Garcia, Andoni, Garcia, Borja Hernandez, Garusinghe, Sanjeewa, Gebreegziabher, Biniam, Gelb, Adrian, George, Jerome St, Germanò, Antonino Francesco, Ghetti, Ilaria, Ghimire, Prajwal, Giammarusti, Alessandro, Gil, Jose Luis, Gkolia, Panagiota, Godebo, Yoseph, Gollapudi, Prakash Rao, Golubovic, Jagos, Gomes, Jeremias Fernando, Gonzales, Javier, Gormley, William, Gots, Alexander, Gribaudi, Giulia Letizia, Griswold, Dylan, Gritti, Paolo, Grobler, Ruan, Gunawan, Rudy, Hailemichael, Birhanu, Hakkou, Elmehdi, Haley, Mark, Hamdan, Alhafidz, Hammed, Ali, Hamouda, Waeel, Hamzah, Nurul Ashikin, Han, Nyein Latt, Hanalioglu, Sahin, Haniffa, Rashan, Hanko, Martin, Hanrahan, John, Hardcastle, Timothy, Hassani, Fahd Derkaoui, Heidecke, Volkmar, Helseth, Eirik, Hernández-Hernández, Miguel Ángel, Hickman, Zachary, Hoang, Le Minh Chau, Hollinger, Alexa, Horakova, Lenka, Hossain-Ibrahim, Kismet, Hou, Boru, Hoz, Samer, Hsu, Janine, Hunn, Martin, Hussain, Madiha, Iacopino, Giorgia, Ideta, Mylena Miki Lopes, Iglesias, Irene, Ilunga, Ali, Imtiaz, Nafiz, Islam, Rafiza, Ivashchenko, Serge, Izirouel, Karim, Jabal, Mohamed Sobhi, Jabal, Soubhi, Jabang, John Nute, Jamjoom, Aimun, Jan, Irfan, Jarju, Landing BM, Javed, Saad, Jelaca, Bojan, Jhawar, Sukhdeep Singh, Jiang, Ting Ting, Jimenez, Fernando, Jiris, Jorge, Jithoo, Ron, Johnson, Walt, Joseph, Mathew, Joshi, Rameshman, Junttila, Eija, Jusabani, Mubashir, Kache, Stephen Akau, Kadali, Satyavara Prasad, Kalkmann, Gabriela F, Kamboh, Usman, Kandel, Hitham, Karakus, Ahmet Kamil, Kassa, Mengistu, Katila, Ari, Kato, Yoko, Keba, Martin, Kehoe, Kristy, Kertmen, Huseyin Hayri, Khafaji, Soha, Khajanchi, Monty, Khan, Mohammed, Khan, Muhammad Mukhtar, Khan, Sohail Daud, Khizar, Ahtesham, Khriesh, Amir, Kierońska, Sara, Kisanga, Paul, Kivevele, Boniface, Koczyk, Kacper, Koerling, Anna-Lucia, Koffenberger, Danielle, Kõiv, Kennet, Kõiv, Leho, Kolarovszki, Branislav, König, Marton, Könü-Leblebicioglu, Dilek, Koppala, Santhoshi Devi, Korhonen, Tommi, Kostkiewicz, Boguslaw, Kostyra, Kacper, Kotakadira, Srinivas, Kotha, Arjun Reddy, Kottakki, Madhu Narayana Rao, Krajcinovic, Nenad, Krakowiak, Michal, Kramer, Andreas, Krishnamoorthy, Selvamuthukumaran, Kumar, Ashok, Kumar, Pankaj, Kumar, Pradhumna, Kumarasinghe, Nilaksha, Kuncha, Gowtham, Kutty, Raja K., Laeke, Tsegazeab, Lafta, Ghazwan, Lammy, Simon, Lapolla, Pierfrancesco, Lardani, Jacopo, Lasica, Nebojsa, Lastrucci, Giancarlo, Launey, Yoann, Lavalle, Laura, Lawrence, Tim, Lazaro, Albert, Lebed, Vitalii, Leinonen, Ville, Lemeri, Lawrence, Levi, Leon, Lim, Jia Yi, Lim, Xiao Yi, Linares-Torres, Jorge, Lippa, Laura, Lisboa, Lurdes, Liu, Jinfang, Liu, Ziyuan, Lo, William B, Lodin, Jan, Loi, Federico, Londono, Daniella, Lopez, Pedro Antonio Gomez, López, Cristina Barceló, Lotbiniere-Bassett, Madeleine De, Lulens, Rihards, Luna, Facundo Hector, Luoto, Teemu, M.V., Vijaya Sekhar, Mabovula, Ndyebo, MacAllister, Matthew, Macie, Alcina Americo, Maduri, Rodolfo, Mahfoud, Moufid, Mahmood, Ashraf, Mahmoud, Fathia, Mahoney, Dominic, Makhlouf, Wissam, Malcolm, George, Malomo, Adefolarin, Malomo, Toluyemi, Mani, Manoranjitha