Rapid depletion of mutant eukaryotic initiation factor 5A at restrictive temperature reveals connections to actin cytoskeleton and cell cycle progression.
about
Specificity of the deoxyhypusine hydroxylase-eukaryotic translation initiation factor (eIF5A) interaction: identification of amino acid residues of the enzyme required for binding of its substrate, deoxyhypusine-containing eIF5APosttranslational synthesis of hypusine: evolutionary progression and specificity of the hypusine modificationMutational analyses of human eIF5A-1--identification of amino acid residues critical for eIF5A activity and hypusine modificationFertility and polarized cell growth depends on eIF5A for translation of polyproline-rich formins in Saccharomyces cerevisiae.Inhibition of deoxyhypusine synthase enhances islet {beta} cell function and survival in the setting of endoplasmic reticulum stress and type 2 diabetesThe unique hypusine modification of eIF5A promotes islet beta cell inflammation and dysfunction in mice.Characterization of a eukaryotic translation initiation factor 5A homolog from Tamarix androssowii involved in plant abiotic stress tolerance.eIF5A promotes translation elongation, polysome disassembly and stress granule assemblyFunctional significance of eIF5A and its hypusine modification in eukaryotesThe role of polyamines in supporting growth of mammalian cells is mediated through their requirement for translation initiation and elongationeIF5A facilitates translation termination globally and promotes the elongation of many non polyproline-specific tripeptide sequencesInhibition of HIV-1 gene expression by Ciclopirox and Deferiprone, drugs that prevent hypusination of eukaryotic initiation factor 5A.Overexpression of eukaryotic initiation factor 5A2 enhances cell motility and promotes tumor metastasis in hepatocellular carcinoma.The hypusine-containing translation factor eIF5A.Expression of eukaryotic initiation factor 5A and hypusine forming enzymes in glioblastoma patient samples: implications for new targeted therapiesGenome-wide analyses and functional classification of proline repeat-rich proteins: potential role of eIF5A in eukaryotic evolutionProduction of active recombinant eIF5A: reconstitution in E.coli of eukaryotic hypusine modification of eIF5A by its coexpression with modifying enzymes.Deoxyhypusine synthase haploinsufficiency attenuates acute cytokine signaling.Essential role of eIF5A-1 and deoxyhypusine synthase in mouse embryonic development.Loss of elongation factor P disrupts bacterial outer membrane integrityImproper organization of the actin cytoskeleton affects protein synthesis at initiationNeuronal growth and survival mediated by eIF5A, a polyamine-modified translation initiation factor.Deoxyhypusine Modification of Eukaryotic Translation Initiation Factor 5A (eIF5A) Is Essential for Trypanosoma brucei Growth and for Expression of Polyprolyl-containing ProteinsHolophytochrome-Interacting Proteins in Physcomitrella: Putative Actors in Phytochrome Cytoplasmic Signaling.The molecular basis of wound healing processes induced by lithospermi radix: a proteomics and biochemical analysis.Hypusine modification for growth is the major function of spermidine in Saccharomyces cerevisiae polyamine auxotrophs grown in limiting spermidine.Posttranslational hypusination of the eukaryotic translation initiation factor-5A regulates Fusarium graminearum virulenceGlobal quantitative proteomics reveal up-regulation of endoplasmic reticulum stress response proteins upon depletion of eIF5A in HeLa cells.The Drosophila deoxyhypusine hydroxylase homologue nero and its target eIF5A are