about
sameAs
P54nrb forms a heterodimer with PSP1 that localizes to paraspeckles in an RNA-dependent manner.Nuclear speckles: a model for nuclear organellesDirected proteomic analysis of the human nucleolusThe nuclear PP1 interacting protein ZAP3 (ZAP) is a putative nucleoside kinase that complexes with SAM68, CIA, NF110/45, and HNRNP-GLive-cell imaging RNAi screen identifies PP2A-B55alpha and importin-beta1 as key mitotic exit regulators in human cellsSNEV is an evolutionarily conserved splicing factor whose oligomerization is necessary for spliceosome assemblyDistinct and overlapping sets of SUMO-1 and SUMO-2 target proteins revealed by quantitative proteomicsMass spectrometry and EST-database searching allows characterization of the multi-protein spliceosome complex3D3/lyric: a novel transmembrane protein of the endoplasmic reticulum and nuclear envelope, which is also present in the nucleolusDirect interaction between hnRNP-M and CDC5L/PLRG1 proteins affects alternative splice site choiceCharacterization of hCINAP, a novel coilin-interacting protein encoded by a transcript from the transcription factor TAFIID32 locusIdentification and functional characterization of FMN2, a regulator of the cyclin-dependent kinase inhibitor p21hLodestar/HuF2 interacts with CDC5L and is involved in pre-mRNA splicingTwo distinct arginine methyltransferases are required for biogenesis of Sm-class ribonucleoproteinsInteraction of U-box E3 ligase SNEV with PSMB4, the beta7 subunit of the 20 S proteasomeA novel function for human factor C1 (HCF-1), a host protein required for herpes simplex virus infection, in pre-mRNA splicingYeast Pescadillo is required for multiple activities during 60S ribosomal subunit synthesis.The nucleolus under stressAnalysis of human small nucleolar RNAs (snoRNA) and the development of snoRNA modulator of gene expression vectorsIdentification of peptide inhibitors of pre-mRNA splicing derived from the essential interaction domains of CDC5L and PLRG1Assembly of snRNP-containing coiled bodies is regulated in interphase and mitosis--evidence that the coiled body is a kinetic nuclear structureMutational analysis of p80 coilin indicates a functional interaction between coiled bodies and the nucleolusIn vivo analysis of NHPX reveals a novel nucleolar localization pathway involving a transient accumulation in splicing specklesLarge-scale proteomic analysis of the human spliceosomeCajal bodies and coilin--moving towards functionCondensed mitotic chromatin is accessible to transcription factors and chromatin structural proteinsNuclear processes controlled by molecular machinesNOPdb: Nucleolar Proteome DatabaseA perspective on proteomics in cell biologyMultidimensional proteomics for cell biologyPerturbation of chromatin structure globally affects localization and recruitment of splicing factorshCINAP is an atypical mammalian nuclear adenylate kinase with an ATPase motif: Structural and functional studiesThe histone chaperone Vps75 forms multiple oligomeric assemblies capable of mediating exchange between histone