Kumari, Marçal, Tomás Gazzinelli, Marchello, Jacopo, Marchesini, Nicolò, Marhold, Franz, Marklund, Niklas, Martín-Láez, Rubén, Mathaneswaran, Vickneswaran, Mato-Mañas, David José, Maye, Helen, McLean, Aaron Lawson, McMahon, Catherine, Mediratta, Saniya, Mehboob, Mehreen, Meneses, Alisson, Mentri, Nesrine, Mersha, Hagos, Mesa, Ana Milena, Meyer, Cristy, Millward, Christopher, Mimbir, Salomao Amone, Mingoli, Andrea, Mishra, Parashruram, Mishra, Tejesh, Misra, Basant, Mittal, Siddharth, Mohammed, Imran, Moldovan, Ioana, Molefe, Masechaba, Moles, Alexis, Moodley, Preston, Morales, Mario Augusto Narváez, Morgan, Lucy, Morillo, German Del Castillo, Moustafa, Wahab, Moustakis, Nikolaos, Mrichi, Salma, Munjal, Satya Shiva, Muntaka, Abdul-Jalilu Mohammed, Naicker, Denver, Nakashima, Paulo E H, Nandigama, Pratap Kumar, Nash, Samantha, Negoi, Ionut, Negoita, Valetina, Neupane, Samundra, Nguyen, Manh Hung, Niantiarno, Fajar Herbowo, Noble, Abbi, Nor, Mohd Arman Muhamad, Nowak, Blazej, Oancea, Andrei, O'Brien, Frazer, Okere, Oghenekevwe, Olaya, Sandra, Oliveira, Leandro, Oliveira, Louise Makarem, Omar, Fatma, Ononeme, Okezi, Opšenák, René, Orlandini, Simone, Osama, Alrobah, Osei-Poku, Dorcas, Osman, Haytham, Otero, Alvaro, Ottenhausen, Malte, Otzri, Shuli, Outani, Oumaima, Owusu, Emmanuel Abem, Owusu-Agyemang, Kevin, Ozair, Ahmad, Ozoner, Baris, Paal, Elli, Paiva, Mauro Sérgio, Paiva, Wellingson, Pandey, Sharad, Pansini, Gastone, Pansini, Luigi, Pantel, Tobias, Pantelas, Nikolaos, Papadopoulos, Konstantinos, Papic, Vladimir, Park, Kee, Park, Nick, Paschoal, Eric Homero Albuquerque, Paschoalino, Mylla Christie de Oliveira, Pathi, Rajesh, Peethambaran, Anilkumar, Pereira, Thiago Andrade, Perez, Irene Panero, Pérez, Claudio José Piqueras, Periyasamy, Tamilanandh, Peron, Stefano, Phillips, Michael, Picazo, Sofía Sotos, Pinar, Ertugrul, Pinggera, Daniel, Piper, Rory, Pirakash, Pathmanesan, Popadic, Branko, Posti, Jussi P., Prabhakar, Rajmohan Bhanu, Pradeepan, Sivanesalingam, Prasad, Manjunath, Prieto, Paola Calvachi, Prince, Ron, Prontera, Andrea, Provaznikova, Eva, Quadros, Danilo, Quintero, Nezly Jadid Romero, Qureshi, Mahmood, Rabiel, Happiness, Rada, Gabriel, Ragavan, Sivagnanam, Rahman, Jueria, Ramadhan, Omar, Ramaswamy, Padma, Rashid, Sakina, Rathugamage, Jagath, Rätsep, Tõnu, Rauhala, Minna, Raza, Asif, Reddycherla, Naga Raju, Reen, Linus, Refaat, Mohamed, Regli, Luca, Ren, Haijun, Ria, Antonio, Ribeiro, Thales Francisco, Ricci, Alessandro, Richterová, Romana, Ringel, Florian, Robertson, Faith, Rocha, Catarina Mayrink Siqueira Cabral, Rogério, Juvenal de Souza, Romano, Adan Anibal, Rothemeyer, Sally, Rousseau, Gail Rousseau Gail, Roza, Ranette, Rueda, Kevin David Farelo, Ruiz, Raiza, Rundgren, Malin, Rzeplinski, Radoslaw, S.Chandran, Raj, Sadayandi, Ramesh Andi, Sage, William, Sagerer, André Norbert Josef, Sakar, Mustafa, Salami, Mohcine, Sale, Danjuma, Saleh, Youssuf, Sánchez-Viguera, Cristina, Sandila, Saning'o, Sanli, Ahmet Metin, Santi, Laura, Santoro, Antonio, Santos, Aieska Kellen Dantas Dos, Santos, Samir Cezimbra