|Characterization and primary structure of the poly(C)-binding heterogeneous nuclear ribonucleoprotein complex K protein.
|Identification, molecular cloning, expression and chromosome mapping of a family of transformation upregulated hnRNP-K proteins derived by alternative splicing.
|Hepatitis C virus core protein interacts with heterogeneous nuclear ribonucleoprotein K.
|High precision solution structure of the C-terminal KH domain of heterogeneous nuclear ribonucleoprotein K, a c-myc transcription factor.
|Cluster analysis of an extensive human breast cancer cell line protein expression map database.
|Purification and characterization of native spliceosomes suitable for three-dimensional structural analysis.
|Molecular basis of sequence-specific single-stranded DNA recognition by KH domains: solution structure of a complex between hnRNP K KH3 and single-stranded DNA.
|An RNA helicase, DDX1, interacting with poly(A) RNA and heterogeneous nuclear ribonucleoprotein K.
|Complete sequencing and characterization of 21,243 full-length human cDNAs.
|DNA sequence and analysis of human chromosome 9.
|The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).
|hnRNP K: an HDM2 target and transcriptional coactivator of p53 in response to DNA damage.
|PITK, a PP1 targeting subunit that modulates the phosphorylation of the transcriptional regulator hnRNP K.
|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.
|A quantitative atlas of mitotic phosphorylation.
|Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle.
|African swine fever virus protein p30 interaction with heterogeneous nuclear ribonucleoprotein K (hnRNP-K) during infection.
|Human protein factory for converting the transcriptome into an in vitro-expressed proteome.
|Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach.
|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.
|A large intergenic noncoding RNA induced by p53 mediates global gene repression in the p53 response.
|Initial characterization of the human central proteome.
|System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation.
|Proteomic analysis of podosome fractions from macrophages reveals similarities to spreading initiation centres.
|N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB.
|DNA damage-induced heterogeneous nuclear ribonucleoprotein K SUMOylation regulates p53 transcriptional activation.
|Characterization of O-GlcNAc cycling and proteomic identification of differentially O-GlcNAcylated proteins during G1/S transition.
|Toward a comprehensive characterization of a human cancer cell phosphoproteome.
|Immunoaffinity enrichment and mass spectrometry analysis of protein methylation.
|An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome.
|Mapping of SUMO sites and analysis of SUMOylation changes induced by external stimuli.
|Uncovering global SUMOylation signaling networks in a site-specific manner.
|System-wide analysis of SUMOylation dynamics in response to replication stress reveals novel small ubiquitin-like modified target proteins and acceptor lysines relevant for genome stability.
|N-terminome analysis of the human mitochondrial proteome.
|GeneMatcher aids in the identification of a new malformation syndrome with intellectual disability, unique facial dysmorphisms, and skeletal and connective tissue abnormalities caused by de novo variants in HNRNPK.
|Site-specific mapping of the human SUMO proteome reveals co-modification with phosphorylation.