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High specificity of a phosphate transport protein determined by hydrogen bonds

Hartmut Luecke
Florante A. Quiocho
Research27 Sept 1990
Nature

Volume: 347, P: 402-406
Cryo-EM structure of native honey bee vitellogenin

Vitellogenin is present in almost all egg-laying animals and is known for its multiple functions in reproduction, immunity and social organization. Here, the authors present the cryo-EM structure of native Vitellogenin from the honey bee.

Mateu Montserrat-Canals
Kilian Schnelle
Hartmut Luecke
ResearchOpen Access01 Jul 2025
Nature Communications

Volume: 16, P: 1-13
Crystal structure of the annexin XII hexamer and implications for bilayer insertion

Hartmut Luecke
Bryna T. Chang
Harry T. Haigler
Research30 Nov 1995
Nature

Volume: 378, P: 512-515
A low energy short hydrogen bond in very high resolution structures of protein receptor-phosphate complexes

A very short hydrogen bond between an Asp and a phosphate is established in two high resolution structures (0.98 and 1.05 Å). A mutant complex that changes the Asp to an Asn, which forms a normal hydrogen bond, has a similar free energy of binding to the wild type complex, suggesting that the contribution of the short hydrogen bond is not extraordinarily strong.

Zhongmin Wang
Hartmut Luecke
Florante A. Quiocho
Correspondence01 Jul 1997
Nature Structural Biology

Volume: 4, P: 519-522
Author Correction: Cryo-EM structure of Helicobacter pylori urease with an inhibitor in the active site at 2.0 Å resolution

Eva S. Cunha
Xiaorui Chen
Hartmut Luecke
Amendments and CorrectionsOpen Access06 Feb 2023
Nature Communications

Volume: 14, P: 1
Oleylethanolamide regulates feeding and body weight through activation of the nuclear receptor PPAR-α

Jin Fu
Silvana Gaetani
Daniele Piomelli
Research04 Sept 2003
Nature

Volume: 425, P: 90-93
Cryo-EM structure of Helicobacter pylori urease with an inhibitor in the active site at 2.0 Å resolution

Infection by Helicobacter pylori is associated with peptic ulcers and gastric cancer. H. pylori urease is required for colonization of the stomach and thus an attractive antimicrobial drug target. Cryo-EM analyses of the H. pylori urease with inhibitors bound reveal structural details useful in rational drug design.

Eva S. Cunha
Xiaorui Chen
Hartmut Luecke
ResearchOpen Access11 Jan 2021
Nature Communications

Volume: 12, P: 1-8
Structure of the proton-gated urea channel from the gastric pathogen Helicobacter pylori

The crystal structure of the inner-membrane urea channel HpUreI from Helicobacter pylori, the causative organism of peptic ulcers, reveals how the channel selectively transports urea across the membrane and buffers the pathogen’s periplasmic pH against the acidic gastric environment.

David Strugatsky
Reginald McNulty
Hartmut Luecke
Research09 Dec 2012
Nature

Volume: 493, P: 255-258
Computational identification of a transiently open L1/S3 pocket for reactivation of mutant p53

About 40% of human cancers carry missense mutations in the tumour suppressor protein p53. Here the authors identify a transiently open pocket in the protein, and by targeting a small molecule to it, partially restore mutant p53 tumour suppressor activity.

Christopher D. Wassman
Roberta Baronio
Rommie E. Amaro
ResearchOpen Access29 Jan 2013
Nature Communications

Volume: 4, P: 1-9
Mechanisms of molecular transport through the urea channel of Helicobacter pylori

Helicobacter pylori survives in the acidic environment of the stomach by taking up urea and converting it to ammonia and carbon dioxide, which buffer the bacterial periplasm. Using molecular dynamics simulations, McNulty et al. provide insight into the mechanism of urea uptake through the H. pyloriurea transporter.

Reginald McNulty
Jakob P. Ulmschneider
Martin B. Ulmschneider
ResearchOpen Access05 Dec 2013
Nature Communications

Volume: 4, P: 1-10

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High specificity of a phosphate transport protein determined by hydrogen bonds

Cryo-EM structure of native honey bee vitellogenin

Crystal structure of the annexin XII hexamer and implications for bilayer insertion

A low energy short hydrogen bond in very high resolution structures of protein receptor-phosphate complexes

Author Correction: Cryo-EM structure of Helicobacter pylori urease with an inhibitor in the active site at 2.0 Å resolution

Oleylethanolamide regulates feeding and body weight through activation of the nuclear receptor PPAR-α

Cryo-EM structure of Helicobacter pylori urease with an inhibitor in the active site at 2.0 Å resolution

Structure of the proton-gated urea channel from the gastric pathogen Helicobacter pylori

Computational identification of a transiently open L1/S3 pocket for reactivation of mutant p53

Mechanisms of molecular transport through the urea channel of Helicobacter pylori

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