dos, Sanz, Borja, Sapkota, Shabal, Sasidharan, Gopalakrishnan, Sasillo, Ibrahim, Satoskar, Rajeev, Sayar, Ali Caner, Sayee, Vignesh, Scheichel, Florian, Schiavo, Felipe Lourenzon, Schupper, Alexander, Schwarz, Andreas, Scott, Teresa, Seeberger, Esther, Segundo, Claudionor Nogueira Costa, Seidu, Anwar Sadat, Selfa, Antonio, Selmi, Nazan Has, Selvarajah, Claudiya, Şengel, Necmiye, Seule, Martin, Severo, Luiz, Shah, Purva, Shahzad, Muhammad, Shangase, Thobekile, Sharma, Mayur, Shiban, Ehab, Shimber, Emnet, Shokunbi, Temitayo, Siddiqui, Kaynat, Sieg, Emily, Siegemund, Martin, Sikder, Shahidur Rahman, Silva, Ana Cristina Veiga, Silva, Ana, Silva, Pedro Alberto, Singh, Deepinder, Skadden, Carly, Skola, Josef, Skouteli, Eirini, Słoniewski, Pawel, Smith, Brandon, Solanki, Guirish, Solla, Davi Fontoura, Solla, Davi, Sonmez, Ozcan, Sönmez, Müge, Soon, Wai Cheong, Stefini, Roberto, Stienen, Martin Nikolaus, Stoica, Bogdan, Stovell, Matthew, Suarez, Maria Natalia, Sulaiman, Alaa, Suliman, Mazin, Sulistyanto, Adi, Sulubulut, Şeniz, Sungailaite, Sandra, Surbeck, Madlen, Szmuda, Tomasz, Taddei, Graziano, Tadele, Abraham, Taher, Ahmed Saleh Ahmed, Takala, Riikka, Talari, Krishna Murthy, Tan, Bih Huei, Tariciotti, Leonardo, Tarmohamed, Murad, Taroua, Oumayma, Tatti, Emiliano, Tenovuo, Olli, Tetri, Sami, Thakkar, Poojan, Thango, Nqobile, Thatikonda, Satish Kumar, Thesleff, Tuomo, Thomé, Claudius, Thornton, Owen, Timmons, Shelly, Timoteo, Eva Ercilio, Tingate, Campbell, Tliba, Souhil, Tolias, Christos, Toman, Emma, Torres, Ivan, Torres, Luis, Touissi, Youness, Touray, Musa, Tropeano, Maria Pia, Tsermoulas, Georgios, Tsitsipanis, Christos, Turkoglu, Mehmet Erhan, Uçkun, Özhan Merzuk, Ullman, Jamie, Ungureanu, Gheorghe, Urasa, Sarah, Ur-Rehman, Obaid, Uysal, Muhammed, Vakis, Antonios, Valeinis, Egils, Valluru, Vaishali, Vannoy, Debby, Vargas, Pablo, Varotsis, Phillipos, Varshney, Rahul, Vats, Atul, Veljanoski, Damjan, Venturini, Sara, Verma, Abhijit, Villa, Clara, Villa, Genaro, Villar, Sofia, Villard, Erin, Viruez, Antonio, Voglis, Stefanos, Vulekovic, Petar, Wadanamby, Saman, Wagner, Katherine, Walshe, Rebecca, Walter, Jan, Waseem, Marriam, Whitworth, Tony, Wijeyekoon, Ruwani, Williams, Adam, Wilson, Mark, Win, Sein, Winarso, Achmad Wahib Wahju, Ximenes, Abraão Wagner Pessoa, Yadav, Anurag, Yadav, Dipak, Yakoub, Kamal Makram, Yalcinkaya, Ali, Yan, Guizhong, Yaqoob, Eesha, Yepes, Carlos, Yılmaz, Ayfer Nazmiye, Yishak, Betelehem, Yousuf, Farhat Basheer, Zahari, Muhammad Zamzuri, Zakaria, Hussein, Zambonin, Diego, Zavatto, Luca, Zebian, Bassel, Zeitlberger, Anna Maria, Zhang, Furong, Zheng, Fengwei, Ziga, Michal, Clark, David, Joannides, Alexis, Adeleye, Amos Olufemi, Bajamal, Abdul Hafid, Bashford, Tom, Biluts, Hagos, Budohoski, Karol, Ercole, Ari, Fernández-Méndez, Rocío, Figaji, Anthony, Gupta, Deepak Kumar, Härtl, Roger, Iaccarino, Corrado, Khan, Tariq, Rubiano, Andrés, Shabani, Hamisi K, Sichizya, Kachinga, Tewari, Manoj, Tirsit, Abenezer, Thu, Myat, Tripathi, Manjul, Trivedi, Rikin, Devi, Bhagavatula Indira, Servadei, Franco, Menon, David, Kolias, Angelos, and Hutchinson, Peter

