about
Interaction of the HIV-1 intasome with transportin 3 protein (TNPO3 or TRN-SR2)LEDGF/p75 is essential for nuclear and chromosomal targeting of HIV-1 integrase in human cellsThe transcriptional co-activator LEDGF/p75 displays a dynamic scan-and-lock mechanism for chromatin tetheringFK506 binding protein 12 differentially accelerates fibril formation of wild type alpha-synuclein and its clinical mutants A30P or A53TIdentification of the LEDGF/p75 binding site in HIV-1 integraseTransient and stable knockdown of the integrase cofactor LEDGF/p75 reveals its role in the replication cycle of human immunodeficiency virusThe LEDGF/p75 integrase interaction, a novel target for anti-HIV therapyRational design of small-molecule inhibitors of the LEDGF/p75-integrase interaction and HIV replication2-Hydroxyisoquinoline-1,3(2H,4H)-diones (HIDs), novel inhibitors of HIV integrase with a high barrier to resistanceStructure of transportin SR2, a karyopherin involved in human disease, in complex with RanRetroviral integration: Site matters: Mechanisms and consequences of retroviral integration site selectionHIV-1 integrase forms stable tetramers and associates with LEDGF/p75 protein in human cellsHIV-1 integration: an interplay between HIV-1 integrase, cellular and viral proteinsIdentification and characterization of a functional nuclear localization signal in the HIV-1 integrase interactor LEDGF/p75Cellular co-factors of HIV-1 integrationNovel targets for HIV therapyA symmetric region of the HIV-1 integrase dimerization interface is essential for viral replicationmiR669a and miR669q prevent skeletal muscle differentiation in postnatal cardiac progenitorsHIV virions as nanoscopic test tubes for probing oligomerization of the integrase enzyme.Comparison of lentiviral vector titration methods.Simple criterion for selection of flavonoid compounds with anti-HIV activity.Virus evolution reveals an exclusive role for LEDGF/p75 in chromosomal tethering of HIV.Differential interaction of HIV-1 integrase and JPO2 with the C terminus of LEDGF/p75.Diffusion of myelin oligodendrocyte glycoprotein in living OLN-93 cells investigated by raster-scanning image correlation spectroscopy (RICS).Regulator of G-protein signaling 18 controls megakaryopoiesis and the cilia-mediated vertebrate mechanosensory system.Seeing genes at work in the living brain with non-invasive molecular imaging.Pharmacophore-based discovery of small-molecule inhibitors of protein-protein interactions between HIV-1 integrase and cellular cofactor LEDGF/p75.Fetal surgery is a clinical reality.Immunohistochemical detection of transgene expression in the brain using small epitope tags.4-Substituted 2-Hydroxyisoquinoline-1,3(2H,4H)-diones as a Novel Class of HIV-1 Integrase InhibitorsLEDGF hybrids efficiently retarget lentiviral integration into heterochromatin.The HIV-1 integrase mutant R263A/K264A is 2-fold defective for TRN-SR2 binding and viral nuclear import.Inhibition of human immunodeficiency virus type 1 integration by diketo derivativesHIV-1 integrase strand-transfer inhibitors: design, synthesis and molecular modeling investigation.LEDGF/p75-independent HIV-1 replication demonstrates a role for HRP-2 and remains sensitive to inhibition by LEDGINsenv chimeric virus technology for evaluating human immunodeficiency virus susceptibility to entry inhibitors.The BET family of proteins targets moloney murine leukemia virus integration near transcription start sites.Phage display-directed discovery of LEDGF/p75 binding cyclic peptide inhibitors of HIV replication.Interplay between HIV entry and transportin-SR2 dependencyLentiviral nuclear import: a complex interplay between virus and host.
