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Articles by Daniel Saar
Autoinhibition of untimely DNA binding by structural disorder in the full-length peroxisome proliferator-activated receptors (PPARs)
Abstract Structural disorder in nuclear receptors is essential for gene transcription, but mechanisms are lacking. Using experiment and computation, including residue-resolution NMR, we demonstrate how structural disorder in full-length peroxisome proliferator-activated receptors (PPARs) contributes to function.
Role of charges in a dynamic disordered complex between an IDP and a folded domain - Nature Communications
Abstract Protein complexes involving intrinsically disordered proteins (IDPs) cover a continuum from IDPs that fully fold upon binding to IDPs that remain fully disordered in the complex. Here we demonstrate a case of charge-driven interactions of a folded domain with an oppositely charged IDP that remains completely disordered in the complex.
The Myotubularin Related Proteins and the Untapped Interaction Potential of Their Disordered C‐Terminal Regions
1 Introduction Myotubularin-related proteins are a large protein family that is named after myotubular myopathy (MTM1) and their original member myotubularin, also called MTM1 [1]. The family consists of 16 members named MTM1, and MTMR1 up to MTMR15, collectively referred to as MTMRs [2-4]. MTMRs are ubiquitously expressed in the human body, notably in the peripheral nervous system and in the gastrointestinal tract, inhabiting diverse locations within the cell.
The GET insertase exhibits conformational plasticity and induces membrane thinning - Nature Communications
Abstract The eukaryotic guided entry of tail-anchored proteins (GET) pathway mediates the biogenesis of tail-anchored (TA) membrane proteins at the endoplasmic reticulum. In the cytosol, the Get3 chaperone captures the TA protein substrate and delivers it to the Get1/Get2 membrane protein complex (GET insertase), which then inserts the substrate via a membrane-embedded hydrophilic groove.
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