Structural and Functional Analysis of the C-Terminal Domain of Nup358/RanBP2 - Test2 - elhamkhani - TriplyDB

Structural and Functional Analysis of the C-Terminal Domain of Nup358/RanBP2

Structural and Functional Analysis of the C-Terminal Domain of Nup358/RanBP2

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The Road Less Traveled: HIV's Use of Alternative Routes through Cellular Pathways HIV-1 capsid undergoes coupled binding and isomerization by the nuclear pore protein NUP358 Evidence for an evolutionary relationship between the large adaptor nucleoporin Nup192 and karyopherins Cyclophilins and nucleoporins are required for infection mediated by capsids from circulating HIV-2 primary isolates.Contribution of glutamine residues in the helix 4-5 loop to capsid-capsid interactions in simian immunodeficiency virus of macaques.A cyclophilin homology domain-independent role for Nup358 in HIV-1 infection.SJP-L-5, a novel small-molecule compound, inhibits HIV-1 infection by blocking viral DNA nuclear entry.Targeting the cyclophilin domain of Ran-binding protein 2 (Ranbp2) with novel small molecules to control the proteostasis of STAT3, hnRNPA2B1 and M-opsin.Heterogeneous susceptibility of circulating SIV isolate capsids to HIV-interacting factors Viral subversion of the nuclear pore complex.Down-modulation of nucleoporin RanBP2/Nup358 impaired chromosomal alignment and induced mitotic catastrophe.Viral and cellular requirements for the nuclear entry of retroviral preintegration nucleoprotein complexes.The Structure Inventory of the Nuclear Pore Complex.Capsid-Dependent Host Factors in HIV-1 Infection.Effects of Inner Nuclear Membrane Proteins SUN1/UNC-84A and SUN2/UNC-84B on the Early Steps of HIV-1 Infection.Keeping your armour intact: how HIV-1 evades detection by the innate immune system: HIV-1 capsid controls detection of reverse transcription products by the cytosolic DNA sensor cGAS.Cellular and molecular mechanisms of HIV-1 integration targeting.Species-specific vulnerability of RanBP2 shaped the evolution of SIV as it transmitted in African apes.Nuclear pore heterogeneity influences HIV-1 infection and the antiviral activity of MX2

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Structural and Functional Analysis of the C-Terminal Domain of Nup358/RanBP2

http://www.wikidata.org/entity/Q27676012

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2013 nî lūn-bûn

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2013 թուականի Ապրիլին հրատարակուած գիտական յօդուած

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2013 թվականի ապրիլին հրատարակված գիտական հոդված

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2013年の論文

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2013年論文

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2013年論文

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2013年論文

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2013年論文

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2013年論文

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2013年论文

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name

Structural and Functional Analysis of the C-Terminal Domain of Nup358/RanBP2

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Structural and Functional Analysis of the C-Terminal Domain of Nup358/RanBP2

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Structural and Functional Analysis of the C-Terminal Domain of Nup358/RanBP2

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Structural and Functional Analysis of the C-Terminal Domain of Nup358/RanBP2

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Structural and Functional Analysis of the C-Terminal Domain of Nup358/RanBP2

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Structural and Functional Analysis of the C-Terminal Domain of Nup358/RanBP2

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Structural and Functional Analysis of the C-Terminal Domain of Nup358/RanBP2

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Structural and Functional Analysis of the C-Terminal Domain of Nup358/RanBP2

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Structural and Functional Analysis of the C-Terminal Domain of Nup358/RanBP2

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J.JMB.2013.01.021

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Journal of Molecular Biology

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Structural and Functional Analysis of the C-Terminal Domain of Nup358/RanBP2

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André Hoelz

http://www.w3.org/2001/XMLSchema#string

Daniel H Lin

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Evelyn Stuwe

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Stephan Zimmermann

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Tobias Stuwe

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P2860

Dbp5, a DEAD-box protein required for mRNA export, is recruited to the cytoplasmic fibrils of nuclear pore complex via a conserved interaction with CAN/Nup159p

Architecture of a coat for the nuclear pore membrane

A giant nucleopore protein that binds Ran/TC4

The structure of the tetratricopeptide repeats of protein phosphatase 5: implications for TPR-mediated protein-protein interactions.

Electrostatics of nanosystems: application to microtubules and the ribosome

The translocation (6;9), associated with a specific subtype of acute myeloid leukemia, results in the fusion of two genes, dek and can, and the expression of a chimeric, leukemia-specific dek-can mRNA

PHENIX: a comprehensive Python-based system for macromolecular structure solution

Nup358 integrates nuclear envelope breakdown with kinetochore assembly

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MolProbity: all-atom contacts and structure validation for proteins and nucleic acids

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1318-29

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10.1016/J.JMB.2013.01.021

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23353830

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4226657

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