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TranscriptomicsCoding sequence targeting by MicC RNA reveals bacterial mRNA silencing downstream of translational initiation
It is well established that small noncoding RNAs (sRNAs) of bacteria recognize the 5â?? regions of target mRNAs, generally at the ribosome binding site. Until now, the translated coding sequence (CDS) of mRNA appeared to be refractory to sRNA interactions. We have discovered that Salmonella MicC RNA...
ORGANISM(S): Salmonella enterica 
2010-05-16 | E-GEOD-16540 | biostudies-arrayexpress
ProteomicsPositional proteomics reveals differences in N-terminal proteoform stability.
To understand the impact of alternative translation initiation on a proteome, we performed the first large-scale study of protein turnover rates in which we distinguish between N-terminal proteoforms pointing to translation initiation events. Using pulsed SILAC combined with N-terminal COFRADIC we m...
ORGANISM(S): Homo Sapiens (ncbitaxon:9606) 
2019-03-13 | MSV000083565 | MassIVE
TranscriptomicsTranslation profiling of human lung fibroblasts treated or not with rapamycin to better understand the molecular mechanism behind alternative translational routes
Deregulation of translational control is frequently implicated in the establishment and maintenance of the cancer phenotype. Anti-cancer drugs targeting protein synthesis are confronted by the problem that genes can exploit alternative translational mechanisms. To better understand the molecular mec...
ORGANISM(S): Homo sapiens 
2008-01-16 | E-TABM-205 | biostudies-arrayexpress
TranscriptomicsRNA 5'end sequencing in polysome profiling fractions
It has been shown that in mammalian cells alternative transcription initiation is extensively regulated during development and across cell-types, which confers dynamic transcript 5’UTR repertoire. However it is underexplored how the heterogeneity of 5’UTR isoforms would affect the downstream ste...
ORGANISM(S): Mus musculus 
2016-07-20 | E-GEOD-78241 | biostudies-arrayexpress
ProteomicsN-terminome profiling in HEK293T
Various forms of the protein, called proteoform, are generated by co- or post-translational modification, alternative splicing and alternative translation initiation site, resulting in interactions between ribosomes, mRNAs, tRNAs, and various enzymes. Here, we introduce a N-terminal peptide enrichme...
ORGANISM(S): Homo sapiens (Human) 
2017-08-17 | PXD005583 | Pride
Protein stability Alternative translational initiation site Acetylation N-terminome Positional proteomics Proteoform N-termini Fasp N-end rule Translational initiation site 
TranscriptomicsGenome-wide search for novel human uORFs and N-terminal protein extensions using ribosomal footprinting
So far, the annotation of translation initiation sites (TISs) has been based mostly upon bioinformatics rather than experimental evidence. We adapted ribosomal footprinting to puromycin-treated cells to generate a transcriptome-wide map of TISs in a human monocytic cell line. A neural network was tr...
ORGANISM(S): Homo sapiens 
2012-08-08 | E-GEOD-39561 | biostudies-arrayexpress
UnknownSynthesis of two SAPAP3 isoforms from a single mRNA is mediated via alternative translational initiation.
Not available
S-EPMC3387777 | biostudies-literature
TranscriptomicsRibosome profiling of HeLa cells infected with Enterovirus coxsackiepol (strain CVA-13/Flores)
Ribosome profiling of enterovirus infected cells was used to investigate expression of the virus polyprotein and upstream open reading frames. Samples were either pretreated with initiation inhibitor lactimidomycin (LTM) to cause ribosomes to accumulate at initiation sites, or were flash frozen with...
ORGANISM(S): Homo sapiens 
2025-11-26 | E-MTAB-14994 | biostudies-arrayexpress
UnknownAlternative translational initiation of ATP sulfurylase underlying dual localization of sulfate assimilation pathways in plastids and cytosol in Arabidopsis thaliana.
Not available
S-EPMC4283515 | biostudies-literature
UnknownA mutation creating an out-of-frame alternative translation initiation site in the GRHPR 5'UTR causing primary hyperoxaluria type II.
Not available
S-EPMC4437915 | biostudies-literature
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