Sort   by:  
 Page size 
ProteomicsLC-MS/MS analysis of KA-PARP1 targets in HeLa celly lysate
KA-PARP1 was expressed in HeLa-KO PARP1 cells. Protein targets of KA-PARP1 were determined in cell lysate by using a DTB-modified NAD+analog.
ORGANISM(S): Homo sapiens (Human) 
2024-05-02 | PXD046956 | Pride
Lc-ms/ms Parp1 
ProteomicsIdentification of ADP-ribosylation targets in living HeLa cells using cell-permeable NAD+ probes
Posttranslational modifications of proteins (PTMs) greatly enhance their functional diversity, surpassing the number of gene-encoded variations. One intriguing PTM is ADP-ribosylation, which utilizes nicotinamide adenine dinucleotide (NAD+) as a substrate and is essential in cell signaling pathways ...
ORGANISM(S): Homo sapiens (Human) 
2024-10-11 | PXD051967 | Pride
Affinity enrichment Hela cells Nad+ Cell-permeable probes Adp-ribosylation 
ProteomicsDiadenosine tetraphosphate as a cosubstrate for AMPylation mediated by FICD
Diadenosine polyphosphates (ApnAs) are noncanonical nucleotides that are ubiquitous across all forms of life. Due to their strong accumulation upon cellular stress, they are considered alarmones to signal homeostatic imbalance. Nonetheless, their cellular role is poorly understood. In this work, we ...
ORGANISM(S): Homo sapiens (Human) 
2023-01-27 | PXD036450 | Pride
Diadenosine tetraphosphate Ampylation Ficd Post-translational modification Proteomics 
ProteomicsChemoproteomic discovery of a human RNA ligase
RNA ligases are present across all forms of life. While enzymatic RNA ligation between 5'-PO4 and 3'-OH termini is prevalent in viruses, fungi, and plants, such RNA ligases are yet to be identified in vertebrates. Here, using a nucleotide-based chemical probe targeting human AMPylated proteome, we h...
ORGANISM(S): Homo sapiens (Human) 
2023-01-27 | PXD038132 | Pride
Rna ligation Ampylation Proteomics Post-translational modification 
ProteomicsThe tumor suppressor Fhit in complex with the alarmone Ap3A binds to the ribosome and impedes translation
Upon cellular stress, the concentration of the alarmone diadenosine triphosphate (Ap3A) increases and is thought to trigger downstream adaptive processes. The known Ap3A-hydrolase fragile histidine triad (Fhit) is known to form a complex with Ap3A. The molecular mechanism of Fhit-Ap3A signaling is h...
ORGANISM(S): Homo sapiens (Human) 
2022-12-20 | PXD029645 | Pride
Ap-ms Mass spectrometry Ribosome Xl-ms Fhit Ap3a Translation 
ProteomicsChemical proteomic profiling reveals protein interactors of the alarmones diadenosine triphosphate and tetraphosphate
The nucleotides diadenosine triphosphate (Ap3A) and diadenosine tetraphosphate (Ap4A) are formed in prokaryotic and eukaryotic cells. Since their concentrations increase significantly upon cellular stress, they are considered to be alarmones triggering stress adaptive processes. However, their cellu...
ORGANISM(S): Homo sapiens (Human) Escherichia coli 
2022-02-15 | PXD020740 | Pride
Photo-affinity labeling Proteomics Apna 
GenomicsEngineering of novel DNA polymerase variants for single enzyme quantitative multiplex Reverse Transcription-PCR
Engineering of novel DNA polymerase variants for single enzyme quantitative multiplex Reverse Transcription-PCR
PRJNA1176519 | ENA
ProteomicsProteomic Profiling of Potential E6AP Substrates via Ubiquitin-based Photo-Crosslinking Assisted Affinity Enrichment
E6AP/UBE3A, the founding member of HECT-type (Homologous to E6AP C-terminus) E3 ligases, is implicated in human papillomaviruses (HPV)-mediated cervical cancer and neurodevelopmental disorders like Angelman and Dup15q syndromes. To elucidate the function of E3 ligases, knowledge about their substrat...
ORGANISM(S): Homo sapiens (Human) 
2025-01-27 | PXD055649 | Pride
Photoaffinity labelling Proteomics Substrate identification Ubiquitination E6ap/ube3a 
UnknownRemote Ischemic Preconditioning Does Not Affect the Release of Humoral Factors in Propofol-Anesthetized Cardiac Surgery Patients: A Secondary Analysis of the RIPHeart Study.
Not available
S-EPMC5979505 | biostudies-literature
TranscriptomicsSensitivity-resistance to the atypical retinoid ST1926 in NB4 acute myeloid leukemia cells
The two cell lines NB4 and NB4.437r, respectively sensitive and resistant to the cytotoxic action of the atypical retinoid ST1926 and CD437 were used to unveil the mechanism of action of these drugs.We compared their transcriptional profiles in conditions of exponential growth in basal medium by mic...
ORGANISM(S): Homo sapiens 
2013-01-08 | E-MEXP-3752 | biostudies-arrayexpress
Sort   by:  
 Page size