|Human U1-70K ribonucleoprotein antigen gene: organization, nucleotide sequence, and mapping to locus 19q13.3.
|The human U1-70K snRNP protein: cDNA cloning, chromosomal localization, expression, alternative splicing and RNA-binding.
|A common RNA recognition motif identified within a defined U1 RNA binding domain of the 70K U1 snRNP protein.
|Cloning of the human cDNA for the U1 RNA-associated 70K protein.
|Identification of an snRNP-associated kinase activity that phosphorylates arginine/serine rich domains typical of splicing factors.
|Identification of an inhibitory element within the human 68-kDa (U1) ribonucleoprotein antigen.
|Sip1, a novel RS domain-containing protein essential for pre-mRNA splicing.
|A coactivator of pre-mRNA splicing.
|The SRm160/300 splicing coactivator is required for exon-enhancer function.
|ZNF265 -- a novel spliceosomal protein able to induce alternative splicing.
|Nuclear relocalization of the pre-mRNA splicing factor PSF during apoptosis involves hyperphosphorylation, masking of antigenic epitopes, and changes in protein interactions.
|Association of polyadenylation cleavage factor I with U1 snRNP.
|Complete sequencing and characterization of 21,243 full-length human cDNAs.
|Dephosphorylated SRp38 acts as a splicing repressor in response to heat shock.
|Robust phosphoproteomic profiling of tyrosine phosphorylation sites from human T cells using immobilized metal affinity chromatography and tandem mass spectrometry.
|The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).
|A probability-based approach for high-throughput protein phosphorylation analysis and site localization.
|Global, in vivo, and site-specific phosphorylation dynamics in signaling networks.
|Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra.
|The full-ORF clone resource of the German cDNA consortium.
|A quantitative atlas of mitotic phosphorylation.
|Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle.
|Crystal structure of human spliceosomal U1 snRNP at 5.5 A resolution.
|Large-scale proteomics analysis of the human kinome.
|Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach.
|Lysine acetylation targets protein complexes and co-regulates major cellular functions.
|Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions.
|Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis.
|Initial characterization of the human central proteome.
|System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation.
|Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features.
|Toward a comprehensive characterization of a human cancer cell phosphoproteome.
|An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome.
|Gemin5 binds to the survival motor neuron mRNA to regulate SMN expression.
|Site-specific mapping of the human SUMO proteome reveals co-modification with phosphorylation.