about
macroH2A1 histone variant represses rDNA transcriptionCentrosomal nucleolin is required for microtubule network organization.The histone variant macroH2A interferes with transcription factor binding and SWI/SNF nucleosome remodelingNucleolin associates with a subset of the human Ro ribonucleoprotein complexesUrokinase-induced mitogenesis is mediated by casein kinase 2 and nucleolin.The histone octamer is invisible when NF-kappaB binds to the nucleosome.Inactivation of nucleolin leads to nucleolar disruption, cell cycle arrest and defects in centrosome duplication.Structure and functions of nucleolin.Nucleosome positioning by genomic excluding-energy barriers.The NH2 tail of the novel histone variant H2BFWT exhibits properties distinct from conventional H2B with respect to the assembly of mitotic chromosomes.In vivo Study of the Histone Chaperone Activity of Nucleolin by FRAP.Dissection of the unusual structural and functional properties of the variant H2A.Bbd nucleosomeNucleolin interacts with US11 protein of herpes simplex virus 1 and is involved in its traffickingATP-dependent chromatin remodeling is required for base excision repair in conventional but not in variant H2A.Bbd nucleosomes.Expression of Nucleolin Affects Microtubule Dynamics.Expression Profiling of Ribosome Biogenesis Factors Reveals Nucleolin as a Novel Potential Marker to Predict Outcome in AML Patients3D chromatin conformation correlates with replication timing and is conserved in resting cellsThe deadenylation conferred by the 3' untranslated region of a developmentally controlled mRNA in Xenopus embryos is switched to polyadenylation by deletion of a short sequence elementNucleolin: a multiFACeTed protein.Stability of maternal mRNA in Xenopus embryos: role of transcription and translation.Functions of the histone chaperone nucleolin in diseases.AS-1411, a guanosine-rich oligonucleotide aptamer targeting nucleolin for the potential treatment of cancer, including acute myeloid leukemia.Sequence-specific RNA recognition by the Xenopus Y-box proteins. An essential role for the cold shock domain.The anti-HIV pentameric pseudopeptide HB-19 binds the C-terminal end of nucleolin and prevents anchorage of virus particles in the plasma membrane of target cells.The roles of nucleolin subcellular localization in cancer.p53 acts as a safeguard of translational control by regulating fibrillarin and rRNA methylation in cancer.Conditional knockout of nucleolin in DT40 cells reveals the functional redundancy of its RNA-binding domains.SWI/SNF remodeling and p300-dependent transcription of histone variant H2ABbd nucleosomal arrays.Transcriptional Coactivator and Chromatin Protein PC4 Is Involved in Hippocampal Neurogenesis and Spatial Memory ExtinctionIntegrated analysis of mRNA and miRNA expression in HeLa cells expressing low levels of Nucleolin.Carbon Dots-AS1411 Aptamer Nanoconjugate for Ultrasensitive Spectrofluorometric Detection of Cancer Cells.Nucleolin is required for an efficient herpes simplex virus type 1 infection.MacroH2A1.1 regulates mitochondrial respiration by limiting nuclear NAD+ consumption.Nucleolin functions in the first step of ribosomal RNA processing.Effect of genomic long-range correlations on DNA persistence length: from theory to single molecule experiments.p53 is localized to a sub-nucleolar compartment after proteasomal inhibition in an energy-dependent manner.Contributions of the RNA-binding and linker domains and RNA structure to the specificity and affinity of the nucleolin RBD12/NRE interaction.Identification of nucleic acid high-affinity binding sequences of proteins by SELEX.MacroH2A histone variants maintain nuclear organization and heterochromatin architecture.Nucleolin provides a link between RNA polymerase I transcription and pre-ribosome assembly.