Published
2022
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6. Cryo-EM shows how dynactin recruits two dyneins for faster movement

Author

Urnavicius, Linas, Lau, Clinton K., Elshenawy, Mohamed M., Morales-Rios, Edgar, Motz, Carina, Yildiz, Ahmet, and Carter, Andrew P.

Subjects
Dynein -- Physiological aspects, Environmental issues, Science and technology, Zoology and wildlife conservation
Abstract

Dynein and its cofactor dynactin form a highly processive microtubule motor in the presence of an activating adaptor, such as BICD2. Different adaptors link dynein and dynactin to distinct cargoes. Here we use electron microscopy and single-molecule studies to show that adaptors can recruit a second dynein to dynactin. Whereas BICD2 is biased towards recruiting a single dynein, the adaptors BICDR1 and HOOK3 predominantly recruit two dyneins. We find that the shift towards a double dynein complex increases both the force and speed of the microtubule motor. Our 3.5 resolution cryo-electron microscopy reconstruction of a dynein taildynactinBICDR1 complex reveals how dynactin can act as a scaffold to coordinate two dyneins side-by-side. Our work provides a structural basis for understanding how diverse adaptors recruit different numbers of dyneins and regulate the motile properties of the dyneindynactin transport machine., Author(s): Linas Urnavicius [1]; Clinton K. Lau [1]; Mohamed M. Elshenawy [2]; Edgar Morales-Rios [3]; Carina Motz [1]; Ahmet Yildiz [2, 4]; Andrew P. Carter (corresponding author) [1] Cytoplasmic dynein-1 [...]

Published
2018
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7. Replisome speed determines the efficiency of the Tus--Ter replication termination barrier

Author

Elshenawy, Mohamed M., Jergic, Slobodan, Xu, Zhi-Qiang, Sobhy, Mohamed A., Takahashi, Masateru, Oakley, Aaron J., Dixon, Nicholas E., and Hamdan, Samir M.

