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ProteomicsIdentification of substrates of LarA-activated Lon protease and Identification of Lon protease interactome
With this analysis we aim to identify proteins that are substrates of LarA-activated Lon protease in Caulobacter crescentus. We will compare samples of wild type cells either harboring an empty vector (vector control, VC) or overexpressing 3xFLAG-tagged LarA (F-LarA). Based on our previous data we h...
ORGANISM(S): Caulobacter crescentus (strain NA1000 / CB15N) 
2023-10-25 | PXD036514 | Pride
Caulobacter crescentus Lon activity regulator Lara Lon protease 
UnknownThe heat shock protein LarA activates the Lon protease in response to proteotoxic stress.
Not available
S-EPMC10665427 | biostudies-literature
UnknownStructural Basis for Catalysis and Substrate Specificity of a LarA Racemase with a Broad Substrate Spectrum.
Not available
S-EPMC11623692 | biostudies-literature
UnknownStructural Basis for the Catalysis and Substrate Specificity of a LarA Racemase with a Broad Substrate Spectrum.
Not available
S-EPMC11851776 | biostudies-literature
UnknownStructural basis for the allosteric activation of Lon by the heat shock protein LarA.
Not available
S-EPMC11882793 | biostudies-literature
TranscriptomicsMemory CD4+ T cell subsets show differential responses to HIV latency reversing agents [LARA]
HIV-1 persists in individuals on ART in infected central (CM), transitional (TM) and effector memory (EM) CD4+ T cells. We developed LARA (latency and reversion assay), which facilitates the examination of HIV latency reversal in CM, TM and EM subsets in a single assay. Studies with latency reversin...
ORGANISM(S): Homo sapiens 
2018-01-26 | GSE94149 | GEO
UnknownLaRA 2: parallel and vectorized program for sequence-structure alignment of RNA sequences.
Not available
S-EPMC8734264 | biostudies-literature
UnknownLasso Peptide Biosynthetic Protein LarB1 Binds Both Leader and Core Peptide Regions of the Precursor Protein LarA.
Not available
S-EPMC5084080 | biostudies-literature
UnknownStructures of two LarA-like nickel-pincer nucleotide cofactor-utilizing enzymes with a single catalytic histidine residue.
Not available
S-EPMC12393405 | biostudies-literature
UnknownStructures of two LarA-like nickel-pincer nucleotide cofactor-utilizing enzymes with a single catalytic histidine residue.
Not available
S-EPMC12611868 | biostudies-literature
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