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GenomicsRNA-based full length immunoglobulin light chain sequencing reveals lambda constant domain mutations with potential implications for thermodynamic stability in light chain amyloidosis
RNA-based full length immunoglobulin light chain sequencing
PRJEB109785 | ENA
ProteomicsThe length of a ubiquitin chain is a general determinant for selective recognition by ubiquitin-binding proteins.
The attachment of differently linked ubiquitin (Ub) chains of varying length to proteins is a prevalent posttranslational modification in eukaryotic cells. The fate of a modified protein is determined by Ub-binding proteins (UBPs) that interact with Ub chains in a linkage-selective manner. Therefore...
ORGANISM(S): Homo sapiens (Human) 
2020-04-20 | PXD015877 | Pride
Chain-length Ubiquitin Ub-binding proteins Posttranslational modification 
ProteomicsLabel-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 
ProteomicsSelection 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
Fatty acyl Rtx toxin Acyltransferase Acylation Cytotoxicity 
MetabolomicsSalmonella enterica and Pseudomonas syringe uniquely alter the exometabolomic profile of the Arabidopsis leaf surface
To successfully colonize healthy plants, bacterial pathogens must overcome stressful conditions on the leaf surface before entering the leaf tissues through natural openings. In this study, we developed an approach to examine the exometabolomic profiles of the leaf surface when exposing plants with ...
2025-06-17 | MTBLS9884 | MetaboLights
ProteomicsRNA-based full length immunoglobulin light chain sequencing reveals lambda constant domain mutations with potential implications for thermodynamic stability in light chain amyloidosis
Background: Systemic light chain amyloidosis is a protein misfolding disorder characterized by deposition of clonal immunoglobulin light chains in vital organs. To date, little is known about the contribution of light chain constant domain mutations in thermodynamic stability and amyloidogenicity.Me...
ORGANISM(S): Homo sapiens (Human) 
2026-05-06 | PXD077140 | Pride
TranscriptomicsComparative analysis of D. shibae wild-type vs. ∆luxI1 supplemented with acetylated homoserine-lactones with different length of the side chain and modifications
Comparison of a quorum sensing null mutant supplemented with AHLs with different length of the side chain and modifications with D. shibae wild-type in order to identify traits induced by distinct autoinducers in this organism.
ORGANISM(S): Dinoroseobacter shibae DFL 12 = DSM 16493 
2014-04-01 | GSE54420 | GEO
UnknownChain length-dependent luminescence in acceptor-doped conjugated polymers.
Not available
S-EPMC6677785 | biostudies-literature
UnknownFructose-Based Production of Short-Chain-Length and Medium-Chain-Length Polyhydroxyalkanoate Copolymer by Arctic Pseudomonas sp. B14-6.
Not available
S-EPMC8123457 | biostudies-literature
UnknownSystematic study of genes influencing cellular chain length in Streptococcus sanguinis.
Not available
S-EPMC3919539 | biostudies-literature
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