|PCM-1, A 228-kD centrosome autoantigen with a distinct cell cycle distribution.
|Huntingtin-associated protein 1 (HAP1) interacts with the p150Glued subunit of dynactin.
|RET/PCM-1: a novel fusion gene in papillary thyroid carcinoma.
|Assembly of centrosomal proteins and microtubule organization depends on PCM-1.
|Basal body dysfunction is a likely cause of pleiotropic Bardet-Biedl syndrome.
|Complete sequencing and characterization of 21,243 full-length human cDNAs.
|The Bardet-Biedl protein BBS4 targets cargo to the pericentriolar region and is required for microtubule anchoring and cell cycle progression.
|Robust phosphoproteomic profiling of tyrosine phosphorylation sites from human T cells using immobilized metal affinity chromatography and tandem mass spectrometry.
|Candidate tumor-suppressor genes on chromosome arm 8p in early-onset and high-grade breast cancers.
|The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).
|Dynamic recruitment of Nek2 kinase to the centrosome involves microtubules, PCM-1, and localized proteasomal degradation.
|The t(8;9)(p22;p24) is a recurrent abnormality in chronic and acute leukemia that fuses PCM1 to JAK2.
|PCM1-JAK2 fusion in myeloproliferative disorders and acute erythroid leukemia with t(8;9) translocation.
|The t(8;9)(p22;p24) translocation in atypical chronic myeloid leukaemia yields a new PCM1-JAK2 fusion gene.
|Five genes from chromosomal band 8p22 are significantly down-regulated in ovarian carcinoma: N33 and EFA6R have a potential impact on overall survival.
|Nudel contributes to microtubule anchoring at the mother centriole and is involved in both dynein-dependent and -independent centrosomal protein assembly.
|DNA sequence and analysis of human chromosome 8.
|A t(8;9) translocation with PCM1-JAK2 fusion in a patient with T-cell lymphoma.
|A combination of cytomorphology, cytogenetic analysis, fluorescence in situ hybridization and reverse transcriptase polymerase chain reaction for establishing clonality in cases of persisting hypereosinophilia.
|Inhibition of centrosome protein assembly leads to p53-dependent exit from the cell cycle.
|A probability-based approach for high-throughput protein phosphorylation analysis and site localization.
|Global, in vivo, and site-specific phosphorylation dynamics in signaling networks.
|A quantitative atlas of mitotic phosphorylation.
|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.
|Control of ciliogenesis by FOR20, a novel centrosome and pericentriolar satellite protein.
|Par6 alpha interacts with the dynactin subunit p150 Glued and is a critical regulator of centrosomal protein recruitment.
|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.
|Autophagy promotes primary ciliogenesis by removing OFD1 from centriolar satellites.
|A new cellular stress response that triggers centriolar satellite reorganization and ciliogenesis.
|An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome.
|Ccdc13 is a novel human centriolar satellite protein required for ciliogenesis and genome stability.
|Proteomic analysis of mammalian sperm cells identifies new components of the centrosome.
|N-terminome analysis of the human mitochondrial proteome.
|OFIP/KIAA0753 forms a complex with OFD1 and FOR20 at pericentriolar satellites and centrosomes and is mutated in one individual with oral-facial-digital syndrome.