Abid Javed
Birkbeck, University of London
11 Papers
Abid Javed is an academic researcher from Birkbeck, University of London. The author has contributed to research in topics: Medicine & Internal medicine. The author has an hindex of 3, co-authored 4 publications. Previous affiliations of Abid Javed include University College London.
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Papers
Unravelling Ribosome Function Through Structural Studies.
Abid Javed,Elena V. Orlova +1 more
TL;DR: This article provides a comprehensive overview of ribosomal structures that represent structural snapshots of the ribosome at its different functional states and gradually improves understanding of this process and how it can be regulated and how the specific ribosomes can be stalled or activated, or completely disabled.
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The use of water immersion technique during device-assisted (single-balloon) enteroscopy to treat actively bleeding jejunal Dieulafoy's lesion
TL;DR: In this paper , the use of the water immersion technique during device-assisted (single-balloon) enteroscopy to treat actively bleeding jejunal Dieulafoy's lesion was described.
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S311 Following Through on Positive Fecal Immunochemical Testing via FIT Navigation and a Direct-to-Colonoscopy Pathway: Preparing for the Next Wave
S Bhaskar,Azubuogu Anudu,Wesley Wright,Samuel O. Slone,S. Prabakaran,Saritza Mendoza,Abid Javed,Philip R. Foulis,Jason Colizzo,Wojciech Blonski,Kaileen Legard,Jose Lezama +11 more
TL;DR: In this paper , the unadjusted and adjusted association between late and early pandemic proportion receiving colonoscopy < 180 days was assessed using binary logistic regression, summarized as odds ratio (OR) and 95% confidence intervals (CI).
Visualising nascent chain dynamics at the ribosome exit tunnel by cryo-electron microscopy
Abid Javed,Lisa D. Cabrita,Anaïs M. E. Cassaignau,Tomasz Wlodarski,John Christodoulou,Elena V. Orlova +5 more
TL;DR: High-resolution cryo-EM structures of stalled ribosomal nascent-chain complexes (RNCs) at two biosynthetic translation time-points that examine the role of the ribosome during co-translational folding reveal that NC is highly dynamic and adopts a range of trajectories within the vestibule of the exit tunnel, affecting positions of the folded immunoglobulin domain outside the ribsome.