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Structural basis of ligand binding modes at the neuropeptide Y Y₁ receptor

Crystal structures of the neuropeptide Y₁ receptor in complex with two distinct antagonists combined with NMR, molecular docking and mutagenesis studies inform a proposed model for receptor–agonist binding.

Zhenlin Yang
Shuo Han
Beili Wu
Research18 Apr 2018
Nature

Volume: 556, P: 520-524
100 Hz ROCS microscopy correlated with fluorescence reveals cellular dynamics on different spatiotemporal scales

In live-cell microscopy, motion blur limits resolution and contrast. Here the authors use 100 Hz super-resolving Rotating Coherent Scattering (ROCS) microscopy on various dynamic biological systems, and time-window analysis to understand biological effects.

Felix Jünger
Dominic Ruh
Alexander Rohrbach
ResearchOpen Access01 Apr 2022
Nature Communications

Volume: 13, P: 1-17
Thrombospondin-4 reduces binding affinity of [³H]-gabapentin to calcium-channel α₂δ-1-subunit but does not interact with α₂δ-1 on the cell-surface when co-expressed

Beatrice Lana
Karen M. Page
Annette C. Dolphin
ResearchOpen Access14 Apr 2016
Scientific Reports

Volume: 6, P: 1-14
Altered intestinal microbiota–host mitochondria crosstalk in new onset Crohn’s disease

Crohn’s disease is associated with altered intestinal microbiota. Here, the authors show that the microbe Atopobium parvulumis associated with Crohn’s disease patients, triggers colitis in a mouse model, and that scavenging microbe-induced hydrogen sulfide improved symptoms in mice.

Walid Mottawea
Cheng-Kang Chiang
Alain Stintzi
ResearchOpen Access23 Nov 2016
Nature Communications

Volume: 7, P: 1-14
MHC class II proteins mediate cross-species entry of bat influenza viruses

The DR isotype of the human leukocyte antigen of the MHC class II—or its homologues in bats, pigs, mice and chickens—is an essential cell entry determinant for bat influenza A viruses.

Umut Karakus
Thiprampai Thamamongood
Silke Stertz
Research20 Feb 2019
Nature

Volume: 567, P: 109-112
The bacterial lectin LecA from P. aeruginosa alters membrane organization by dispersing ordered domains

Continuous, dynamic organisation of plasma membrane nanodomains, or lipid rafts, are closely related to membrane recognition and infection. The authors use supported lipid bilayers to study how the bacterial lectin LecA affects the nanometric organisation of membranes, with potential implications in regulating bacterial infection.

Taras Sych
Ramin Omidvar
Winfried Römer
ResearchOpen Access29 Jun 2023
Communications Physics

Volume: 6, P: 1-11
Differential recognition of lipid domains by two Gb3-binding lectins

Thomas Schubert
Taras Sych
Winfried Römer
ResearchOpen Access16 Jun 2020
Scientific Reports

Volume: 10, P: 1-12

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Structural basis of ligand binding modes at the neuropeptide Y Y₁ receptor

100 Hz ROCS microscopy correlated with fluorescence reveals cellular dynamics on different spatiotemporal scales

Thrombospondin-4 reduces binding affinity of [³H]-gabapentin to calcium-channel α₂δ-1-subunit but does not interact with α₂δ-1 on the cell-surface when co-expressed

Altered intestinal microbiota–host mitochondria crosstalk in new onset Crohn’s disease

MHC class II proteins mediate cross-species entry of bat influenza viruses

The bacterial lectin LecA from P. aeruginosa alters membrane organization by dispersing ordered domains

Differential recognition of lipid domains by two Gb3-binding lectins

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Structural basis of ligand binding modes at the neuropeptide Y Y1 receptor

100 Hz ROCS microscopy correlated with fluorescence reveals cellular dynamics on different spatiotemporal scales

Thrombospondin-4 reduces binding affinity of [3H]-gabapentin to calcium-channel α2δ-1-subunit but does not interact with α2δ-1 on the cell-surface when co-expressed

Altered intestinal microbiota–host mitochondria crosstalk in new onset Crohn’s disease

MHC class II proteins mediate cross-species entry of bat influenza viruses

The bacterial lectin LecA from P. aeruginosa alters membrane organization by dispersing ordered domains

Differential recognition of lipid domains by two Gb3-binding lectins

Search

Quick links

Structural basis of ligand binding modes at the neuropeptide Y Y₁ receptor

Thrombospondin-4 reduces binding affinity of [³H]-gabapentin to calcium-channel α₂δ-1-subunit but does not interact with α₂δ-1 on the cell-surface when co-expressed