Crystal structure of the thioesterase domain of human fatty acid synthase inhibited by Orlistat (Q27646595)

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English	Crystal structure of the thioesterase domain of human fatty acid synthase inhibited by Orlistat	scientific article

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instance of

scholarly article

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title

Crystal structure of the thioesterase domain of human fatty acid synthase inhibited by Orlistat (English)

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main subject

crystal structure

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fatty acid

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author name string

Charles W Pemble

series ordinal

1

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Lynnette C Johnson

series ordinal

2

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Steven J Kridel

series ordinal

3

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W Todd Lowther

series ordinal

4

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publication date

August 2007

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published in

Nature Structural & Molecular Biology

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volume

14

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issue

8

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page(s)

704-9

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cites work

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

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Synthesis and antitumor activity of an inhibitor of fatty acid synthase

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Increased fatty acid synthase as a therapeutic target in androgen-independent prostate cancer progression

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Fatty acid synthase inhibitors are chemopreventive for mammary cancer in neu-N transgenic mice

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Orlistat is a novel inhibitor of fatty acid synthase with antitumor activity

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Inhibition of fatty acid synthase induces endoplasmic reticulum stress in tumor cells.

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Effect of modification of the length and flexibility of the acyl carrier protein-thioesterase interdomain linker on functionality of the animal fatty acid synthase

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Human fatty acid synthase: structure and substrate selectivity of the thioesterase domain

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Identification of the active-site serine in human pancreatic lipase by chemical modification with tetrahydrolipstatin

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Total synthesis and comparative analysis of orlistat, valilactone, and a transposed orlistat derivative: Inhibitors of fatty acid synthase

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Inhibition of endothelial cell proliferation and angiogenesis by orlistat, a fatty acid synthase inhibitor

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Experimental verification of conformational variation of human fatty acid synthase as predicted by normal mode analysis

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31 March 2020

Architecture of mammalian fatty acid synthase at 4.5 A resolution

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Practical, catalytic, asymmetric synthesis of beta-lactones via a sequential ketene dimerization/hydrogenation process: inhibitors of the thioesterase domain of fatty acid synthase

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Crystallographic refinement of ligand complexes

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Identifiers

DOI

10.1038/NSMB1265

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Dimensions Publication ID

1019966432

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PubMed publication ID

17618296

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ResearchGate publication ID

6220240

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