about
Different quaternary structures of human RECQ1 are associated with its dual enzymatic activityA novel gene (PLU-1) containing highly conserved putative DNA/chromatin binding motifs is specifically up-regulated in breast cancerHuman PLU-1 Has transcriptional repression properties and interacts with the developmental transcription factors BF-1 and PAX9Identification and preliminary characterization of a protein motif related to the zinc fingerVCIP135, a novel essential factor for p97/p47-mediated membrane fusion, is required for Golgi and ER assembly in vivoCo-culture systems and technologies: taking synthetic biology to the next levelSolution structure and interaction surface of the C-terminal domain from p47: a major p97-cofactor involved in SNARE disassemblyThe crystal structure of murine p97/VCP at 3.6AAP endonuclease paralogues with distinct activities in DNA repair and bacterial pathogenesisDetailed structural insights into the p97-Npl4-Ufd1 interfaceStructure-based mechanism of lipoteichoic acid synthesis by Staphylococcus aureus LtaSA novel pyrazolo[1,5-a]pyrimidine is a potent inhibitor of cyclin-dependent protein kinases 1, 2, and 9, which demonstrates antitumor effects in human tumor xenografts following oral administrationStructural basis for the recognition and cleavage of abasic DNA in Neisseria meningitidisHuman skeletal-muscle aldolase: N-terminal sequence analysis of CNBr- and o-iodosobenzoic acid-cleavage fragmentsMotions and negative cooperativity between p97 domains revealed by cryo-electron microscopy and quantised elastic deformational modelIonomycin-regulated phosphorylation of the myeloid calcium-binding protein p14The ubiquitin-homology gene PIC1: characterization of mouse (Pic1) and human (UBL1) genes and pseudogenesSyntaxin 5 is a common component of the NSF- and p97-mediated reassembly pathways of Golgi cisternae from mitotic Golgi fragments in vitroThe RING finger domain: a recent example of a sequence-structure familyConformational changes in the AAA ATPase p97-p47 adaptor complexRole of promyelocytic leukemia (PML) sumolation in nuclear body formation, 11S proteasome recruitment, and As2O3-induced PML or PML/retinoic acid receptor alpha degradationStructural basis of the interaction between the AAA ATPase p97/VCP and its adaptor protein p47SteC is a Salmonella kinase required for SPI-2-dependent F-actin remodellingTwo nonconsensus sites in the Epstein-Barr virus oncoprotein EBNA3A cooperate to bind the co-repressor carboxyl-terminal-binding protein (CtBP)Structural and mechanistic insight into the Listeria monocytogenes two-enzyme lipoteichoic acid synthesis system.Genetic and crystallographic studies of the 3',5'-exonucleolytic site of DNA polymerase I.Validating a Coarse-Grained Potential Energy Function through Protein Loop Modelling.A network of enzymes involved in repair of oxidative DNA damage in Neisseria meningitidisIn vivo and in vitro characterization of σ70 constitutive promoters by real-time PCR and fluorescent measurements.The transcriptional regulator CBP has defined spatial associations within interphase nuclei.p37 is a p97 adaptor required for Golgi and ER biogenesis in interphase and at the end of mitosis.Quantitative analysis of cell nucleus organisation.Segmentation of fluorescence microscopy images for quantitative analysis of cell nuclear architecture.Substitution of Asp-210 in HAP1 (APE/Ref-1) eliminates endonuclease activity but stabilises substrate binding.Cocrystal structure of an editing complex of Klenow fragment with DNAIsolation, sequencing and expression of RED, a novel human gene encoding an acidic-basic dipeptide repeat.The BRCA1 C-terminal domain: structure and function.Mutations in a Sar1 GTPase of COPII vesicles are associated with lipid absorption disorders.Analysis of spatial point patterns in nuclear biologyValidation of an entirely in vitro approach for rapid prototyping of DNA regulatory elements for synthetic biology.
