about
YphC and YsxC GTPases assist the maturation of the central protuberance, GTPase associated region and functional core of the 50S ribosomal subunitSynergy of NMR, Computation, and X-Ray Crystallography for Structural BiologyStructure of the GLD-1 homodimerization domain: insights into STAR protein-mediated translational regulation.The Structure of Aquifex aeolicus Ribosomal Protein S8 Reveals a Unique Subdomain that Contributes to an Extremely Tight Association with 16S rRNAThe universal YrdC/Sua5 family is required for the formation of threonylcarbamoyladenosine in tRNA.Systematic chromosomal deletion of bacterial ribosomal protein genesIdentification of a conserved interface between PUF and CPEB proteinsCharacterization of the ribosome biogenesis landscape in E. coli using quantitative mass spectrometrySingle-molecule studies reveal that DEAD box protein DDX1 promotes oligomerization of HIV-1 Rev on the Rev response element.RNA-protein binding kinetics in an automated microfluidic reactorKinetic cooperativity in Escherichia coli 30S ribosomal subunit reconstitution reveals additional complexity in the assembly landscape.Visualizing ribosome biogenesis: parallel assembly pathways for the 30S subunitQuantitative proteomic analysis reveals a simple strategy of global resource allocation in bacteriaDiscovery of a small molecule that inhibits bacterial ribosome biogenesis.Functional interaction between ribosomal protein L6 and RbgA during ribosome assemblyMeasuring Food Intake and Nutrient Absorption in Caenorhabditis elegans.The Activation-Induced Assembly of an RNA/Protein Interactome Centered on the Splicing Factor U2AF2 Regulates Gene Expression in Human CD4 T CellsCooperativity in RNA-protein interactions: global analysis of RNA binding specificityToward a Whole-Cell Model of Ribosome Biogenesis: Kinetic Modeling of SSU Assembly.Differential Sensitivity of Target Genes to Translational Repression by miR-17~92.Biochemical characterization of the Caenorhabditis elegans FBF.CPB-1 translational regulation complex identifies conserved protein interaction hotspots.A protein.protein interaction platform involved in recruitment of GLD-3 to the FBF.fem-3 mRNA complex.UHM-ULM interactions in the RBM39-U2AF65 splicing-factor complex.Overflow metabolism in Escherichia coli results from efficient proteome allocation.FRET Characterization of Complex Conformational Changes in a Large 16S Ribosomal RNA Fragment Site-Specifically Labeled Using Unnatural Base Pairs.Stable isotope pulse-chase monitored by quantitative mass spectrometry applied to E. coli 30S ribosome assembly kinetics.Enzymatic synthesis and structural characterization of 13C, 15N-poly(ADP-ribose).A dominant negative mutant of the E. coli RNA helicase DbpA blocks assembly of the 50S ribosomal subunit.A complex assembly landscape for the 30S ribosomal subunit.Binding properties of YjeQ (RsgA), RbfA, RimM and Era to assembly intermediates of the 30S subunitFunctional domains of the 50S subunit mature late in the assembly process.DDX1 is an RNA-dependent ATPase involved in HIV-1 Rev function and virus replication.Addressing preferred specimen orientation in single-particle cryo-EM through tilting.Quantitative analysis of rRNA modifications using stable isotope labeling and mass spectrometry.Structure and dynamics of bacterial ribosome biogenesis.The effect of ribosome assembly cofactors on in vitro 30S subunit reconstitution.The acidic domain is a unique structural feature of the splicing factor SYNCRIPReally exasperating viral protein from HIV.Quantitation of the ribosomal protein autoregulatory network using mass spectrometry.Modular Assembly of the Bacterial Large Ribosomal Subunit.
P50
Q27322883-E036D4A6-6ACF-4AAE-97C2-1DE09DC989B9Q27654758-5C23F485-CEFB-4271-95D7-D24372FAA977Q27660197-AA4B6136-F82E-4E14-A085-AE5D9EDF6819Q27675545-784B2976-3829-4EA0-ABE0-3D8EACA0C6FDQ27931264-C2C1032D-82C9-4BA0-94FD-57DE2BDB69AAQ28249040-E6E17AFC-9F74-4BD2-ABBE-5D1DCDF7267AQ28264313-C37888EA-C1A8-4D0E-927A-946873C962C1Q28281206-A2E5F268-AC85-471F-B49F-F12E7B756C55Q30502694-79EEC84C-CA01-4339-B725-0B169A918B08Q33503986-3F1C04FE-1870-4E32-8220-4D81FAF6888FQ33777643-6F40928D-DCDD-47FA-A8CC-344999803AAAQ34343355-843CB440-981F-4985-8972-C2233BCBB8F3Q35174117-9C20689A-BB9A-4AE1-BD16-7E7D427279FBQ35261238-0A472EF4-267D-44C4-9276-A2C431E517B3Q35350030-A04BADCB-7C7B-46B0-9EE0-671E90690C01Q35821046-5D698798-6D4A-4D6E-8154-A7C8F467E366Q35862078-AD2301AE-86E5-46C7-B200-3F42EF665C8CQ36034599-5596CEE7-340A-4809-83C8-07326512E2C3Q36076211-955680FC-4719-42EE-A2B2-63A26D281A11Q36291392-2F46B6B3-1B64-4452-A276-733A1D9A0CC0Q36597680-B702B23F-7857-41E7-9594-3052D0EE4FA7Q36597839-C141C6A3-2569-49C0-B5E7-A7A5B23315B9Q36770424-7064D024-6808-428B-9994-BC566999FCA9Q36830680-8FC3E902-BEF5-4788-A3B5-0544575D1B9DQ36922100-58AFA1B9-6DD6-4305-9D29-6EC28B2C94DEQ37366838-D09DEBAB-926D-4393-8AD5-EB4E604428EBQ37380022-DC182803-6219-497B-B5C6-7B2ED2F27E14Q37406095-C457D71B-4EC2-48A7-9175-9FC878C993C7Q37470661-FC2DB5E7-F832-42ED-B027-52D0AE0ABD34Q37522922-926B4FC8-2924-4600-9C4A-2A264B8F5215Q37631824-38560929-8A76-4D15-B553-6CD742C120DBQ38330601-C04BC55D-BDFE-405F-99C6-27C3342E0B5FQ38696835-3303B7CB-0A98-4F78-A1A9-6E73E97B5A49Q38732764-B467E955-CA1F-4080-99D9-D74EAB8D13E5Q39110261-C9F0EA7B-55AD-4933-BD18-7C3C2B29ADB5Q40423368-466BD67A-199E-4041-9682-AEE66FB3AC67Q40798716-8737B36D-A416-4D8B-9650-988B28D73826Q41553303-397B9EE0-8CD9-40E1-BC75-35808E99880AQ41565780-42A794D6-07D9-4432-B4E5-C23812B9E010Q41599858-E6D0CD0B-19A3-4772-B01B-25D89C0B1887
P50
description
hulumtues
@sq
onderzoeker
@nl
researcher
@en
հետազոտող
@hy
name
James R Williamson
@ast
James R Williamson
@en
James R Williamson
@es
James R Williamson
@nl
James R Williamson
@sl
type
label
James R Williamson
@ast
James R Williamson
@en
James R Williamson
@es
James R Williamson
@nl
James R Williamson
@sl
altLabel
Jamie Williamson
@en
prefLabel
James R Williamson
@ast
James R Williamson
@en
James R Williamson
@es
James R Williamson
@nl
James R Williamson
@sl
P1053
B-2891-2009
P106
P21
P31
P3829
P496
0000-0002-8772-468X