Sort   by:  
 Page size 
ProteomicsThe stoichiometry of the outer kinetochore responds to microtubule-proximal regulation
The authors of this manuscript suggest the stoichiometry of outer submodules of the budding yeast kinetochore is strongly influenced by factors at the kinetochore-microtubule interface, including Fin1, Dam1, and microtubule tracking. Outer kinetochore stoichiometry is remarkably plastic and responsi...
ORGANISM(S): Saccharomyces cerevisiae (Baker's yeast) 
2020-01-16 | PXD011384 | Pride
Kinetochore Anaphase Mudpit 
ProteomicsThe histone methyltransferase SETD2 couples transcription and splicing by engaging pre-mRNA processing factors through its SHI domain
The domains of SETD2, a known histone methyltransferase were investigated for specific interaction partners and function using a number of biochemical assays and affinity purification mass spectrometry. The C-terminal domain, named SETD2C, was identified to interact with hnRNP-L through a previousl...
ORGANISM(S): Homo sapiens (Human) 
2021-02-01 | PXD019538 | Pride
Hnrnp Chromatin Complex Mediator Domain 
ProteomicsThermococcus kodakarensis proteins expressed at various temperatures reveals changes in RNA modifications
Thermococcus kodakarensis is a thermophilic archaea used in this study to determine how changes in growth temperature affect protein expression. This organism was chosen, in part, due to the simplified proteome and potential protein stability gained when analyzing proteins at room temperature. Two t...
ORGANISM(S): Thermococcus kodakarensis KOD1 
2020-02-17 | PXD014814 | Pride
Proteomics Thermococcus kodakarensis Theromphile Qexactive plus 
ProteomicsThe histone methyltransferase SETD2 couples transcription and splicing by engaging pre-mRNA processing factors through its SHI domain
The domains of SETD2, a known histone methyltransferase were investigated for specific interaction partners and function using a number of biochemical assays and affinity purification mass spectrometry. The C-terminal domain, named SETD2C, was identified to interact with hnRNP-L through a previousl...
ORGANISM(S): Homo sapiens (Human) 
2021-02-01 | PXD019376 | Pride
Hnrnp Chromatin Complex Mediator Domain 
ProteomicsThe histone methyltransferase SETD2 couples transcription and splicing by engaging pre-mRNA processing factors through its SHI domain
The domains of SETD2, a known histone methyltransferase were investigated for specific interaction partners and function using a number of biochemical assays and affinity purification mass spectrometry. The C-terminal domain, named SETD2C, was identified to interact with hnRNP-L through a previousl...
ORGANISM(S): Homo sapiens (Human) 
2021-02-01 | PXD022946 | Pride
Hnrnp Chromatin Complex Mediator Domain 
ProteomicsHarnessing Ionic Selectivity In Acetyltransferase Chemoproteomic Probes
Chemical proteomics (chemoproteomics) has emerged as a powerful strategy for the high-throughput annotation of protein function. This approach involves using an active site probe to capture an enzyme class of interest from cells, allowing the biological activity of multiple enzymes within that famil...
ORGANISM(S): Homo sapiens (Human) 
2021-08-19 | PXD020856 | Pride
Affinity capture Tmt Acetyltransferase 
ProteomicsProbing the Sensitivity of the Lumos Mass Spectrometer by analyzing varying amounts of whole cell extracts
PROJECT DESCRIPTION The Orbitrap Fusion Lumos mass spectrometer has recently been shown to have better fragmentation and detection than its predecessors. Previous studies using a HeLa digest analyzed on the Lumos mass spectrometer have reported the number of peptides and proteins identified by rever...
ORGANISM(S): Saccharomyces Cerevisiae (ncbitaxon:4932) 
2018-04-19 | MSV000082296 | MassIVE
ProteomicsLC/MS/MS Analyses of enriched ECM-enriched preparations from planaria
ECM isolation - Whole-mount planarian decellularization has been optimized based on a previous publication (Sonpho et al. 2020). We optimized three protocols for decellularization, which we refer to as No Pretreatment ECM (NP-ECM), Formaldehyde ECM (FA-ECM), and N-Acetyl Cysteine pretreatment (NAC-E...
ORGANISM(S): Schmidtea Mediterranea (ncbitaxon:79327) 
2021-03-15 | MSV000087054 | MassIVE
ProteomicsMudPIT analyses of the proteins associated with Human SETD2 deletion mutants
N-terminally Halo-tagged deletions of human SETD2 were constructed such as SETD2 ABCN1, A, B, C, CN, and CC consisted of amino acids 1-1692, 1-503, 504-1403, 1404-2564, 1404-1963, and 1964-2564, respectively. Deletion mutants were expressed in HEK293T cells and affinity purified, each in biological ...
ORGANISM(S): Homo Sapiens (ncbitaxon:9606) 
2021-06-08 | MSV000087587 | MassIVE
ProteomicsThe nuclear granule Paraspeckles interacts with the chromatin remodeling SWI/SNF complex to regulate alternative splicing
Protein samples were analyzed by Multidimensional Protein Identification Technology (MudPIT), as described previously. Briefly, precipitated proteins were resuspended in 30uL of 100mM Tris pH 8.5 with 8M urea to denature proteins. Cysteines were reduced and alkylated prior to digestion with recombi...
ORGANISM(S): Homo Sapiens (ncbitaxon:9606) 
2022-04-04 | MSV000089198 | MassIVE
Sort   by:  
 Page size