Subjects
DNA synthesis -- Analysis, Chromosome replication -- Analysis, Environmental issues, Science and technology, Zoology and wildlife conservation
Abstract

In all domains of life, DNA synthesis occurs bidirectionally from replication origins. Despite variable rates of replication fork progression, fork convergence often occurs at specific sites (1). Escherichia coli sets a 'replication fork trap' that allows the first arriving fork to enter but not to leave the terminus region (2-5). The trap is set by oppositely oriented Tus-bound Ter sites that block forks on approach from only one direction (3-7). However, the efficiency of fork blockage by Tus-Ter does not exceed 50% in vivo despite its apparent ability to almost permanently arrest replication forks in vitro (8, 9). Here we use data from single-molecule DNA replication assays and structural studies to show that both polarity and fork-arrest efficiency are determined by a competition between rates of Tus displacement and rearrangement of Tus-Ter interactions that leads to blockage of slower moving replisomes by two distinct mechanisms. To our knowledge this is the first example where intrinsic differences in rates of individual replisomes have different biological outcomes., In the circular E. coli chromosome, two replication forks move from the replication origin to converge opposite in a region that contains ten 23-base-pair Ter (termination) sites and the dif [...]

Published
2015

10. Sofosbuvir‐containing regimens are safe and effective in the treatment of HCV patients with moderate to severe renal impairment.

Author

Eletreby, Rasha, El‐Serafy, Magdy, Anees, Mahmoud, Kasem, Gamal, Salama, Marwa, Elkhouly, Reham, Hamdy, Mostafa, Abdel Haleem, Hisham, Kamal, Ehab, Abdel‐Razek, Wael, Salama, Rabab, Elshenawy, Mohamed, Shafeek, Ayman, Hassany, Mohamed, El‐Sayed, Manal H., El‐Shazly, Yehia, and Esmat, Gamal

Subjects
CHRONIC hepatitis C, HEPATITIS C virus, VIRAL hepatitis, CHRONIC kidney failure, FAILURE analysis
Abstract

Background and Aims: This study aimed to assess the safety and efficacy of sofosbuvir (SOF)‐based regimens in patients with moderate to severe renal impairment; a subject which has been questioned by many investigators with conflicting results. Methods: This is a real‐life multicentre retrospective cohort study on 4944 chronic Hepatitis C virus (HCV) patients with chronic kidney disease (CKD) (eGFR <60 mL/min/1.73 m2) who received SOF‐based therapy in specialized treatment centres affiliated to the National Committee for the Control of Viral Hepatitis in Egypt. The efficacy and safety of SOF‐based regimens was assessed. Results: Week 12 virological response rates were 97.5%, 96.7%, 85.7% and 80% in the total cohort, patients with eGFR <30 mL/min/1.73 m2, patients with associated hepatic decompensation and patients on dialysis respectively. Various treatment regimens did not statistically affect the response rates. Treatment experience, cirrhosis and diabetes were predictors of treatment failure on multivariate analysis. Serious adverse events occurred in 0.1% of cases. Forty patients (0.8%) discontinued treatment. Conclusion: Sofosbuvir‐based regimens are effective and safe for treating patients with chronic HCV and moderate to severe CKD, and in those with associated hepatic decompensation. [ABSTRACT FROM AUTHOR]

Published
2020
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11. Purification and characterization of theromohalophilic chitinase producing by halophilic Aspergillus flavus isolated from Suez Gulf.

Author

Beltagy, Ehab Aly, Rawway, Mohammed, Abdul-Raouf, Usama Mohamed, Elshenawy, Mohamed Ahmed, and Kelany, Mahmoud Saber

Abstract

Abstract This study aimed at production of chitinase enzyme from marine waste. Out of 27 fungal isolates, Aspergillus flavus (AUMC 13576) obtained from El-Sokhna has proved to be the most potent strain for chitinase production with activity 620.54 U/l using colloidal chitin as carbon source. The enzyme was purified consecutively by ammonium sulphate precipitation, Sephadex G-100 gel filtration column and DEAE - Cellulose A52 ion exchanger chromatographic column. The molecular weight of purified chitinase was estimated to be 30 KDa by SDS-PAGE. The purified enzyme was exposed for different properties investigations. The purified chitinase gave the highest activity (1368.8 U/l) within temperature rang (60 °C) at optimum pH 7.5 and 0.9 g/l of the substrate concentration. The kinetic measurements as Km and Vmax values of the enzyme were determined to be 0.18 g chitin/ml and 274.31 U/l, respectively. The enzyme showed thermal stability at 50 °C for 15 min. in salinity concentrations (NaCl) up to 0.8 M. Among different tested heavy metals, MnCl 2 and FeSO 4 boosted the activity positively. These results indicate the potential of mesophilic A. flavus (AUMC 13576) in the production of chitinases employing shrimp as an ideal substrate. [ABSTRACT FROM AUTHOR]

Published
2018
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13. Harnessing the Power of HPC in Simulation and Optimization of Large Transportation Networks: Spatio-Temporal Traffic Management in the Greater Toronto Area.

