Sequence of a cDNA encoding human ribosomal protein L26 and of a cDNA probably encoding human ribosomal protein L6.Zaman G.J.R.Cited forNUCLEOTIDE SEQUENCE [MRNA]CategoriesSequencesSourceUniProtKB reviewed (Swiss-Prot)PubMedEurope PMCNucleic Acids Res. 21:1673-1673 (1993)Cited in2
Characterization of the human homologue to rat ribosomal protein L26 from HL60 cells.Butterfield L.H., Stephen K., Snyder C., Winston S.Cited forNUCLEOTIDE SEQUENCE [GENOMIC DNA]CategoriesSequencesSourceUniProtKB reviewed (Swiss-Prot)Submission Submitted to EMBL/GenBank/DDBJ databases (APR-1993)Cited in1
The human ribosomal protein genes: sequencing and comparative analysis of 73 genes.Yoshihama M., Uechi T., Asakawa S., Kawasaki K., Kato S., Higa S., Maeda N., Minoshima S., Tanaka T.[...], Kenmochi N.View abstractCited forNUCLEOTIDE SEQUENCE [GENOMIC DNA]CategoriesSequencesSourceUniProtKB reviewed (Swiss-Prot)PubMedEurope PMCGenome Res. 12:379-390 (2002)Cited in313
Complete sequencing and characterization of 21,243 full-length human cDNAs.Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H.[...], Sugano S.View abstractCited forNUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]TissueTestisCategoriesSequencesSourceUniProtKB reviewed (Swiss-Prot)PubMedEurope PMCNat. Genet. 36:40-45 (2004)Cited in99+99+
No title available.Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H.[...], Venter J.C.Cited forNUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]CategoriesSequencesSourceUniProtKB reviewed (Swiss-Prot)Submission Submitted to EMBL/GenBank/DDBJ databases (SEP-2005)Cited in99+
The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).The MGC Project TeamView abstractCited forNUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]TissueColonCategoriesSequencesSourceUniProtKB reviewed (Swiss-Prot)PubMedEurope PMCGenome Res. 14:2121-2127 (2004)Cited in99+99+
A quantitative atlas of mitotic phosphorylation.Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.View abstractCited forPHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-139, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]TissueCervix carcinomaCategoriesPTM / Processing, SequencesSourceUniProtKB reviewed (Swiss-Prot)PubMedEurope PMCProc. Natl. Acad. Sci. U.S.A. 105:10762-10767 (2008)Cited in99+99+
Initial characterization of the human central proteome.Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.View abstractCited forIDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]CategoriesSequencesSourceUniProtKB reviewed (Swiss-Prot)PubMedEurope PMCBMC Syst. Biol. 5:17-17 (2011)Cited in99+99+
Frameshift mutation in p53 regulator RPL26 is associated with multiple physical abnormalities and a specific pre-ribosomal RNA processing defect in diamond-blackfan anemia.Gazda H.T., Preti M., Sheen M.R., O'Donohue M.F., Vlachos A., Davies S.M., Kattamis A., Doherty L., Landowski M.[...], Beggs A.H.View abstractCited forINVOLVEMENT IN DBA11CategoriesDisease & VariantsSourceUniProtKB reviewed (Swiss-Prot)PubMedEurope PMCHum. Mutat. 33:1037-1044 (2012)Cited in3Mapped to1
A new system for naming ribosomal proteins.Ban N., Beckmann R., Cate J.H.D., Dinman J.D., Dragon F., Ellis S.R., Lafontaine D.L.J., Lindahl L., Liljas A.[...], Yusupov M.View abstractCited forNOMENCLATURECategoriesNamesSourceUniProtKB reviewed (Swiss-Prot)PubMedEurope PMCCurr. Opin. Struct. Biol. 24:165-169 (2014)Cited in99+
Uncovering global SUMOylation signaling networks in a site-specific manner.Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M., Vertegaal A.C.View abstractCited forSUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-136, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]CategoriesPTM / Processing, SequencesSourceUniProtKB reviewed (Swiss-Prot)PubMedEurope PMCNat. Struct. Mol. Biol. 21:927-936 (2014)Cited in99+99+Mapped to47
SUMO-2 orchestrates chromatin modifiers in response to DNA damage.Hendriks I.A., Treffers L.W., Verlaan-de Vries M., Olsen J.V., Vertegaal A.C.View abstractCited forSUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-136, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]CategoriesPTM / Processing, SequencesSourceUniProtKB reviewed (Swiss-Prot)PubMedEurope PMCCell Rep. 10:1778-1791 (2015)Cited in99+99+
The DHX33 RNA Helicase Promotes mRNA Translation Initiation.Zhang Y., You J., Wang X., Weber J.View abstractCited forINTERACTION WITH DHX33CategoriesInteractionSourceUniProtKB reviewed (Swiss-Prot)PubMedEurope PMCMol. Cell. Biol. 35:2918-2931 (2015)Cited in15Mapped to7
