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MetabolomicsInsights into the stereochemical mechanism of the B12-dependent radical SAM glutamine C- methyltransferases QCMT
Methyl-coenzyme M reductase (MCR) is a crucial enzyme for methanogenesis and harbors several unusual post-translational modifications. Recent studies have identified glutamine C-methyltransferase (QCMT), as a B12-dependent radical SAM enzyme responsible for methylating a glutamine residue within the...
2026-04-28 | MTBLS14287 | MetaboLights
TranscriptomicsAtypical DNA methylation of genes encoding cysteine-rich peptides in Arabidopsis thaliana
In plants, transposons and non-protein-coding repeats are epigenetically silenced by CG and non-CG methylation. This pattern of methylation is mediated in part by small RNAs and two specialized RNA polymerases, Pol IV and Pol V, in a process called RNA-directed DNA methylation. By contrast, many pr...
ORGANISM(S): Arabidopsis thaliana 
2012-11-22 | E-GEOD-34207 | biostudies-arrayexpress
TranscriptomicsEffect of phenylalanine-rich peptide on growth and survival of Mycobacterium tuberculosis H37Rv (Mtb)
During our efforts to isolate potantial binding partners of Esat6, we isolated few peptides rich in phenylalanine residues that strongly interacted with Esat6. All peptides were less than fifty amino acids in length, One of them, Hcl1, when expressed in mycobacteria showed significant retardation in...
ORGANISM(S): Mycobacterium tuberculosis 
2009-11-10 | E-GEOD-16618 | biostudies-arrayexpress
TranscriptomicsThe IDA-LIKE peptides IDL6 and IDL7 are negative modulators of stress responses in Arabidopsis thaliana
We present a functional characterisation of two members of the IDA-LIKE (IDL) peptide family in Arabidopsis thaliana, IDL6 and IDL7. They are processed both C- and N-terminally to produce active peptides. Structure analyses of synthesized IDL6 and IDL7 peptides indicate that they lack secondary stru...
ORGANISM(S): Arabidopsis thaliana 
2016-03-31 | E-GEOD-77467 | biostudies-arrayexpress
TranscriptomicsMOTS-c: A Novel Peptide Encoded by a Short Mitochondrial Open Reading Frame Regulates Metabolic Homeostasis
Mitochondria are known to be functional organelles, but their role as a signaling unit is increasingly being appreciated. The recent identification of a short open reading frame (sORF) in the mitochondrial DNA (mtDNA) that encodes a signaling peptide, humanin, suggests the possible existence of addi...
ORGANISM(S): Homo sapiens 
2015-03-07 | E-GEOD-65068 | biostudies-arrayexpress
TranscriptomicsTranscription profiling of human osteoblasts differentiated from human mesenchymal stem cells and treated with three bioactive peptides
Effects of bioactive peptides IPP(Ile-Pro-Pro), VPP (Val-Pro-Pro), and LKP(Leu-Lys-Pro) on gene expression of osteoblast differentiated from human mesenchymal stem cells. Experimental design types: compound treatment and augmented reference design.
ORGANISM(S): Homo sapiens 
2008-01-23 | E-MEXP-885 | biostudies-arrayexpress
TranscriptomicsTranscription profiling of human CD4+ T cells induced by HIV-1 gp120/V3 loop peptides, time series
Comparative changes of gene expression in human primary CD4+ T cells induced by HIV-1 gp120/V3 loop synthetic peptides, during antigen presentation
ORGANISM(S): Homo sapiens 
2008-09-01 | E-MEXP-1586 | biostudies-arrayexpress
ProteomicsDeMix:efficient identification of co-fragmented peptides
A data analysis workflow with a simple deconvolution method based on high resolution data-dependent tandem mass spectrometry.
ORGANISM(S): Homo Sapiens (ncbitaxon:9606) 
2017-03-28 | MSV000080702 | MassIVE
ProteomicsXilmass: a new approach towards the identification of cross-linked peptides
Chemical cross-linking coupled with mass spectrometry plays an important role in unravelling protein interactions, especially weak and transient interactions. Moreover, cross-linking complements several structure determination approaches such as cryo-EM. Although several computational approaches are...
ORGANISM(S): Homo Sapiens (ncbitaxon:9606) 
2017-03-29 | MSV000080758 | MassIVE
ProteomicsIn-source CID improves HCD-dependent fragmentation of ADP-ribosyl peptides
ADP-ribosylation is a posttranslational modification whose HCD products are dominated by complete or partial modification losses, complicating peptide sequencing and acceptor site localization efforts. We tested whether in-source CID performed on a quadrupole Orbitrap could convert ADPr to the small...
ORGANISM(S): Homo sapiens (Human) 
2024-12-05 | PXD055586 | Pride
Sid Proteomics Hcd Exploris480 Adp-ribosylation 
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