Author

Aboudina, Aya, Kamel, Islam, Elshenawy, Mohamed, Abdelgawad, Hossam, and Abdulhai, Baher

Abstract

The significant growth of many urban areas comes at a cost of increasing demand for mobility and traffic congestion in large-scale urban environments. As congestion levels soar to unprecedented levels, and researchers and governments are challenged addressing the basic needs for transportation and mobility; solutions are becoming more complex and untraditional, creating a strong potential for optimization and simulation of large-scale transportation networks. In this paper, we present a generic traffic management framework for solving large-scale constraint optimization problems in advanced Intelligent Transportation systems (ITS) applications. The framework employs a distributed computing approach to enable replicating analysis of large-scale traffic simulation networks, providing a practical mechanism for solving complex optimization problems in transportation applications. We discuss employing the framework in two use cases, congestion pricing and emergency evacuation, targeting optimization of spatial and temporal traffic management. [ABSTRACT FROM PUBLISHER]

Published
2018
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14. What is all this fuss about Tus? Comparison of recent findings from biophysical and biochemical experiments.

Author

Berghuis, Bojk A., Raducanu, Vlad-Stefan, Elshenawy, Mohamed M., Jergic, Slobodan, Depken, Martin, Dixon, Nicholas E., Hamdan, Samir M., and Dekker, Nynke H.

Subjects
ESCHERICHIA coli DNA, DNA replication, PROTEIN-protein interactions, SINGLE molecules, MAGNETIC tweezers
Abstract

Synchronizing the convergence of the two-oppositely moving DNA replication machineries at specific termination sites is a tightly coordinated process in bacteria. InEscherichia coli, a “replication fork trap” – found within a chromosomal region where forks are allowed to enter but not leave – is set by the protein–DNA roadblock Tus–Ter. The exact sequence of events by which Tus–Terblocks replisomes approaching from one direction but not the other has been the subject of controversy for many decades. Specific protein–protein interactions between the nonpermissive face of Tus and the approaching helicase were challenged by biochemical and structural studies. These studies show that it is the helicase-induced strand separation that triggers the formation of new Tus–Terinteractions at the nonpermissive face – interactions that result in a highly stable “locked” complex. This controversy recently gained renewed attention as three single-molecule-based studies scrutinized this elusive Tus–Termechanism – leading to new findings and refinement of existing models, but also generating new questions. Here, we discuss and compare the findings of each of the single-molecule studies to find their common ground, pinpoint the crucial differences that remain, and push the understanding of this bipartite DNA–protein system further. [ABSTRACT FROM PUBLISHER]

Published
2018
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19. Real-time dynamic single-molecule protein sequencing on an integrated semiconductor device.

Author

Reed BD, Meyer MJ, Abramzon V, Ad O, Ad O, Adcock P, Ahmad FR, Alppay G, Ball JA, Beach J, Belhachemi D, Bellofiore A, Bellos M, Beltrán JF, Betts A, Bhuiya MW, Blacklock K, Boer R, Boisvert D, Brault ND, Buxbaum A, Caprio S, Choi C, Christian TD, Clancy R, Clark J, Connolly T, Croce KF, Cullen R, Davey M, Davidson J, Elshenawy MM, Ferrigno M, Frier D, Gudipati S, Hamill S, He Z, Hosali S, Huang H, Huang L, Kabiri A, Kriger G, Lathrop B, Li A, Lim P, Liu S, Luo F, Lv C, Ma X, McCormack E, Millham M, Nani R, Pandey M, Parillo J, Patel G, Pike DH, Preston K, Pichard-Kostuch A, Rearick K, Rearick T, Ribezzi-Crivellari M, Schmid G, Schultz J, Shi X, Singh B, Srivastava N, Stewman SF, Thurston TR, Thurston TR, Trioli P, Tullman J, Wang X, Wang YC, Webster EAG, Zhang Z, Zuniga J, Patel SS, Griffiths AD, van Oijen AM, McKenna M, Dyer MD, and Rothberg JM

