Structural basis for cooperativity of CRM1 export complex formation
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A structurally plastic ribonucleoprotein complex mediates post-transcriptional gene regulation in HIV-1Structural Basis of Targeting the Exportin CRM1 in CancerEvidence for an evolutionary relationship between the large adaptor nucleoporin Nup192 and karyopherinsA deep proteomics perspective on CRM1-mediated nuclear export and nucleocytoplasmic partitioning.The interaction of RNA helicase DDX3 with HIV-1 Rev-CRM1-RanGTP complex during the HIV replication cycleThe RanBP2/RanGAP1*SUMO1/Ubc9 SUMO E3 ligase is a disassembly machine for Crm1-dependent nuclear export complexesThe export receptor Crm1 forms a dimer to promote nuclear export of HIV RNACombining dehydration, construct optimization and improved data collection to solve the crystal structure of a CRM1-RanGTP-SPN1-Nup214 quaternary nuclear export complex.Atomic basis of CRM1-cargo recognition, release and inhibitionBiochemical and cellular analysis of human variants of the DYT1 dystonia protein, TorsinA/TOR1AHighly polarized C-terminal transition state of the leucine-rich repeat domain of PP32 is governed by local stability.Small GTP-binding protein Ran is regulated by posttranslational lysine acetylationThe Combination of X-Ray Crystallography and Cryo-Electron Microscopy Provides Insight into the Overall Architecture of the Dodecameric Rvb1/Rvb2 Complex.MD simulations and FRET reveal an environment-sensitive conformational plasticity of importin-βp53 SUMOylation promotes its nuclear export by facilitating its release from the nuclear export receptor CRM1Allosteric control of the exportin CRM1 unraveled by crystal structure analysis.Crystal structure of the Xpo1p nuclear export complex bound to the SxFG/PxFG repeats of the nucleoporin Nup42p.CRM1 is a cellular target of curcumin: new insights for the myriad of biological effects of an ancient spice.XPO1 in B cell hematological malignancies: from recurrent somatic mutations to targeted therapy.A non-canonical mechanism for Crm1-export cargo complex assembly.Structural characterization of the principal mRNA-export factor Mex67-Mtr2 from Chaetomium thermophilum.Interpretation of solution x-ray scattering by explicit-solvent molecular dynamics.An integrated approach for genome annotation of the eukaryotic thermophile Chaetomium thermophilumInteraction network of the ribosome assembly machinery from a eukaryotic thermophile.Two zinc-binding domains in the transporter AdcA from Streptococcus pyogenes facilitate high-affinity binding and fast transport of zinc.Exportin Crm1 is repurposed as a docking protein to generate microtubule organizing centers at the nuclear pore.
P2860
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P2860
Structural basis for cooperativity of CRM1 export complex formation
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2013 nî lūn-bûn
@nan
2013 թուականի Յունուարին հրատարակուած գիտական յօդուած
@hyw
2013 թվականի հունվարին հրատարակված գիտական հոդված
@hy
2013年の論文
@ja
2013年論文
@yue
2013年論文
@zh-hant
2013年論文
@zh-hk
2013年論文
@zh-mo
2013年論文
@zh-tw
2013年论文
@wuu
name
Structural basis for cooperativity of CRM1 export complex formation
@ast
Structural basis for cooperativity of CRM1 export complex formation
@en
Structural basis for cooperativity of CRM1 export complex formation
@nl
type
label
Structural basis for cooperativity of CRM1 export complex formation
@ast
Structural basis for cooperativity of CRM1 export complex formation
@en
Structural basis for cooperativity of CRM1 export complex formation
@nl
prefLabel
Structural basis for cooperativity of CRM1 export complex formation
@ast
Structural basis for cooperativity of CRM1 export complex formation
@en
Structural basis for cooperativity of CRM1 export complex formation
@nl
P2093
P2860
P50
P3181
P356
P1476
Structural basis for cooperativity of CRM1 export complex formation
@en
P2093
Andreas Russek
Emma Thomson
Holger Stark
P2860
P3181
P356
10.1073/PNAS.1215214110
P407
P50
P577
2013-01-15T00:00:00Z