Nature Search

Erratum: Transduction of bitter and sweet taste by gustducin

Gwendolyn T. Wong
Kimberley S. Gannon
Robert F. Margolskee
Amendments and Corrections10 Oct 1996
Nature

Volume: 383, P: 557
Crystal structure of a PDZ domain

João H. Morais Cabral
Carlo Petosa
Robert C. Liddington
Research15 Aug 1996
Nature

Volume: 382, P: 649-652
Activation of nif gene expression in Azotobacter by the nifA gene product of Klebsiella pneumoniae

Christina Kennedy
Robert L. Robson
Research17 Feb 1983
Nature

Volume: 301, P: 626-628
Bile salt hydrolase acyltransferase activity expands bile acid diversity

Acyltransferase activity of the enzyme bile salt hydrolase is identified and shown to mediate microbial bile acid conjugation, diversifying the bile acid pool and expanding their role in gut physiology.

Douglas V. Guzior
Maxwell Okros
Robert A. Quinn
Research07 Feb 2024
Nature

Volume: 626, P: 852-858
Oxidative demethylation by Escherichia coli AlkB directly reverts DNA base damage

Sarah C. Trewick
Timothy F. Henshaw
Barbara Sedgwick
Research12 Sept 2002
Nature

Volume: 419, P: 174-178
Inhibitors of Mycobacterium tuberculosis DosRST signaling and persistence

A high-throughput screen identifies inhibitors of the M. tuberculosis dormancy regulation system, DosRST, including compounds that inhibit autophosphorylation of the DosS and DosT sensor kinases and those that inhibit the catalytic heme of these kinases.

Huiqing Zheng
Christopher J Colvin
Robert B Abramovitch
Research19 Dec 2016
Nature Chemical Biology

Volume: 13, P: 218-225
Ni and CO: more surprises

Recent structural studies of acetyl-coenzyme A synthase/carbon monoxide dehydrogenase from Moorella thermoacetica revealed a unique Cu-Ni-[Fe₄-S₄] active site. New data now indicate that active enzyme contains a Ni-Ni-[Fe₄-S₄] site. Novel chemistry is posited for the central Ni atom of this enzyme, which utilizes the toxic gas CO as a catalytic intermediate.

Robert P. Hausinger
News & Views01 Apr 2003
Nature Structural & Molecular Biology

Volume: 10, P: 234-236
Transformation by the (R)-enantiomer of 2-hydroxyglutarate linked to EGLN activation

The (R)-enantiomer of 2-hydroxyglutarate, which is produced when IDH is mutated in human tumours, is shown to stimulate the activity of the EGLN prolyl 4-hydroxylases, leading to diminished levels of HIF and enhanced human astrocyte proliferation.

Peppi Koivunen
Sungwoo Lee
William G. Kaelin Jr
Research15 Feb 2012
Nature

Volume: 483, P: 484-488
Uncovering a superfamily of nickel-dependent hydroxyacid racemases and epimerases

Benoît Desguin
Julian Urdiain-Arraiza
Patrice Soumillion
ResearchOpen Access22 Oct 2020
Scientific Reports

Volume: 10, P: 1-11
Crystallographic characterization of a tri-Asp metal-binding site at the three-fold symmetry axis of LarE

Matthias Fellner
Kamren G. Huizenga
Jian Hu
ResearchOpen Access02 Apr 2020
Scientific Reports

Volume: 10, P: 1-9
Host–pathogen interactions in urinary tract infection

Urinary tract infections are experienced by a large section of the population and cause significant morbidity. Here, Nielubowicz and Mobley explain the pathogenic mechanisms utilized byEscherichia coli and Proteus mirabilisduring complicated and uncomplicated infection, respectively. They outline the strategies currently underway to exploit these processes for the identification of new treatment options.

Greta R. Nielubowicz
Harry L. T. Mobley
Reviews20 Jul 2010
Nature Reviews Urology

Volume: 7, P: 430-441

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Erratum: Transduction of bitter and sweet taste by gustducin

Crystal structure of a PDZ domain

Activation of nif gene expression in Azotobacter by the nifA gene product of Klebsiella pneumoniae

Bile salt hydrolase acyltransferase activity expands bile acid diversity

Oxidative demethylation by Escherichia coli AlkB directly reverts DNA base damage

Inhibitors of Mycobacterium tuberculosis DosRST signaling and persistence

Ni and CO: more surprises

Transformation by the (R)-enantiomer of 2-hydroxyglutarate linked to EGLN activation

Uncovering a superfamily of nickel-dependent hydroxyacid racemases and epimerases

Crystallographic characterization of a tri-Asp metal-binding site at the three-fold symmetry axis of LarE

Host–pathogen interactions in urinary tract infection

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