H3-H4 tetramers and Asf1-H3-H4 complexesProtein phosphatase 4 interacts with the Survival of Motor Neurons complex and enhances the temporal localisation of snRNPsCajal body proteins SMN and Coilin show differential dynamic behaviour in vivoA direct interaction between the carboxyl-terminal region of CDC5L and the WD40 domain of PLRG1 is essential for pre-mRNA splicingSplicing regulation at the second catalytic step by Sex-lethal involves 3' splice site recognition by SPF45In vivo identification of human small ubiquitin-like modifier polymerization sites by high accuracy mass spectrometry and an in vitro to in vivo strategyA proteomic study of SUMO-2 target proteinsPHD1 links cell-cycle progression to oxygen sensing through hydroxylation of the centrosomal protein Cep192
P50
Q22066089-F3396314-6427-499C-AE75-918338B26EA9Q22121993-7C3BF8FF-6885-469C-B2E9-D47B515E2F2DQ24292165-33A3D294-4248-40F3-A91D-50FCBCBA84DCQ24294829-C7CD09DB-E75C-4074-B463-C988C0CC6A86Q24295682-5A90185E-D47D-4107-89ED-95284D3EC86DQ24298242-D4D2F1E4-BF38-4343-9705-138F88061087Q24304372-7ADB9204-605D-41FF-BA9D-DB984281F0C1Q24311408-FE1212F7-AB35-49D6-8953-7EAA7CD5BF62Q24311579-0F1F6755-9B56-4B99-B3EF-04C608F22BD3Q24312238-C5DE0535-B200-409E-ADA7-4F413EB1E0EAQ24312861-9E04AC42-FE79-4992-A719-18E538F7B191Q24313202-C24AA8F9-8B40-4A3D-B408-8389707F1B08Q24316802-271F116D-9EEB-413A-9CE8-BCF8F5C78CFBQ24337867-A1C04507-C9EA-4DD8-B073-4B43730A9321Q24529004-8B63D7F5-9F79-499B-902E-6765588C8E54Q24539224-29FB6699-6C2C-424D-8BA3-DFCB03685A46Q24540106-FC944372-0F7E-4C49-9112-9B7427104E26Q24597470-8D63F920-45D2-4D38-9EF0-E254E9885051Q24630878-32267846-8B57-4CE9-AE12-3443305AF782Q24644221-0C2608C3-EB86-417B-87D4-9C46F4A748BCQ24651270-C06DA07D-1273-4DE3-92D8-CD277F60AC09Q24651426-BBAFCAD6-8D04-4267-9B13-98C147A6AAFAQ24671777-BB3216D1-C7B1-40C3-B120-EEED24EBFF9DQ24671785-2EA81A5C-AD1D-4CE7-9D66-3D9E9346AED7Q24672790-5D9BFEDA-C5AA-4E97-B5CD-BA8C1DB27048Q24678676-64E03B1A-3830-44E3-8C1A-9EFE8B3962FDQ24792032-6B6750CD-4C17-40B4-93BF-D048974C3B2EQ25257475-73FDCE03-57F2-40D0-A0B3-1E4145912BF6Q26823909-60DA713A-E898-423B-AF2A-EA7B6BF14301Q27008027-79D00FE6-0796-4930-8A84-BEF8A69C007CQ27313223-33477146-A3CD-4F4F-8B1D-45BF15F194AAQ27675295-51A4E7B6-D44F-4DC7-8DF0-F6F8106F4AADQ27704509-147C4D2B-E4A9-48D7-A0B4-9B734D8606EDQ28187838-844F2F0D-1E2B-4766-B0C1-5656DE5F5C3CQ28189028-77C129FE-D08B-46D5-B99F-6FE9D231DA76Q28215561-2F0B2916-28E7-4C51-86DC-E5A107EB1ECFQ28217970-B31F4C43-5D04-411C-ABDD-A47DA587E90FQ28253409-C39793BF-587A-4AD3-95DC-4AFF0B60A4BDQ28264738-7991EAED-317E-45A9-BB31-8245C912C41AQ28296254-44D4C358-9543-43E2-A7F0-CEE66ACA29A2
P50
description
biochemicus
@nl
biochemist
@en
name
Angus Lamond
@ast
Angus Lamond
@en
Angus Lamond
@es
Angus Lamond
@nl
type
label
Angus Lamond
@ast
Angus Lamond
@en
Angus Lamond
@es
Angus Lamond
@nl
altLabel
Angus I. Lamond
@en
Angus Iain Lamond
@en
prefLabel
Angus Lamond
@ast
Angus Lamond
@en
Angus Lamond
@es
Angus Lamond
@nl
P106
P1153
7005392995
P2070
angus-lamond-11781
P21
P31
P463
P496
0000-0001-6204-6045
P569
2000-01-01T00:00:00Z