required for cell growth and the regulation of autophagy.Mammalian polyamine metabolism and functionIdentification of the target proteins of rosiglitazone in 3T3-L1 adipocytes through proteomic analysis of cytosolic and secreted proteins.Structural modeling and mutational analysis of yeast eukaryotic translation initiation factor 5A reveal new critical residues and reinforce its involvement in protein synthesiseIF5A and EF-P: two unique translation factors are now traveling the same road.Proteomic analysis of rosiglitazone and guggulsterone treated 3T3-L1 preadipocytes.Evolutionary conserved role of eukaryotic translation factor eIF5A in the regulation of actin-nucleating formins.Regulation of gene expression by translation factor eIF5A: Hypusine-modified eIF5A enhances nonsense-mediated mRNA decay in human cells.Eukaryotic initiation factor 5A dephosphorylation is required for translational arrest in stationary phase cells.Exploring polyamines: Functions in embryo/fetal development.Modification of translation factor aIF5A from Sulfolobus solfataricus
P2860
Q24292717-9B91470E-0F46-43C3-ACA5-2F42670E2041Q24648365-BC8FAE49-2E4A-4EE0-A44C-25B8982F8EC5Q24650882-4353D28B-1E11-44FC-A67F-B3DDED6B6C1CQ27932452-ABC2D044-399B-412E-96FF-FCEF00553943Q30429251-CCABE93B-CD13-44AC-BDD2-1445E68ED665Q30435990-AAEA5113-DB80-44D1-B461-CD3C2C3AB794Q31077285-E8CB3C31-941B-44A3-B250-0042D8776E1DQ33550797-AAC75353-31FB-45E2-8E78-6C952EAFE6B6Q33691772-E965187C-262A-4E4A-86CC-1C8A870810D1Q33800179-7550E993-609E-4BCF-96D7-DCC3F95245FAQ33878081-4879D5C6-2230-40B5-82F3-E1D10CBB27F3Q34019744-983446C3-3A88-41DC-9728-900942CA69D7Q34095605-2DEEA971-1EE5-42C2-BD8F-0DBAD196428CQ34283037-B5A7D26B-2A96-42DC-B35E-5B29D9AFEF9CQ34395707-9842D451-D723-4F29-A60A-24170086C463Q34445789-0355B6B0-5CAA-4576-A651-4453129E64AEQ34571712-E6369676-82DE-4824-AFBE-123B5C5D981EQ35002343-0775E86A-8183-42B4-801E-4B80A663F101Q35563868-3EE0118C-053D-4F05-8CE9-139779B24C8EQ35668094-31DB3CD7-AC9F-4C4F-A35D-F45DB458A18AQ35676157-7023763C-8F1A-4378-BD3A-04A5F87C611FQ35676858-3AC3B94A-EB1D-4128-8AF4-2F049EE36F64Q35925923-5B1E6B27-29DF-4BCF-A95F-74433D783E95Q36034566-C08A4F53-D81B-4CF2-A40E-73906CC10048Q36277869-0EDE8687-C685-4BD8-AE77-473F9B9DAF85Q36638733-7EA59F65-EBA9-4CAD-A785-7961A0D215B1Q36819488-17FC50AB-10E9-4947-9FF0-F201A81A0D14Q36903031-708B36D0-1108-42B3-943B-09BB2F818275Q37267639-13D03C90-5AC7-43F5-9646-4FEB1EF7B260Q37365983-D992B18F-1999-43C4-B54F-5D703EBAC56AQ37599428-C7379D96-7944-4BD5-A71C-03AD6FD13004Q37612654-31E0EEA1-8725-491F-BC64-AF82FF274FACQ38176836-7CCFCCE6-4522-48C4-9F20-EB04AF93CAE6Q39218842-B971ED6C-2C25-4F90-A0D1-EAD86C6E162BQ41548085-445C3222-1080-4EE9-880B-6B98EB6E7341Q42778157-EE3F03A0-6A57-4DB4-890A-24EAE03A6B8CQ45924848-2AE81B3D-2A61-4641-823A-F5A929C8C7E6Q54951438-0525ABD4-25CF-4B7F-81F9-C936958DD4B0Q57091143-BE9B8768-A489-4402-808A-B6076FF9DCDF
P2860
Rapid depletion of mutant eukaryotic initiation factor 5A at restrictive temperature reveals connections to actin cytoskeleton and cell cycle progression.
description
2006 nî lūn-bûn
@nan
2006年の論文
@ja
2006年学术文章
@wuu
2006年学术文章
@zh-cn
2006年学术文章
@zh-hans
2006年学术文章
@zh-my
2006年学术文章
@zh-sg
2006年學術文章
@yue
2006年學術文章
@zh
2006年學術文章
@zh-hant
name
Rapid depletion of mutant euka ...... on and cell cycle progression.
@en
type
label
Rapid depletion of mutant euka ...... on and cell cycle progression.
@en
prefLabel
Rapid depletion of mutant euka ...... on and cell cycle progression.
@en
P2860
P1476
Rapid depletion of mutant euka ...... ton and cell cycle progression
@en
P2093
Ishita Chatterjee
Kuang Yu Chen
P2860
P2888
P304
P356
10.1007/S00438-005-0086-4
P577
2006-01-12T00:00:00Z