Results 31 to 40 of about 11,653 (194)

Mapping allosteric communications within individual proteins

Nature Communications, 2020
The computational prediction of protein allostery can guide experimental studies of protein function and cellular activity. Here, the authors develop a network-based method to detect allosteric coupling within proteins solely based on their structures ...
Jian Wang, Abha Jain, Leanna R. McDonald, Craig Gambogi, Andrew L. Lee, Nikolay V. Dokholyan   +5 more
doaj   +1 more source

The genotype‐phenotype landscape of an allosteric protein

Molecular Systems Biology, 2021
Allostery is a fundamental biophysical mechanism that underlies cellular sensing, signaling, and metabolism. Yet a quantitative understanding of allosteric genotype‐phenotype relationships remains elusive.
Drew S Tack, Peter D Tonner, Abe Pressman, Nathan D Olson, Sasha F Levy, Eugenia F Romantseva, Nina Alperovich, Olga Vasilyeva, David Ross   +8 more
doaj   +1 more source

AIM for Allostery: Using the Ising Model to Understand Information Processing and Transmission in Allosteric Biomolecular Systems

Entropy, 2015
In performing their biological functions, molecular machines must process and transmit information with high fidelity. Information transmission requires dynamic coupling between the conformations of discrete structural components within the protein ...
Michael V. LeVine, Harel Weinstein
doaj   +1 more source

Allostery in the dynamic coactivator domain KIX occurs through minor conformational micro-states.

PLoS Computational Biology, 2022
The coactivator KIX of CBP uses two binding surfaces to recognize multiple activators and exhibits allostery in ternary complex formation. Activator•coactivator interactions are central to transcriptional regulation, yet the microscopic origins of ...
Amanda L Peiffer, Julie M Garlick, Stephen T Joy, Anna K Mapp, Charles L Brooks   +4 more
doaj   +1 more source

Investigation of the Possible Allostery of Koumine Extracted From Gelsemium elegans Benth. And Analgesic Mechanism Associated With Neurosteroids

Frontiers in Pharmacology, 2021
Translocator protein 18 kDa (TSPO) is an evolutionarily conserved 5-transmembrane domain protein, and has been considered as an important therapeutic target for the treatment of pain.
Bojun Xiong, Bojun Xiong, Wenbing You, Yufei Luo, Guilin Jin, Guilin Jin, Minxia Wu, Ying Xu, Ying Xu, Jian Yang, Jian Yang, Huihui Huang, Changxi Yu, Changxi Yu   +13 more
doaj   +1 more source

Identification of Koumine as a Translocator Protein 18 kDa Positive Allosteric Modulator for the Treatment of Inflammatory and Neuropathic Pain

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, Bojun Xiong, Guilin Jin, Guilin Jin, Ying Xu, Ying Xu, Wenbing You, Yufei Luo, Menghan Fang, Bing Chen, Huihui Huang, Jian Yang, Jian Yang, Xu Lin, Changxi Yu, Changxi Yu   +15 more
doaj   +1 more source

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
openaire   +3 more sources

Quantitative Analysis of Dynamic Allostery

, 2022
Dynamic allostery refers to one important class of allosteric regulation that does not involve noticeable conformational changes upon effector binding.
Zhirong Liu, Qiaojing Huang, Zhirong Liu (135388), Luhua Lai (36732), Qiaojing Huang (9521556), Luhua Lai   +5 more
core   +1 more source

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, David B Ascher, Michael Inouye   +2 more
doaj   +1 more source

Multi-scale Modelling of Allostery in Protein Homodimers [PDF]

, 2015
Allostery is a form of signalling within biomolecules such that ligand binding to a protein affects its activity at a second site. Allostery was described by early models to be driven by structural changes in the protein. However, more recently there has
BURNELL, DAVID
core   +6 more sources