Alaa Abdine

ORCID: 0000-0003-1924-1819
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About
Contact & Profiles
Research Areas
  • Lipid Membrane Structure and Behavior
  • Protein Structure and Dynamics
  • RNA and protein synthesis mechanisms
  • Advanced NMR Techniques and Applications
  • Ion channel regulation and function
  • Protein Interaction Studies and Fluorescence Analysis
  • Solid-state spectroscopy and crystallography
  • Venomous Animal Envenomation and Studies
  • Crystallography and Radiation Phenomena
  • ATP Synthase and ATPases Research
  • Advanced Biosensing Techniques and Applications
  • Monoclonal and Polyclonal Antibodies Research
  • Nanopore and Nanochannel Transport Studies
  • Drug Transport and Resistance Mechanisms
  • Enzyme Structure and Function
  • Alzheimer's disease research and treatments
  • Carbon Nanotubes in Composites
  • Cellular Mechanics and Interactions
  • Advanced biosensing and bioanalysis techniques

Icahn School of Medicine at Mount Sinai
2014-2018

Université Paris Cité
2010-2011

Centre National de la Recherche Scientifique
2010-2011

Institut de Biologie Physico-Chimique
2008-2011

Délégation Paris 7
2010-2011

Sorbonne Université
2010

Because of the importance their physiological functions, cell membranes represent critical targets in biological research. Membrane proteins, which make up approximately 1/3 proteome, interact with a wide range small ligands and macromolecular partners as well foreign molecules such synthetic drugs, antibodies, toxins, or surface recognition proteins pathogenic organisms. Whether it is for sake basic biomedical pharmacological research, great interest to develop tools facilitating study...

10.1073/pnas.0807132106 article EN Proceedings of the National Academy of Sciences 2008-12-31

Intramembrane-cleaving proteases (I-CLiPs) play crucial roles in physiological and pathological processes, such as Alzheimer's disease cancer. However, the mechanisms of substrate recognition by I-CLiPs remain poorly understood. The aspartic I-CLiP presenilin is catalytic subunit γ-secretase complex, which releases amyloid-β peptides (Aβs) through intramembrane proteolysis transmembrane domain amyloid precursor protein (APPTM). Here we used solution NMR to probe docking APPTM homologs (PSHs)...

10.1038/s41598-018-30015-6 article EN cc-by Scientific Reports 2018-08-13
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