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ProteomicsStructural basis of the interaction between SETD2 methyltransferase and hnRNP L paralogs for governing co-transcriptional 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) 
2021-05-11 | MSV000087403 | MassIVE
ProteomicsMudPIT analysis of HSV-1 infected and mock-infected microsomal membranes and nuclear envelopes
Nuclear envelopes (NEs) and microsomal membranes (MMs) were isolated from HeLa cells infected or not with HSV-1 using well-established procedures as described in: Wilkie GS, et al. (2011) Mol Cell Proteomics 10: M110 003129. Korfali N, et al. (2010) Mol Cell Proteomics 9: 2571-2585. Florens L, Korf...
ORGANISM(S): Homo Sapiens (ncbitaxon:9606) Herpes Simplex Virus (type 1 / Strain 17) (ncbitaxon:10299) 
2016-07-05 | MSV000079886 | MassIVE
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 
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 | PXD019538 | Pride
Hnrnp Chromatin Complex Mediator Domain 
ProteomicsMudPIT analysis of HIV-1 Vpr-asssociated proteins from the permissive CEM.SS human T4-lymphoblastoid cell line
CEM.SS-iH1.Vpr cells expressing a tandem HA-FLAG- epitope-tagged HIV-1 NL4-3 Vpr (hfa-H.Vpr) under control of the Lenti-X Tet-On 3G Inducible Expression System (Clontech), and control CEM.SS cells (3x105 cells/ml, 4 liters), were induced with doxycycline (0.1ug/ml) for 9 hours. Whole cell extracts w...
ORGANISM(S): Hiv-1 Vector Pnl4-3 (ncbitaxon:151458) Homo Sapiens (ncbitaxon:9606) 
2016-03-24 | MSV000079605 | MassIVE
UnknownStructural basis of the interaction between SETD2 methyltransferase and hnRNP L paralogs for governing co-transcriptional splicing.
Not available
S-EPMC8575775 | biostudies-literature
Proteomics,MultiomicsMudPIT analyses of the proteins co-purified with Halo-tagged Human HNRNP proteins from HEK293T cells with and without RNAse
Plasmids encoding full-length open-reading frames (ORF) of heterogeneous nuclear ribonucleoproteins fused to a HaloTag (HT) were transfected in human HEK293T cells in biological duplicates. The expressed proteins were: HNRNPA0 (NM_006805; NP_006796.1), HNRNPA1 (NM_002136; NP_002127.1), HNRNPD (NM_00...
ORGANISM(S): Homo Sapiens (ncbitaxon:9606) 
2016-04-18 | MSV000079669 | MassIVE
ProteomicsLC/MS Analysis of Myc-Affinity Captured, on-Beads Crosslinked, and on-Beads Digested S. cerevisiae SCC2 subunit of cohesin loading factor
Myc-Affinity Capture and on-Beads Crosslinking For each Saccharomyces cerevisiae strain (C-terminally myc-tagged Scc2 subunit of the cohesin loading factor complex or wild-type BY4741), 2x 3 L YPD medium (add 300 ml 20% Glucose to each 3 L of YPD before using) were separately inoculated in a 5L flas...
ORGANISM(S): Saccharomyces Cerevisiae (ncbitaxon:4932) 
2020-10-20 | MSV000086339 | MassIVE
ProteomicsMudPIT analyses of the proteins co-purified with Ada2b-PB-FLAG-HA FLAG-affinity purified from Drosophila melanogaster S2 cells
Protein Complexes Purification- Stable S2 cell lines expressing Ada2b (isoform B; NP_001027151.1) in the pRmHa3-CHA2FL2 (Ada2b-PBH2F2) were maintained at 1-2 e6 cells/mL in SFX medium (HyQ SFX-Insect). Cells stably transfected with empty vector served as negative controls. Protein complexes containi...
ORGANISM(S): Drosophila Melanogaster (ncbitaxon:7227) 
2018-11-20 | MSV000083153 | MassIVE
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