about
Expression, purification and characterization of recombinant human choline acetyltransferase: phosphorylation of the enzyme regulates catalytic activityRepression of TFII-I-dependent transcription by nuclear exclusionNucleocytoplasmic distribution of the ovalbumin serpin PI-9 requires a nonconventional nuclear import pathway and the export factor Crm1Mitotic phosphorylation of chromosomal protein HMGN1 inhibits nuclear import and promotes interaction with 14.3.3 proteins.The evolutionarily conserved region of the U snRNA export mediator PHAX is a novel RNA-binding domain that is essential for U snRNA exportNXT1 (p15) is a crucial cellular cofactor in TAP-dependent export of intron-containing RNA in mammalian cells.Suppression of post-transcriptional gene silencing by a plant viral protein localized in the nucleusHerpes simplex virus type 1 immediate-early protein ICP27 is required for efficient incorporation of ICP0 and ICP4 into virionsSTRA13 expression and subcellular localisation in normal and tumour tissues: implications for use as a diagnostic and differentiation markerParts plus pipes: synthetic biology approaches to metabolic engineeringNuclear export of Far1p in response to pheromones requires the export receptor Msn5p/Ste21p.DNA damage response-mediated degradation of Ho endonuclease via the ubiquitin system involves its nuclear export.Subcellular localization of Aft1 transcription factor responds to iron status in Saccharomyces cerevisiae.Novel role for a Saccharomyces cerevisiae nucleoporin, Nup170p, in chromosome segregation.Starvation promotes nuclear accumulation of the hsp70 Ssa4p in yeast cells.The carrier Msn5p/Kap142p promotes nuclear export of the hsp70 Ssa4p and relocates in response to stress.Pse1/Kap121-dependent nuclear localization of the major yeast multidrug resistance (MDR) transcription factor Pdr1.Tripartite regulation of Gln3p by TOR, Ure2p, and phosphatases.Nuclear sequestration of the exchange factor Cdc24 by Far1 regulates cell polarity during yeast mating.Ubiquitin-mediated proteolysis of a short-lived regulatory protein depends on its cellular localizationPosttranslational processing of infected cell proteins 0 and 4 of herpes simplex virus 1 is sequential and reflects the subcellular compartment in which the proteins localizeRegulated nuclear localization of stress-responsive factors: how the nuclear trafficking of protein kinases and transcription factors contributes to cell survival.Role of the influenza virus M1 protein in nuclear export of viral ribonucleoproteins.Nuclear targeting signal recognition: a key control point in nuclear transport?The peptide near the C terminus regulates receptor CAR nuclear translocation induced by xenochemicals in mouse liver.Impaired DNA damage response in cells expressing an exon 11-deleted murine Brca1 variant that localizes to nuclear fociReceptor-mediated targeting of gene delivery vectors: insights from molecular mechanisms for improved vehicle design.The primary function of RNA binding by the influenza A virus NS1 protein in infected cells: Inhibiting the 2'-5' oligo (A) synthetase/RNase L pathway.Genotoxic stress and cellular stress alter the subcellular distribution of human T-cell leukemia virus type 1 tax through a CRM1-dependent mechanismNuclear localization of the meiosis-specific transcription factor Ndt80 is regulated by the pachytene checkpointThe ins and outs of STAT1 nuclear transport.The function of introns.Phosphorylation regulates the Star-PAP-PIPKIα interaction and directs specificity toward mRNA targets.The roles of multiple importins for nuclear import of murine aristaless-related homeobox protein.Predicting subcellular localization via protein motif co-occurrence.The C-terminal nuclear localization signal of the sex-determining region Y (SRY) high mobility group domain mediates nuclear import through importin beta 1.Karyopherin-mediated nuclear import of the homing endonuclease VMA1-derived endonuclease is required for self-propagation of the coding region.Systematic characterization of nuclear proteome during apoptosis: a quantitative proteomic study by differential extraction and stable isotope labeling.Cytoplasmic localization of pregnane X receptor and ligand-dependent nuclear translocation in mouse liver.Cell density regulates intracellular localization of aryl hydrocarbon receptor.
