Machin Jonathan M相关文献与解析，生知库

Molecular insights into how the motions of the β-barrel and POTRA domains of BamA are coupled for efficient function

从分子层面深入了解BamA的β桶状结构域和POTRA结构域的运动如何耦合以实现高效功能

Csoma, Naemi; Machin, Jonathan M; Whitehouse, James M; Rodrìguez-Alonso, Raquel; Olejnik, Monika; Cahill, Adam K; Cho, Seung-Hyun; Schäberle, Till F; Iorga, Bogdan I; Ranson, Neil A; Radford, Sheena E; Calabrese, Antonio N; Collet, Jean-François

发表日期：2025

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OmpA Specifically Modulates the Activity of Enzymes that Reside in the Crowded Bacterial Outer Membrane.

OmpA 专门调节位于拥挤的细菌外膜中的酶的活性

期刊:Journal of Molecular Biology

影响因子:4.5

doi:10.1016/j.jmb.2025.169346

Machin Jonathan M, Ranson Neil A, Radford Sheena E

微生物学

发表日期：2025

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Protein-induced membrane asymmetry modulates OMP folding kinetics and stability

蛋白质诱导的膜不对称性调节外膜蛋白的折叠动力学和稳定性

期刊:Faraday Discussions

影响因子:3.1

doi:10.1039/d4fd00180j

Machin, Jonathan M; Ranson, Neil A; Radford, Sheena E

发表日期：2025

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Dual client binding sites in the ATP-independent chaperone SurA

ATP非依赖性分子伴侣SurA中的双重客户结合位点

期刊:Nature Communications

影响因子:15.7

doi:10.1038/s41467-024-52021-1

Schiffrin, Bob; Crossley, Joel A; Walko, Martin; Machin, Jonathan M; Nasir Khan, G; Manfield, Iain W; Wilson, Andrew J; Brockwell, David J; Fessl, Tomas; Calabrese, Antonio N; Radford, Sheena E; Zhuravleva, Anastasia

发表日期：2024

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Protein-lipid charge interactions control the folding of outer membrane proteins into asymmetric membranes

蛋白质-脂质电荷相互作用控制外膜蛋白折叠成不对称膜

期刊:Nature Chemistry

影响因子:20.2

doi:10.1038/s41557-023-01319-6

Machin, Jonathan M; Kalli, Antreas C; Ranson, Neil A; Radford, Sheena E

发表日期：2023

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Dynamic interplay between the periplasmic chaperone SurA and the BAM complex in outer membrane protein folding

周质分子伴侣SurA与BAM复合物在胞外膜蛋白折叠中的动态相互作用

期刊:Communications Biology

影响因子:5.1

doi:10.1038/s42003-022-03502-w

Schiffrin, Bob; Machin, Jonathan M; Karamanos, Theodoros K; Zhuravleva, Anastasia; Brockwell, David J; Radford, Sheena E; Calabrese, Antonio N

发表日期：2022

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The complex of Plasmodium falciparum falcipain-2 protease with an (E)-chalcone-based inhibitor highlights a novel, small, molecule-binding site

恶性疟原虫恶性蛋白酶-2与(E)-查尔酮类抑制剂的复合物揭示了一种新型的小分子结合位点

期刊:Malaria Journal

影响因子:3

doi:10.1186/s12936-019-3043-0

Machin, Jonathan M; Kantsadi, Anastassia L; Vakonakis, Ioannis

发表日期：2019

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Integration of Membrane Proteins into the Outer Membrane of Diderm Bacteria by the BAM Complex

BAM复合物将膜蛋白整合到双膜细菌的外膜中

Molecular insights into how the motions of the β-barrel and POTRA domains of BamA are coupled for efficient function

从分子层面深入了解BamA的β桶状结构域和POTRA结构域的运动如何耦合以实现高效功能

OmpA Specifically Modulates the Activity of Enzymes that Reside in the Crowded Bacterial Outer Membrane.

OmpA 专门调节位于拥挤的细菌外膜中的酶的活性

Protein-induced membrane asymmetry modulates OMP folding kinetics and stability

蛋白质诱导的膜不对称性调节外膜蛋白的折叠动力学和稳定性

Dual client binding sites in the ATP-independent chaperone SurA

ATP非依赖性分子伴侣SurA中的双重客户结合位点

Protein-lipid charge interactions control the folding of outer membrane proteins into asymmetric membranes

蛋白质-脂质电荷相互作用控制外膜蛋白折叠成不对称膜

Dynamic interplay between the periplasmic chaperone SurA and the BAM complex in outer membrane protein folding

周质分子伴侣SurA与BAM复合物在胞外膜蛋白折叠中的动态相互作用

The complex of Plasmodium falciparum falcipain-2 protease with an (E)-chalcone-based inhibitor highlights a novel, small, molecule-binding site

恶性疟原虫恶性蛋白酶-2与(E)-查尔酮类抑制剂的复合物揭示了一种新型的小分子结合位点