Nature Search

Design and application of synthetic 17B-HSD13 substrates reveals preserved catalytic activity of protective human variants

Several 17B-HSD13 variants have been identified as protective against NASH/MASH. However the protein’s endogenous function is unknown. Here authors describe sulfonamide-based inhibitors and synthetic substrates, then apply to multiple cellular systems revealing that the most prevalent IsoD variant maintains NAD-dependent catalytic activity.

Michelle R. Garnsey
Yang Wang
Michelle F. Clasquin
ResearchOpen Access02 Jan 2025
Nature Communications

Volume: 16, P: 1-10
Structural basis of lipid-droplet localization of 17-beta-hydroxysteroid dehydrogenase 13

Hydroxysteroid 17-beta-dehydrogenase 13 (HSD17B13) is a hepatic lipid droplet-associated enzyme that is upregulated in patients with non-alcoholic fatty liver disease. Here, the authors report crystal structures of HSD17B13 and its complexes with two series of inhibitors.

Shenping Liu
Ruth F. Sommese
Michelle F. Clasquin
ResearchOpen Access24 Aug 2023
Nature Communications

Volume: 14, P: 1-14
De novo lipogenesis is essential for platelet production in humans

Pharmacological targeting of de novo lipogenesis is an attractive clinical target for a wide range of diseases. Kelly et al. report that de novo lipogenesis is essential for platelet production in primates, but not in dogs and rats.

Kenneth L. Kelly
William J. Reagan
William P. Esler
Research14 Sept 2020
Nature Metabolism

Volume: 2, P: 1163-1178
Correction: Corrigendum: mTORC1-dependent AMD1 regulation sustains polyamine metabolism in prostate cancer

Amaia Zabala-Letona
Amaia Arruabarrena-Aristorena
Arkaitz Carracedo
Amendments and Corrections17 Jan 2018
Nature

Volume: 554, P: 554
Serine catabolism generates liver NADPH and supports hepatic lipogenesis

Liver and adipose tissue are shown to use different metabolic routes to generate NADPH for de novo lipogenesis, with the liver relying on a unique cytosolic serine catabolic pathway involving the enzyme SHMT1.

Zhaoyue Zhang
Tara TeSlaa
Joshua D. Rabinowitz
Research29 Nov 2021
Nature Metabolism

Volume: 3, P: 1608-1620
mTORC1-dependent AMD1 regulation sustains polyamine metabolism in prostate cancer

mTOR complex 1 signalling regulates polyamine metabolism and thereby promotes tumorigenesis, through regulation of the stability of a key enzyme, AMD1.

Amaia Zabala-Letona
Amaia Arruabarrena-Aristorena
Arkaitz Carracedo
Research28 Jun 2017
Nature

Volume: 547, P: 109-113

Search

Filter By:

Design and application of synthetic 17B-HSD13 substrates reveals preserved catalytic activity of protective human variants

Structural basis of lipid-droplet localization of 17-beta-hydroxysteroid dehydrogenase 13

De novo lipogenesis is essential for platelet production in humans

Correction: Corrigendum: mTORC1-dependent AMD1 regulation sustains polyamine metabolism in prostate cancer

Serine catabolism generates liver NADPH and supports hepatic lipogenesis

mTORC1-dependent AMD1 regulation sustains polyamine metabolism in prostate cancer

Search

Quick links