P2860
Q22254344-E8846831-A68C-4F7D-B8A1-30DC341D686BQ24291410-887E6E77-97C3-4B93-9C2D-2066B8AB26B0Q24291464-6111BAEB-3F25-4796-AC96-B268FEEE1209Q24537789-2E60507B-7CD3-48D6-807D-ECA07D72CA1EQ24539945-3ED7237A-7C80-443C-A722-4FDAF793FEAFQ24550980-D8CB6526-78DD-424C-ABAF-1D1AEE6E9891Q24630654-65CDEE09-749A-42D8-B6A5-9FA842DC357BQ24657245-0A308CE6-9A17-4FD7-AA0C-21F25CAD5DECQ24673459-3F73C668-1A58-43DE-8981-11DE66BF74BBQ27000122-4A6D8C26-4897-47F2-B7B5-DE06879B5B0EQ27930028-4AF2BC43-FA78-4510-8E77-DCB5E4721357Q27930230-E7D6C944-C88F-444C-A8B9-052D77799C9BQ27931033-FB1DCC8B-4933-4AC4-8FE7-27BC99DF6038Q27932004-DD4473C8-0241-420E-8597-405AA77A48EFQ27932157-3ECB2AA8-9D7C-4C6B-BF2B-EEE4C03C594DQ27932946-D464AABF-688A-4605-8170-E5CF1B02FD7CQ27934017-D73D2CF7-462F-4C93-8975-DB97E861C4FDQ27937548-21A35D8D-A496-46F8-8239-6012AD7D9EACQ27939119-E0327426-8A87-426E-9E59-CFE86AC3A302Q28138877-99DBE00B-E535-4683-A38D-4E6FC285C0C7Q28345181-4EC4F5E1-6CF8-4FFD-975F-23FAF352DF7EQ33771763-F795EE4F-D60D-49E5-A296-C5A4751E1908Q33797502-2D9789E5-5075-45B6-BA47-9A63F9CE68BDQ33936678-EC78369A-618A-4309-BB01-F1F684DF192DQ33967931-97E2D138-8EB7-41A5-8308-05C4EB8EEE71Q33968470-C82AD343-CA87-479A-86C5-D9EC023A9B98Q34076933-DDA363E4-F361-4C04-9F63-F23E8A26668CQ34598589-D0952A1B-6916-4E44-A0F3-482265F6AC50Q34716828-8E107A65-3C6D-4A72-8E32-A75D79ABB52DQ35011217-EC8798E2-B7C2-4013-9C02-5488D03D52A5Q35198415-75A15396-5B73-42A7-A710-CA3824BB0E79Q35886478-1B087F16-4889-485C-8DAE-D64A99A89326Q35961966-D6B249F3-47AE-43AF-AD64-8F8E5062A0FAQ37339087-6F779DD5-557C-4528-B403-4D150EBF86B1Q37593051-00F41861-84D3-4A2B-85A4-4CBBA484AD9FQ38297223-2A7F9588-EF32-4BE5-83FD-355CB7DCF623Q39740354-169CAB39-E190-4D96-ACEE-B54D84FE56C7Q40304313-777B3ED8-E5DC-4614-8F03-A8FCAD635350Q40519268-172E56CD-5B29-4977-902A-C730CA008528Q40585570-93CA5719-EAE2-482D-B7C9-C325666B23BB
P2860
description
1999 nî lūn-bûn
@nan
1999 թուականի Ապրիլին հրատարակուած գիտական յօդուած
@hyw
1999 թվականի ապրիլին հրատարակված գիտական հոդված
@hy
1999年の論文
@ja
1999年論文
@yue
1999年論文
@zh-hant
1999年論文
@zh-hk
1999年論文
@zh-mo
1999年論文
@zh-tw
1999年论文
@wuu
name
In or out? Regulating nuclear transport.
@ast
In or out? Regulating nuclear transport.
@en
type
label
In or out? Regulating nuclear transport.
@ast
In or out? Regulating nuclear transport.
@en
prefLabel
In or out? Regulating nuclear transport.
@ast
In or out? Regulating nuclear transport.
@en
P1476
In or out? Regulating nuclear transport.
@en
P2093
P304
P356
10.1016/S0955-0674(99)80032-5
P577
1999-04-01T00:00:00Z