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Oded Lewinson

Researcher at Technion – Israel Institute of Technology

Publications -  40
Citations -  2983

Oded Lewinson is an academic researcher from Technion – Israel Institute of Technology. The author has contributed to research in topics: ATP-binding cassette transporter & ATP hydrolysis. The author has an hindex of 22, co-authored 39 publications receiving 2525 citations. Previous affiliations of Oded Lewinson include California Institute of Technology & Rappaport Faculty of Medicine.

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ABC transporters: the power to change

TL;DR: An important goal is to develop quantitative models that detail the kinetic and molecular mechanisms by which ABC transporters couple the binding and hydrolysis of ATP to substrate translocation.
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Structural basis for heavy metal detoxification by an atm1-type abc exporter

TL;DR: In this paper, structural analysis of the Atm1/ABCB7/HMT1 /ABCB6 ortholog from Novosphingobium aromaticivorans DSM 12444, NaAtm1, at 2.4 angstrom resolution is presented.
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The Size of the Proteasomal Substrate Determines Whether Its Degradation Will Be Mediated by Mono- Or Polyubiquitylation

TL;DR: It is demonstrated that the size of the substrate is an important determinant in its extent of ubiquitylation: a single ubiquitin moiety fused to a tail of up to ∼150 residues derived from either short artificial repeats or from naturally occurring proteins, is sufficient to target them for proteasomal degradation.
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Structural and functional diversity calls for a new classification of ABC transporters.

Christoph Thomas, +44 more
- 01 Dec 2020 - 
TL;DR: A new ABC transporter classification that currently comprises seven different types based on structural homology in the TMDs is proposed, suggesting that during evolution, the ancient motor domains were combined with different transmembrane mechanical systems to orchestrate a variety of cellular processes.
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Alkalitolerance: A biological function for a multidrug transporter in pH homeostasis

TL;DR: It is demonstrated that a single protein has an unprecedented capacity to turn E. coli from an obligatory neutrophile into an alkalitolerant bacterium, and a previously uncharacterized physiological role for MdfA in pH homeostasis is suggested.