Results 41 to 50 of about 10,740 (213)
Known allosteric proteins have central roles in genetic disease.
PLoS Computational Biology, 2022 Allostery is a form of protein regulation, where ligands that bind sites located apart from the active site can modify the activity of the protein. The molecular mechanisms of allostery have been extensively studied, because allosteric sites are less ...
György Abrusán +2 more
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Frontiers in Pharmacology, 2021 Koumine is an alkaloid that displays notable activity against inflammatory and neuropathic pain, but its therapeutic target and molecular mechanism still need further study.
Bojun Xiong +15 more
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Frontiers in Molecular Biosciences, 2023 Mesophilic and thermophilic enzyme counterparts are often studied to understand how proteins function under harsh conditions. To function well outside of standard temperature ranges, thermophiles often tightly regulate their structural ensemble through ...
Alexa L. Knight +2 more
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Allostery and Kinetic Proofreading [PDF]
The Journal of Physical Chemistry B, 2019 Kinetic proofreading is an error correction mechanism present in the processes of the central dogma and beyond, and typically requires the free energy of nucleotide hydrolysis for its operation. Though the molecular players of many biological proofreading schemes are known, our understanding of how energy consumption is managed to promote fidelity ...
Vahe Galstyan, Rob Phillips
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PLoS Biology, 2013 Allostery is a fundamental process by which ligand binding to a protein alters its activity at a distinct site. There is growing evidence that allosteric cooperativity can be communicated by modulation of protein dynamics without conformational change ...
Thomas L Rodgers +8 more
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Angewandte Chemie, EarlyView.This work explores the interactions between the oxazine dye ATTO655 and two macrocyclic hosts using optical (single‑molecule) spectroscopy. Although ATTO655 forms a classical inclusion complex with cucurbit[8]uril (CB8), its interaction with p‑sulfonatocalix[4]arene (sCX4) leads to the formation of dim exclusion complexes.
Siyu Lu +7 more
wiley +2 more sources
Angewandte Chemie, EarlyView.Hsf1 undergoes phase separation around target DNA, activating stress‐responsive transcription. DNA binding tunes conformational dynamics of Hsf1DBD, which propagates through large‐scale domain rearrangements involving DBD–IDR interactions to regulate phase separation. This hierarchical framework illustrates how local structural events at the side chain
Soichiro Kawagoe +2 more
wiley +2 more sources
Long-Range Signaling in MutS and MSH Homologs via Switching of Dynamic Communication Pathways. [PDF]
PLoS Computational Biology, 2016 Allostery is conformation regulation by propagating a signal from one site to another distal site. This study focuses on the long-range communication in DNA mismatch repair proteins MutS and its homologs where intramolecular signaling has to travel over ...
Beibei Wang +5 more
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Evidence of variable human Fcγ receptor-Fc affinities across differentially-complexed IgG
mAbs, 2023 Antibody-mediated effector functions are widely considered to unfold according to an associative model of IgG-Fcγ receptor (FcγR) interactions. The associative model presupposes that Fc receptors cannot discriminate antigen-bound IgG from free IgG in ...
Andrew R. Crowley +5 more
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Decoding the mechanisms of allostery
eLife, 2023 A complex interplay between structure, conformational dynamics and pharmacology defines distant regulation of G protein-coupled receptors.
Saif Khan, Cornelius Gati
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