Acyl-chain length

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N-Acetylneuraminic acid (3)
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Lab affiliation

Biomolecular characterization unit, Center for Sustainable Resource Science, RIKEN (1)
Department Biomolecular Sciences and the Joseph Meyerhoff Professor of Biochemistry at the Weizmann Institute of Science, Rehovot 76100, Israel (1)
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Department of Pediatric Hematology and Oncology, National Center for Tumor Diseases (NCT/UCC) Dresden (1)
Institute of Microbiology of the CAS, v. v. i. (1)
Instituto de Tecnologia Química e Biológica António Xavier, Universidade Nova de Lisboa - ITQB NOVA (1)
Laboratory of Chemical Biology and Microbial Pathogenesis, The Rockefeller University, New York, NY 10065, USA (1)
Lehrstuhl für Ernährungsphysiologie, Technische Universität München (TUM), Gregor-Mendel-Str. 2, 85354 Freising, Germany; Phone: +498161-71-2385 (1)
Medizinisches Proteom-Center, Medical Faculty, Ruhr-University Bochum, Bochum, Germany, Medical Proteome Analysis, Center for Proteindiagnostics (PRODI), Ruhr-University Bochum, Bochum, Germany (1)
Plateforme Proteome, Univ. Bordeaux, Bordeaux, France (1)
Professor of Chemical Physiology and Biochemistry, School of Medicine at OHSU Chair, Chemical Physiology and Biochemistry, School of Medicine Helen Jo Whitsell Dean's Leadership Professor Graduate Program in Biomedical Sciences, School of Medicine (1)
Proteome Research (AG Stühler) Institute of Molecular Medicine Heinrich Heine University Düsseldorf 40225 Düsseldorf Germany (1)
State Key Laboratory of Oral Diseases & National Clinical Research Center for Oral Diseases, West China Hospital of Stomatology, Sichuan University, Chengdu, China (1)
UNC Chapel Hill Nutrition Department (1)
de Duve Institute UCLouvain and WELBIO (1)

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Selection of the length of fatty acyl chain and of the acylation site by the acyltransferase governs activation of RTX toxins

Numerous proteins synthesized in cells ranging from bacteria to humans have to be posttranslationally acylated to become biologically active. Bacterial Repeats in ToXin (RTX) cytolysins form a prominent group of proteins that are synthesized as inactive protoxins and undergo a posttranslational acyl...

ORGANISM(S): Escherichia coli Bordetella pertussis (strain Tohama I / ATCC BAA-589 / NCTC 13251)

2020-05-20 | PXD018859 | Pride

Label-free proteomics of immuno-purified SYP61-trans-Golgi Network compartment in control condition and upon sphingolipid acyl-chain length reduction by metazachlor.

The trans-Golgi Network (TGN) in plants is a main sorting hub for proteins and lipids. The lipid composition at the TGN is instrumental to the polar sorting of the auxin efflux carrier PIN2 from TGN to the apical membrane. Here, we immuno-purified the full and intact TGN using the TGN-resident synta...

ORGANISM(S): Arabidopsis thaliana (Mouse-ear cress)

2021-12-01 | PXD026252 | Pride

Arabidopsis thaliana Sphingolipid Acyl-chain length Free proteomics Immuno-purification Metazachlor Trans-golgi network

Conformational Changes of Acyl Carrier Protein Switch the Chain Length Preference of Acyl-ACP Thioesterase ChFatB2.

Not available

S-EPMC10095102 | biostudies-literature

Endocytic trafficking of sphingomyelin depends on its acyl chain length.

Not available

S-EPMC2096594 | biostudies-literature

Acyl chain length of phosphatidylserine is correlated with plant lifespan.

Not available

S-EPMC4110022 | biostudies-literature