P50
Q21145897-D2358307-2716-4DB0-ABBC-465419A3104FQ22010068-09FAC3FA-D00A-487A-98FF-75148F60F25BQ24298477-21263D97-50E5-4813-A1AF-BBBB9D257A14Q24563322-14C293B8-04AE-446C-BDA0-18EE7974D29BQ24673098-D20393C6-5634-4C0C-95F5-3463FD5D40F0Q27007227-9660AE79-0B35-4758-939F-F1D8F1258E5DQ27633732-DF394561-59C2-49B1-8F95-773D6357B958Q27642642-69358DF7-D573-4AE2-BB33-94E4519BFD64Q27643887-C80A9E44-C8A0-4188-A1EE-DC23449830B3Q27644733-BDE18F0B-8C50-441F-B9BF-824D7808B5A9Q27653515-BE7FCCF7-C4A9-4D35-879F-82A761851B79Q27665906-25FFF0E6-CD49-4062-A1E6-6E56487B7EB7Q27674179-7E22CE7F-5114-4396-B699-C0748C12F470Q28118947-FE866D7F-144E-4803-8E93-A1155177501DQ28182801-27F904E8-882D-4D9D-A49D-54B82131FC00Q28239285-D10403C9-7D28-446C-B546-D46A0B4536E0Q28261815-23E1B9E4-F0D9-424D-A47C-3A75BAFB76A0Q28264896-26FB0AA3-EC42-41C0-A262-8A525D4F5B5EQ28289644-D6DDD06A-F874-4020-B492-A69A0C170C8BQ28306308-12148AB5-25C4-485F-8484-725EF1E37855Q28367104-173B2BF2-59B4-487D-9E35-B3293A7BF3C5Q28511891-5F32A517-111A-4FCB-AE90-505D5B64E2F7Q28563583-467C7A70-90DC-4B2D-9CEC-CDFB582BBF88Q28579873-17EF9A50-2E9B-46AA-B25E-DEE27BDB48B0Q30365756-115E7867-AE42-452B-96F7-FA04DB690159Q30400206-2375C7CC-8321-4FB1-9B56-6180E8D4BD03Q30432695-9C682966-DD67-4F61-AA08-2AB1A5FA97EEQ30543327-6EC9A9F8-E084-49E8-B4A7-67582BC71AFCQ31135947-F60B0459-8D49-48F8-9FB9-4561DD411F04Q33260998-4606EF5A-FE1C-4EB1-A200-6EC15183BCE7Q33265274-5B0D7E6B-E202-4882-8E06-AFD0565BD19AQ33293161-EB00D2D6-2907-4EEA-AFE3-B63BEEE5F360Q33433305-2A46D7F9-1B11-4BE3-BA45-071FC8E89393Q33615904-5B28EB2C-D992-4823-BDCB-A3836076216CQ33677240-C3A3F1BB-D4A7-4B62-B4FD-9F4E1ECEB49BQ33859696-02BBD7B6-1619-464C-8668-BB2262858622Q33914275-C283F792-1C6F-4AEE-98A0-F9083E13E056Q34190319-07CC36B8-C8A7-4B68-976C-627E625EBA94Q34277440-1BB299DA-4205-42FA-B814-193B1FD7BC7FQ34570672-8455DB1C-51A9-4824-ABA9-C08B3DF92A86
P50
description
hulumtues
@sq
onderzoeker
@nl
researcher
@en
ricercatore
@it
հետազոտող
@hy
name
Paul Freemont
@ast
Paul Freemont
@de
Paul Freemont
@en
Paul Freemont
@es
Paul Freemont
@nl
Paul Freemont
@sl
type
label
Paul Freemont
@ast
Paul Freemont
@de
Paul Freemont
@en
Paul Freemont
@es
Paul Freemont
@nl
Paul Freemont
@sl
prefLabel
Paul Freemont
@ast
Paul Freemont
@de
Paul Freemont
@en
Paul Freemont
@es
Paul Freemont
@nl
Paul Freemont
@sl
P214
P227
P244
P106
P21
P214
P227
1113207736
P244
no2011114655
P31
P496
0000-0002-5658-8486
P734
P735
P7859
lccn-no2011114655