P50
Q24337356-C893AAD8-BBB0-47D8-B95C-5BCA92ED5554Q27311410-CDB150FD-AA37-4A14-829C-6090E7BF84EBQ28201540-145EEE55-37AA-47DC-B5B0-52B047709FD8Q28208632-B161D068-0EAD-4150-B039-C2A86AADC5A8Q30828562-6ED80DE1-ACEB-42C0-8192-48A00CC03D8DQ33205095-011511ED-1C7C-4B70-AAA5-65542CDA7646Q33293872-9C63CE9F-3BD1-45A8-AAE6-4B49A343D451Q33536089-07906817-3203-4FC1-8192-66D07D605FC0Q33564119-C6CCB78D-098D-4B54-BEB2-18AEE9E73D8FQ34490204-B722CB97-844D-415D-AC67-155C625D903CQ34626920-A511028A-0E58-4171-B89A-73BADC2790F6Q35040018-E536EAA9-4BDA-4492-9104-8237788A4DA0Q35689672-E4CAF833-BC6B-4C9A-91F7-034CFACC81E9Q35950275-C9E69935-75EC-456D-A516-10CD503FFAADQ36053965-915F82E9-66A8-44F2-B3FD-FDD35CB85DBCQ36254052-0716F6CF-BEE9-4D66-81EB-8E29C4DCE6E4Q36341542-DDAF094C-37F5-4B57-89A6-703AB0858445Q36648008-D34431C6-4C7C-47AF-8E63-4E92F2A2189CQ36678131-403A7A49-874C-45D6-AE20-F72673209BBEQ36719853-4A2EB426-CEE1-4420-978D-39398BF6B465Q36813006-65746D41-D87E-4AFF-B656-8C4845D4CCDEQ37689055-C8D9A717-D40B-4F25-A757-41F42449D82BQ38288971-E98019BB-E3BA-4F90-A4B6-3116C95821BAQ38290769-D14BC03F-60DA-4E61-8786-E40939CF9773Q38417667-99CC8AD7-F5D2-4298-9D46-F65DF6D1E2F1Q39096715-DA4D7850-2E12-4333-9164-99815CF40448Q39959717-07EC0B62-3278-4B46-8FCD-9930642EB8BEQ40197606-80EE37D4-A565-4A43-A772-3C8BA478C67FQ41161592-C0C0349D-9990-4067-A66A-09856F399012Q41488996-A3A6756B-3921-44F7-BF1C-7B92B542DFDBQ41621278-31570824-80BF-4872-BB61-FCECA744E30AQ42090068-CA82AC8A-AB4B-4316-AAF5-0E85EC833A37Q42516548-AA2F5CF1-2C69-4A9A-B6D7-4F5010558140Q42639990-2577ADF5-3F1A-4CDF-8F4A-8DED6D60A852Q42995824-F3BFC7E5-538E-44C5-BC54-98AD23E3A479Q46228945-0BCAC261-9B85-4133-A9EC-12A31ED5D9B3Q46854392-3D532373-11DB-41A4-97C6-2FD2B89AD3D2Q47981704-17DDC533-6E11-4F14-B8CC-AB6B42039703Q48138473-CA81E476-C792-47EB-AAE6-D8A298BF348BQ48831648-83A7D55B-A1D2-41D4-9117-2622A3222063
P50
description
onderzoeker
@nl
researcher
@en
հետազոտող
@hy
name
Philippe Bouvet
@ast
Philippe Bouvet
@en
Philippe Bouvet
@es
Philippe Bouvet
@nl
Philippe Bouvet
@ro
Philippe Bouvet
@sl
type
label
Philippe Bouvet
@ast
Philippe Bouvet
@en
Philippe Bouvet
@es
Philippe Bouvet
@nl
Philippe Bouvet
@ro
Philippe Bouvet
@sl
altLabel
Bouvet P
@ro
prefLabel
Philippe Bouvet
@ast
Philippe Bouvet
@en
Philippe Bouvet
@es
Philippe Bouvet
@nl
Philippe Bouvet
@ro
Philippe Bouvet
@sl
P106
P21
P31
P496
0000-0003-4524-2233