Subjects
Amino Acids chemistry, Aminopeptidases, Peptides chemistry, Semiconductors, Sequence Analysis, Protein methods, Proteome, Proteomics methods
Abstract

Studies of the proteome would benefit greatly from methods to directly sequence and digitally quantify proteins and detect posttranslational modifications with single-molecule sensitivity. Here, we demonstrate single-molecule protein sequencing using a dynamic approach in which single peptides are probed in real time by a mixture of dye-labeled N-terminal amino acid recognizers and simultaneously cleaved by aminopeptidases. We annotate amino acids and identify the peptide sequence by measuring fluorescence intensity, lifetime, and binding kinetics on an integrated semiconductor chip. Our results demonstrate the kinetic principles that allow recognizers to identify multiple amino acids in an information-rich manner that enables discrimination of single amino acid substitutions and posttranslational modifications. With further development, we anticipate that this approach will offer a sensitive, scalable, and accessible platform for single-molecule proteomic studies and applications.

Published
2022
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20. Kinesin and dynein use distinct mechanisms to bypass obstacles.

Author

Ferro LS, Can S, Turner MA, ElShenawy MM, and Yildiz A

Subjects
Humans, Dyneins metabolism, Kinesins metabolism, Movement
Abstract

Kinesin-1 and cytoplasmic dynein are microtubule (MT) motors that transport intracellular cargoes. It remains unclear how these motors move along MTs densely coated with obstacles of various sizes in the cytoplasm. Here, we tested the ability of single and multiple motors to bypass synthetic obstacles on MTs in vitro. Contrary to previous reports, we found that single mammalian dynein is highly capable of bypassing obstacles. Single human kinesin-1 motors fail to avoid obstacles, consistent with their inability to take sideways steps on to neighboring MT protofilaments. Kinesins overcome this limitation when working in teams, bypassing obstacles as effectively as multiple dyneins. Cargos driven by multiple kinesins or dyneins are also capable of rotating around the MT to bypass large obstacles. These results suggest that multiplicity of motors is required not only for transporting cargos over long distances and generating higher forces, but also for maneuvering cargos on obstacle-coated MT surfaces., Competing Interests: LF, SC, MT, ME, AY No competing interests declared, (© 2019, Ferro et al.)

Published
2019
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21. Dynamic structure mediates halophilic adaptation of a DNA polymerase from the deep-sea brines of the Red Sea.

Author

Takahashi M, Takahashi E, Joudeh LI, Marini M, Das G, Elshenawy MM, Akal A, Sakashita K, Alam I, Tehseen M, Sobhy MA, Stingl U, Merzaban JS, Di Fabrizio E, and Hamdan SM

Subjects
Indian Ocean, Archaeal Proteins chemistry, DNA-Directed DNA Polymerase chemistry, Molecular Dynamics Simulation, Thermococcus enzymology
Abstract

The deep-sea brines of the Red Sea are remote and unexplored environments characterized by high temperatures, anoxic water, and elevated concentrations of salt and heavy metals. This environment provides a rare system to study the interplay between halophilic and thermophilic adaptation in biologic macromolecules. The present article reports the first DNA polymerase with halophilic and thermophilic features. Biochemical and structural analysis by Raman and circular dichroism spectroscopy showed that the charge distribution on the protein's surface mediates the structural balance between stability for thermal adaptation and flexibility for counteracting the salt-induced rigid and nonfunctional hydrophobic packing. Salt bridge interactions via increased negative and positive charges contribute to structural stability. Salt tolerance, conversely, is mediated by a dynamic structure that becomes more fixed and functional with increasing salt concentration. We propose that repulsive forces among excess negative charges, in addition to a high percentage of negatively charged random coils, mediate this structural dynamism. This knowledge enabled us to engineer a halophilic version of Thermococcus kodakarensis DNA polymerase.-Takahashi, M., Takahashi, E., Joudeh, L. I., Marini, M., Das, G., Elshenawy, M. M., Akal, A., Sakashita, K., Alam, I., Tehseen, M., Sobhy, M. A., Stingl, U., Merzaban, J. S., Di Fabrizio, E., Hamdan, S. M. Dynamic structure mediates halophilic adaptation of a DNA polymerase from the deep-sea brines of the Red Sea.

Published
2018
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