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.Xiao Z., Chang J.G., Hendriks I.A., Sigurdsson J.O., Olsen J.V., Vertegaal A.C.View abstractCited forSUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-136, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]CategoriesPTM / Processing, SequencesSourceUniProtKB reviewed (Swiss-Prot)PubMedEurope PMCMol. Cell. Proteomics 14:1419-1434 (2015)Cited in99+99+
Site-specific mapping of the human SUMO proteome reveals co-modification with phosphorylation.Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C., Nielsen M.L.View abstractCited forSUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-136, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]CategoriesPTM / Processing, SequencesSourceUniProtKB reviewed (Swiss-Prot)PubMedEurope PMCNat. Struct. Mol. Biol. 24:325-336 (2017)Cited in99+99+
A genome-wide ER-phagy screen highlights key roles of mitochondrial metabolism and ER-Resident UFMylation.Liang J.R., Lingeman E., Luong T., Ahmed S., Muhar M., Nguyen T., Olzmann J.A., Corn J.E.View abstractCited forUFMYLATIONSourceUniProtKB reviewed (Swiss-Prot)PubMedEurope PMCCell 180:1160-1177 (2020)Cited in8
Structures of the human and Drosophila 80S ribosome.Anger A.M., Armache J.P., Berninghausen O., Habeck M., Subklewe M., Wilson D.N., Beckmann R.View abstractCited forSTRUCTURE BY ELECTRON MICROSCOPY (5.0 ANGSTROMS), FUNCTION, SUBUNIT, SUBCELLULAR LOCATIONCategoriesFunction, Interaction, Structure, Subcellular LocationSourceUniProtKB reviewed (Swiss-Prot)PubMedEurope PMCNature 497:80-85 (2013)Cited in99+17Mapped to67
Structural snapshots of human pre-60S ribosomal particles before and after nuclear export.Liang X., Zuo M.Q., Zhang Y., Li N., Ma C., Dong M.Q., Gao N.View abstractCited forSTRUCTURE BY ELECTRON MICROSCOPY (3.09 ANGSTROMS), FUNCTION, SUBUNITCategoriesFunction, Interaction, StructureSourceUniProtKB reviewed (Swiss-Prot)PubMedEurope PMCNat. Commun. 11:3542-3542 (2020)Cited in51Mapped to2
Molecular cloning of a novel member of the eukaryotic polypeptide chain- releasing factors (eRF). Its identification as eRF3 interacting with eRF1.Hoshino S., Imai M., Mizutani M., Kikuchi Y., Hanaoka F., Ui M., Katada T.View abstractAnnotationPathwayCategoriesFunctionSourceReactome: R-HSA-72436PubMedEurope PMCJ. Biol. Chem. 273:22254-22259 (1998)Cited in2Mapped to97
The role of assembly in insulin's biosynthesis.Dodson G., Steiner D.View abstractAnnotationPathwayCategoriesFunctionSourceReactome: R-HSA-72436PubMedEurope PMCCurr Opin Struct Biol 8:189-194 (1998)Mapped to99+
Dimerization by translation initiation factor 2 kinase GCN2 is mediated by interactions in the C-terminal ribosome-binding region and the protein kinase domain.Qiu H., Garcia-Barrio M.T., Hinnebusch A.G.View abstractAnnotationPathwayCategoriesFunctionSourceReactome: R-HSA-72436PubMedEurope PMCMol. Cell. Biol. 18:2697-2711 (1998)Cited in1Mapped to91
Autophosphorylation in the activation loop is required for full kinase activity in vivo of human and yeast eukaryotic initiation factor 2alpha kinases PKR and GCN2.Romano P.R., Garcia-Barrio M.T., Zhang X., Wang Q., Taylor D.R., Zhang F., Herring C., Mathews M.B., Qin J., Hinnebusch A.G.View abstractAnnotationPathwayCategoriesFunctionSourceReactome: R-HSA-72436PubMedEurope PMCMol. Cell. Biol. 18:2282-2297 (1998)Cited in1Mapped to91
GCN1, a translational activator of GCN4 in Saccharomyces cerevisiae, is required for phosphorylation of eukaryotic translation initiation factor 2 by protein kinase GCN2.Marton M.J., Crouch D., Hinnebusch A.G.View abstractAnnotationPathwayCategoriesFunctionSourceReactome: R-HSA-72436PubMedEurope PMCMol. Cell. Biol. 13:3541-3556 (1993)Cited in1Mapped to94
Evolutionary conservation of components of the protein translocation complex.Hartmann E., Sommer T., Prehn S., Goerlich D., Jentsch S., Rapoport T.A.View abstractAnnotationPathwayCategoriesFunctionSourceReactome: R-HSA-72436PubMedEurope PMCNature 367:654-657 (1994)Cited in4Mapped to99+
A highly conserved eukaryotic protein family possessing properties of polypeptide chain release factor.Frolova L., Le Goff X., Rasmussen H.H., Cheprergin S., Drugeon G., Haenni A.-L., Celis J.E., Philippe M., Justesen J., Kisselev L.View abstractAnnotationPathwayCategoriesFunctionSourceReactome: R-HSA-72436PubMedEurope PMCNature 372:701-703 (1994)Cited in22Mapped to90