A human fatty acid synthase inhibitor binds β-ketoacyl reductase in the keto-substrate site (Q27694705)

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11 March 2020

title

A human fatty acid synthase inhibitor binds β-ketoacyl reductase in the keto-substrate site (English)

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11 March 2020

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11 March 2020

author name string

Mary Ann Hardwicke

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11 March 2020

Alan R Rendina

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Michael L Moore

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Liping Wang

5

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11 March 2020

Julie A Krueger

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Ramona N Plant

7

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11 March 2020

Rachel D Totoritis

8

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11 March 2020

Guofeng Zhang

9

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11 March 2020

Jacques Briand

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11 March 2020

William A Burkhart

11

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11 March 2020

Kristin K Brown

12

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Cynthia A Parrish

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publication date

3 August 2014

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11 March 2020

published in

Nature Chemical Biology

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11 March 2020

volume

10

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issue

9

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11 March 2020

page(s)

774-779

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Structure and molecular organization of mammalian fatty acid synthase

11 March 2020

cites work

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Fatty acid synthase and the lipogenic phenotype in cancer pathogenesis

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Structure and function of animal fatty acid synthase

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Mitochondrial fatty acid synthesis type II: more than just fatty acids

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Two-site ELISA for the quantitative determination of fatty acid synthase

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Fatty acid synthase as a potential therapeutic target in cancer

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Fatty acid synthase and cancer: new application of an old pathway

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Discovery of GSK837149A, an inhibitor of human fatty acid synthase targeting the beta-ketoacyl reductase reaction

21 January 2018

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New synthetic inhibitors of fatty acid synthase with anticancer activity

21 January 2018

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Imidazopyridine-Based Fatty Acid Synthase Inhibitors That Show Anti-HCV Activity and in Vivo Target Modulation

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Improving drug candidates by design: a focus on physicochemical properties as a means of improving compound disposition and safety

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Substrate recognition by the human fatty-acid synthase.

21 January 2018

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Fatty acid synthase drives the synthesis of phospholipids partitioning into detergent-resistant membrane microdomains.

21 January 2018

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The major sites of cellular phospholipid synthesis and molecular determinants of Fatty Acid and lipid head group specificity

21 January 2018

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Cofactor-induced conformational rearrangements establish a catalytically competent active site and a proton relay conduit in FabG.

21 January 2018

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Simultaneous quantification of malonyl-CoA and several other short-chain acyl-CoAs in animal tissues by ion-pairing reversed-phase HPLC/MS.

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Fatty-acid biosynthesis in man, a pathway of minor importance. Purification, optimal assay conditions, and organ distribution of fatty-acid synthase

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12 December 2020

Discovery of BI 99179, a potent and selective inhibitor of type I fatty acid synthase with central exposure

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12 December 2020

Fatty acid synthase (FAS): a target for cytotoxic antimetabolites in HL60 promyelocytic leukemia cells

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Selective inhibition of fatty acid synthase for lung cancer treatment

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12 December 2020

Acetoacetyl-CoA reductase activity of lactating bovine mammary fatty acid synthase

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12 December 2020

Fatty acid synthetase from pig liver. 2. Characterization of the enzyme complex with oxidoreductase activity for alicyclic ketones as a fatty acid synthetase

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12 December 2020

STUDIES ON LIVER ALCOHOL HYDROGENASE COMPLEXES. 3. MULTIPLE INHIBITION KINETICS IN THE PRESENCE OF TWO COMPETITIVE INHIBITORS

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Derivation of rate equations for multisite ping-pong mechanisms with ping-pong reactions at one or more sites.

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Architecture of mammalian fatty acid synthase at 4.5 A resolution

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Fatty acid synthetase. A steady state kinetic analysis of the reaction catalyzed by the enzyme from pigeon liver

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Identifiers

DOI

10.1038/NCHEMBIO.1603

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:25086508%20AND%20SRC:MED&resulttype=core&format=json

Dimensions Publication ID

11 March 2020

1034702400

0 references

1 reference

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