P50
Q24295223-2AAD0CE0-9BD2-4769-933E-A0D60EC5D104Q24304259-52698B3B-0EC0-4B88-979A-472D52769FFAQ24304357-649C8DE3-361D-4870-90CE-30DD2D03357FQ24311758-88ABEC9D-5DD7-4709-8197-E4FD474554A6Q24321722-815A131E-4ABF-4127-A80C-87356EB23F19Q24538808-0ABABB45-3992-4B9C-A26F-BCC67E13E212Q26849265-664D7944-04FC-4598-82E5-F48B119CDA9AQ27661671-5AEEC4AE-2939-4394-8F65-F6ACC9E335ACQ27684221-22709C11-B319-4438-B638-8EA76B6B107CQ27684280-6E9773E9-4265-4C7A-9D1B-B28DCF86F3F8Q28088514-DC37A61A-6C4A-4796-95F2-3414C9CE327EQ28212168-AD91ACAC-05B8-485E-9721-C2A265CEEB12Q28248740-EA8FE5E3-3070-4A78-8976-E204F809700AQ28263591-8A96D482-80DB-4820-9875-9249249C4020Q28290761-89801B33-7BE5-4DC1-A143-397268FF0243Q28293786-D84D6C47-0F8F-4544-B5D1-CFEBD1CCF2C4Q28483813-FFEFEC12-2E65-4244-8D36-D1FDD7FD8E65Q28592363-8F73ABD3-CFA4-44A5-B4FE-604595F1A7A4Q30407372-E203A2B2-1F89-4D1B-887D-9C80C6E9D40CQ33249932-16396E03-071B-4574-923F-667CAE1C3F1EQ33267641-166B0C96-60E1-4EAF-ABE9-F5A61B1E2BA9Q33280633-BC7238D9-0E85-4BCF-9DD4-C54F1330F5CBQ33292744-59C63B43-0E83-479D-8F73-DF0798D7D0CDQ33315397-CB92F2BC-2B6D-4AAB-A39F-D1C2AF1F91A2Q33399499-3B61CFDA-C05D-4FA6-B3CF-A6E944C67205Q33466434-35DD9DFF-8CE9-49EC-B8FE-A04B7A3B4F39Q33476232-114F406B-2F07-492B-BC05-BC6CAA8B044BQ33515953-E3509B19-5E7B-4BC6-A733-7B224BF11D5FQ33532297-A0819F46-ADFA-445F-A228-6B4314C7B209Q33636046-D2EA3652-7549-4686-A896-15A332DE9E82Q33731166-3CFB5993-393F-44AE-8956-812A1B1D9EB8Q34139212-59F663B9-3421-429A-906A-17CCD70E970EQ34143182-75E8B212-EAC2-4E12-9880-A086FA7E2939Q34158634-E25BB20C-E278-4BE2-AE3A-ADEA84AF4557Q34186964-2363B3BF-A3AD-4AB0-A55C-D6EE2C4867BDQ34253200-A8118994-16CB-410D-87A3-9062987FD28CQ34342339-FB65144F-EA13-4278-9DD5-63695BAC6EEDQ34350400-9A3601B9-9C2B-47C1-B5C2-BB6411CCC02EQ34586080-696B1E2C-05B1-4794-B4C3-E6A8695CC465Q34621545-070CF2ED-090D-4E72-B478-1132966D37E2
P50
description
hulumtues
@sq
onderzoeker
@nl
researcher
@en
հետազոտող
@hy
name
Zeger Debyser
@ast
Zeger Debyser
@en
Zeger Debyser
@es
Zeger Debyser
@nl
Zeger Debyser
@sl
type
label
Zeger Debyser
@ast
Zeger Debyser
@en
Zeger Debyser
@es
Zeger Debyser
@nl
Zeger Debyser
@sl
altLabel
Zeger Marie Jacques Debyser
@en
prefLabel
Zeger Debyser
@ast
Zeger Debyser
@en
Zeger Debyser
@es
Zeger Debyser
@nl
Zeger Debyser
@sl
P1053
H-1310-2013
P106
P19
P21
P31
P3829
P3835
zeger-debyser
P496
0000-0002-3982-1565
P569
1965-06-18T00:00:00Z
2000-01-01T00:00:00Z